\r\n\tFurthermore, during the preparation of high-quality dairy products, several physical, chemical, enzymatic, and microbial transformations take place. We will consciously focus on this interaction of different constituents of milk under different processing conditions for the development of the products.
",isbn:"978-1-83768-093-1",printIsbn:"978-1-83768-092-4",pdfIsbn:"978-1-83768-094-8",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,isSalesforceBook:!1,isNomenclature:!1,hash:"420e687768b56ca7b3238d77f63f1302",bookSignature:"Dr. Neelam Upadhyay",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/12173.jpg",keywords:"Protein, Fat, Lactose, Carbohydrates, Milk Processing, Milk Products, Milk Constituents, Acid Coagulated, Enzyme Treated, Heat Treated, Dairy Products, Protocols of Manufacturing",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 18th 2022",dateEndSecondStepPublish:"June 15th 2022",dateEndThirdStepPublish:"August 14th 2022",dateEndFourthStepPublish:"November 2nd 2022",dateEndFifthStepPublish:"January 1st 2023",dateConfirmationOfParticipation:null,remainingDaysToSecondStep:"21 days",secondStepPassed:!1,areRegistrationsClosed:!1,currentStepOfPublishingProcess:2,editedByType:null,kuFlag:!1,biosketch:"Dr. Upadhyay has received many awards most notable being the Young Woman Scientist Award 2020 from the Agro-Environmental Development Society and the Best Poster Award 2021 from the National Conference on Moringa Food Conclave 2021. She is a dedicated researcher in food and dairy processing and has published many research articles and papers in both national and international journals and publications.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"269538",title:"Dr.",name:"Neelam",middleName:null,surname:"Upadhyay",slug:"neelam-upadhyay",fullName:"Neelam Upadhyay",profilePictureURL:"https://mts.intechopen.com/storage/users/269538/images/system/269538.jpg",biography:"BRIEF BIODATA\n1.\tName in full: Neelam Upadhyay \n2.\tDate & Place of Birth: 29th December, 1987 at Delhi\n3.\tField of specialization: Food Technology\n4.\tPresent Position/ Designation: Scientist- Senior Scale\n5.\tAddress:\t(a)\tOfficial:\tTel. No.:0184-2259258\n\t\t\t\tE-mail: \ticar.neelam@gmail.com; neelam.upadhyay@icar.gov.in \n\t\t\t\tAddress: \tLaboratory No. 146, Dairy Technology Division, ICAR- \n\t\t\t\t\t\tNational Dairy Research Institute, Karnal \n\t\t\t(b)\tResidential: Tel. No.: +91-9255772587\n\tAddress (Permanent): 41-D, MIG DDA Flats, Shivam Enclave, Delhi-110032\n6.\t(a) Academic career and (b) professional attainments\n(a) Examination\tClass/ Percentage\tYear of Passing\tSubjects Taken\tName of University / Board\nXth \t1st/83\n(415/500)\t2003\tMathematics, Social Science, Science, English, Hindi\tK.V., Mumbai (CBSE)\nXIIth\t1st/78.2 \n(391/500)\t2005\tPhysics, Mathematics, Chemistry, Biology, English\tK.V., Delhi (CBSE)\nB.A.Sc. (Hons.)\t1st/83.43 (2044/2450)\n(3rd position)\t2008\tFood Technology\tSRCASW, University of Delhi, Delhi\nM.Sc.\t1st/8.62\n(1st position)\t2010\tFood Science & Technology\tCCS Har. Agri. Uni., Hisar, Haryana\nTitle of Research:\tDevelopment of flavoured whey-soya milk beverage\nMajor Advisor:\tDr. R. S. Dabur (Professor and Head)\nPh.D.\t1st/8.0\n(1st position)\t2014\tDairy Chemistry\tNational Dairy Research Institute, Karnal, Haryana\nTitle of Research: \tDetection of vegetable oil and animal body fat adulteration in ghee using solvent fractionation technique\nMajor Advisor:\tDr. Darshan Lal (Principal Scientist and Ex-Head)\nDistinctions during Academics\nDegree\tDistinctions\nBachelor of Applied Science (Hons.)\ti.\tY.K. Kapoor Memorial Scholarship 2006 by All India Food Processor’s Association \nii.\t3rd position in university\niii.\tReceived highest attendance award\niv.\tReceived trophy for ‘Most Disciplined Student’ for the graduation period 2005-2008\nv.\tCertificate of Honor from Honb’le Mr. Justice K.G. Balakrishnan, Chief Justice of India\nMaster of Science\ti.\t1st position in discipline and 2nd position in college\nii.\tReceived recognition for academic excellence from Jawaharlal Nehru Memorial Fund; \niii.\tQualified GATE\niv.\t2nd in inter-college yoga competition\nv.\tParticipated in various events of All India Youth Festival organized at UAS, Bangalore.\nDoctor of Philosophy\ti.\tReceived Merit Certificate for Academic Excellence in PhD course work\nii.\tReceived Certificate of Appreciation for outstanding work in the field of Dairy Processing during PhD\niii.\tQualified ICAR’s National Eligibility Test in 2010; Qualified the ICAR’s All India Examination, ICAR-SRF (PGS_-2011-2012 for award of ICAR-SRF (PGS) with 2nd rank (both in first attempt) \niv.\tQualified Agricultural Research Service Examination-2013 conducted by Agricultural Scientist Recruitment Board against the single vacancy (for UR) in the discipline of Food Technology\nv.\tStage Management Secretary of student’s council 2010-11\nvi.\tLiterary secretary of Student’s Council 2011-12\nvii.\tCompleted certificate e-course on “Publishing a Journal Manuscript - the Groundwork” directed by Springer in 2013\nviii.\tHave successfully completed certificate e-course – “Peer Review Academy” directed by Springer in 2013\nix.\tReceived a certificate on accomplishment IRIS 4-2 Information Literacy Plagiarism Quiz (on-line) in 2013 developed by Distance Learning Council of Washington, USA \n (b) Position Held\tInstitution \tPeriod of Appointment\tNature of Appointment\nScientist (Food Technology)\tICAR- National Academy of Agricultural Research Management, Hyderabad\t3 months\n(1st January, 2015 till 31st March, 2015)\tPermanent\n(Received ‘A’ grade for FOCARS)\nScientist \n(Food Technology)\tICAR- National Dairy Research Institute, Karnal\t10th March, 2015 till 31st December, 2018\n(after availing 10 days of transfer period)\tPermanent\nScientist-Senior Scale\n(Food Technology)\tICAR- National Dairy Research Institute, Karnal\t1st January, 2019 till date\tPermanent\n\n7. Special attainments in Research\n(https://scholar.google.co.in/citations?hl=en&user=PRz0Tz4AAAAJ&view_op=list_works&sortby=pubdate)\nPublications\tNumbers\tRemarks \nResearch Articles\t35\n(24 Intl, 9 National, 2 others)\tTotal Impact: 72.302\n\nBook Chapters\t7\t5 APA/CRC Press; 1 InTech Open; \n1 National\nReview Articles\t2\tTotal Impact:8.327\nTechnical Articles\t7\tCompendium of trainings, seminars, etc\nInstitute publication\t1\t\nPopular Article\t12\t6 in English; 5 in hindi\nCitations \t1066\t(as per googlescholar)\nH-index/ i10-index\t15/ 17\t\n.\n.\nJournal\tNumber of publications\tImpact factor\nResearch Articles\t35\t72.302\nInternational\t24 (15 as either corresponding or first author)\t72.302\nNational\t9 (3 as first or corresponding author)\tNAAS score\nOthers\t2\t\nReview article (International)\t2\t8.327\nInternational\t2\t8.327\n.\n \n\n\n\nRESEARCH ARTICLES\nInternational Journals \n1.\tTiwari, S., Upadhyay, N.*, Singh, A. K. (2022). Stability assessment of emulsion of carotenoids extracted from carrot bio-waste in flaxseed oil and its application in food model system. Food Bioscience, 47, 101631. https://doi.org/10.1016/j.fbio.2022.101631.\n2.\tPatil, A. T., Meena, G. S., Upadhyay, N., Khetra, Y., Singh, A. K., & Borad, S. G. (2021). Buffalo milk protein concentrate 60: Effect of skim milk heat treatment on its reconstitutability and functionality. Food Science & Technology – Lebensmittel -Wissenschaft & Tech, 148, 111638. \n3.\tUttamrao, H. J., Meena, G. S., Khetra, Y., Upadhyay, N., Singh, A. K., Arora, S., & Borad, S. G. (2022). Homogenization and sodium hydrogen phosphate induced effect on physical and rheological properties of ultrafilterd concentrated milk. Journal of Food Science and Technology, 59(3), 956-967. \n4.\tTiwari, S., Upadhyay, N.*, Malhotra, R. (2021). Three way ANOVA for emulsion of carotenoids extracted in flaxseed oil from carrot bio-waste. Waste Management, 121, 67-76. \n5.\tRanvir, S., Sharma, R., Gandhi, K., Upadhyay, N., Mann, B. (2020). Assessment of proteolysis in ultra-high temperature milk using attenuated total reflectance–Fourier transform infrared spectroscopy. International Journal of Dairy Technology. 73(2): 366-375. doi: 10.1111/1471-0307.12683. \n6.\tPonbhagavathi, T.R., Singh, A.K., Raju, P.N., Upadhyay, N. (2020). High performance liquid chromatographic (HPLC) determination of available lysine in milk protein-maize composite extrudates and its stability during storage. Journal of the Indian Chemical Society, 97(11a), 2344-2350\n7.\tTiwari, S., Upadhyay, N.*, Singh, A. K., Meena, G. S., & Arora, S. (2019). Organic solvent-free extraction of carotenoids from carrot bio-waste and its physico-chemical properties. Journal of Food Science and Technology, 1-10. 10.1007/s13197-019-03920-5\n8.\tBaria, B., Upadhyay, N.*, Singh, A. K., & Malhotra, R. K. (2019). Optimization of ‘green’extraction of carotenoids from mango pulp using split plot design and its characterization. Food Science & Technology – Lebensmittel -Wissenschaft & Tech, 104, 186-194. \n9.\tPatil, A. T., Meena, G. S., Upadhyay, N., Khetra, Y., Borad, S. G., & Singh, A. K. (2019). Effect of change in pH, heat treatment and diafiltration on properties of medium protein buffalo milk protein concentrate. Journal of Food Science and Technology, 56(3), 1462-1472. \n10.\tUttamrao, H. J., Meena, G. S., Borad, S. G., Punjaram, S. A., Khetra, Y., Upadhyay, N., & Singh, A. K. (2019). Effect of disodium phosphate and homogenization on physico-chemical and rheological properties of buffalo skim milk based ultrafiltered retentate. Journal of food science and technology, 56(5), 2426-2435. \n11.\tMeena, G.S., Dewan, A., Upadhyay, N., Barapatre, R., Kumar, N., Singh, A.K., & Rana, J.S. (2019). Fuzzy Analysis of Sensory Attributes of Gluten Free Pasta Prepared From Brown Rice, Amaranth, Flaxseed Flours and Whey Protein Concentrates. Journal of Food Science and Nutrition Research, 2(1), 022-037. DOI: 10.26502/jfsnr.2642-1100006\n12.\tPatil, A. T., Meena, G. S., Upadhyay, N.*, Khetra, Y., Borad, S., & Singh, A. K. (2018). Production and characterization of milk protein concentrates 60 (MPC60) from buffalo milk. Food Science & Technology – Lebensmittel -Wissenschaft & Tech, 91, 368-374. https://doi.org/10.1016/j.lwt.2018.01.028 \n13.\tUpadhyay, N.*, Jaiswal, P., & Jha, S. N. (2018). Application of attenuated total reflectance Fourier Transform Infrared spectroscopy (ATR–FTIR) in MIR range coupled with chemometrics for detection of pig body fat in pure ghee (heat clarified milk fat). Journal of Molecular Structure, 1153, 275-281. \n14.\tUpadhyay, N.*, Kumar A., Goyal A. and Lal, D. (2017). Complete liquification time test coupled with solvent fractionation technique to detect adulteration of foreign fats in ghee (heat-clarified milk fat). International Journal of Dairy Technology. 70(1): 110-118. doi: 10.1111/1471-0307.12323. \n15.\tUpadhyay, N.*, Goyal A., Kumar A. and Lal, D. (2017). Detection of adulteration of caprine body fat and mixture of caprine body fat and groundnut oil in bovine and buffalo ghee using Differential Scanning Calorimetry. International Journal of Dairy Technology. 70(2): 297-303. May 2017.doi:10.1111/1471-0307.12336. \n16.\tKumar, A., Upadhyay, N.*, Ghai, D.L., Kumar, A. Gandhi, K. and Sharma, V. (2016). Effect of preparation and storage of khoa on physico-chemical properties of milk fat. International Journal of Dairy Technology. 69(2): 294-300. doi: 10.1111/1471-0307.12266. \n17.\tUpadhyay, N.*, Jaiswal, P. & Jha, S.N. (2016). Detection of goat body fat adulteration in pure ghee using ATR-FTIR spectroscopy coupled with chemometric strategy. Journal of Food Science and Technology. 53 (10): 3752-3760. doi:10.1007/s13197-016-2353-2 ISSN 0022-1155\n18.\tRathi, M., Upadhyay, N.*, Dabur, R.S. and Goyal A. (2015). Formulation and physic-chemical analysis of whey –soymilk dahi. Journal of Food Science and Technology. 52(2): 968-975. doi 10.1007/s13197-013-1074-z. ISSN: 0022-1155. \n19.\tKanthale, P., Kumar, A. Upadhyay, N.*, Lal, D., Rathod G. and Sharma, V. (2015). Qualitative test for the detection of extraneous Thiocyanate in Milk. Journal of Food Science and Technology. 52(3): 1698-1704. DOI: 10.1007/s13197-013-1174-9. ISSN: 0022-1155.\n20.\tGoyal, A., Sharma, V., Upadhyay, N., Singh, A.K., Arora, S. and Ghai, D.L. (2015). Development of stable flaxseed oil emulsions as a potential delivery system of ω-3 fatty acids. Journal of Food Science and Technology. 52(7):4256-4265. \n21.\tUpadhyay, N.*, Kumar, A., Rathod, G., Goyal, A. and Lal, D. (2015). Development of a method employing reversed-phase thin-layer chromatography for establishing milk fat purity with respect to adulteration with vegetable oils. International Journal of Dairy Technology. 68(2): 207-217. doi. 10.1111/1471-0307.12178. \n22.\tGoyal, A., Siddiqui, S. Upadhyay, N., Soni, J. (2014). Effects of ultraviolet irradiation, pulsed electric field, hot water and ethanol vapours treatment on functional properties of mung bean sprouts. Journal of Food Science and Technology. 51(4): 708-714. doi 10.1007/s13197-011-0538-2. Publisher Springer. ISSN (electronic version): 0975-8402. \n23.\tKundu, H., Grewal, R.B., Goyal, A., Upadhyay, N.*, and Prakash S. (2014). Effect of incorporation of pumpkin (Cucurbita moshchata) powder and guar gum on the rheological properties of wheat flour. Journal of Food Science and Technology. 51(10):2600-2607. DOI: 10.1007/s13197-012-0777-x. ISSN: 0022-1155. \n24.\tUpadhyay, N.*, Kumar, A., Goyal, A. and Lal, D. (2014). A planar chromatographic method to detect adulteration of vegetable oils in ghee. JPC-Journal of Planar Chromatography-Modern TLC. 27 (6): 431-437. DOI: 10.1556/JPC.27.2014.6.5 \nNational Journals\n1.\tPonbhagavathi, T. R., Singh, A. K., Raju, P. N., Upadhyay, N. (2021). Textural and Sensory Characteristics of Milk Protein-Maize Flour-based Extrudates. Journal of Agricultural Engineering, 58(2), 124-136. 10.52151/jae2021581.1740\n2.\tPonbhagavathi, T.R., Singh, A.K., Raju, P.N., Upadhyay, N. (2020). Effect of Rennet Casein and Whey Protein Concentrate on Extrusion Behavior of Maize Flour. Current Journal of Applied Science and Technology. 39(33), 16-27, Article no.CJAST.57830.\n3.\tUpadhyay, N.*, Kumar, A., Lal, D., Kant, R., & Goyal, A. (2018). Detection of groundnut oil and goat body fat adulteration in ghee using principal component analysis on fatty acid profile. Indian Journal of Dairy Science. 71(5):464-472. \n4.\tUpadhyay, N.*, Kumar, A., Gandhi, K., Goyal, A. and Lal, D. (2014). Standardization of solvent fractionation technique for detection of adulteration in ghee by enriching animal body fat and vegetable oil in different fractions. Indian Journal of Dairy Science. 67 (4):323-327.\n5.\tGandhi. K., Upadhyay, N., Aghav, A.D., Sharma, V., and Lal, D. (2014). Detection of adulteration of ghee (clarified milk fat) with palmolein and sheep body fat using Reichert-Meissl (RM) value coupled with solvent fractionation technique. Indian Journal of Dairy Science. 67(5): 387-393. Received Second Best Paper Award during 44th Dairy Industry Conference organized by ICAR-NDRI, Karnal and Indian Dairy Association from 18-20, February 2016.\n6.\tAghav, A.D., Gandhi, K., Upadhyay, N., Kumar, A. and Lal, D. (2014). A study on the physico-chemical changes occurring in the milk fat during preparation of Paneer. Indian Journal of Dairy Science. 67 (5): 398-404.\n7.\tKumar, A., Upadhyay, N., Gandhi, K., Lal, D. and Sharma, V. (2013). Detection of soybean oil and buffalo depot fat in ghee using Normal-Phase Thin Layer Chromatography. Indian Journal of Dairy Science. 66(4): 294-99. ISSN: 0019-5146.\n8.\tKumar, A., Upadhyay, N., Gandhi, K., Kumar, A., Lal, D. and Sharma, V. (2013). Reverse-Phase Thin Layer Chromatography of Unsaponifiable Matter of ghee for detecting adulteration with soybean oil and buffalo depot fat. Indian Journal of Dairy Science. 66(6): 496-501. ISSN: 0019-5146.\n9.\tUpadhyay, N.*, Dabur R.S. and Rathi, M. (2011). Development and Shelf life Study of Flavoured Whey-soya milk beverage. Indian Journal of Dairy Science. 64(2): 92-101. ISSN: 0019-5146.\nOther Journals\n1.\tDewan, A., Meena, G.S., Upadhyay, N., Barapatre, R. Singh, A.K., Rana, J.S. (2017). Formulation of non-Gluten Pasta from the Optimized levels of Dairy and Non-Dairy ingredients. Madridge Journal of Food Technology. 2(2): 92–98. \n2.\tGalmessa, U., Prasad, S., Kumaresan, A., Oberoi, P. S., Baithalu, R. K., Upadhyay, N., and Dang, A. K. (2015). Modulation of Milk Fatty acid profile milk yield and composition through supplementation of omega-3 fatty acid in transition cow’s diet. Journal of Science and Sustainable Development. 3(1): 25-38. ISSN: 2070-1748\nREVIEW ARTICLES\n1.\tUpadhyay, N.*, Goyal, A. Kumar, A., Lal, D. and Singh, D. (2014). Preservation of milk and milk products for analytical purposes: A review. Food Reviews International. 30(3):203-224. DOI 10.1080/87559129.2014.913292. ISSN: 1525-6103\n2.\tGoyal, A., Sharma, V., Upadhyay, N., Gill, S. and Sihag, M. (2014). Flax and flaxseed oil: an ancient medicine & modern functional food. Journal of Food Science and Technology. 51(9): 1633-1653. DOI 10.1007/s13197-013-1247-9. ISSN: 0975-8402. \nBOOK CHAPTERS\n1.\tKumari, L., Sharma, M., & Upadhyay, N. (2021). Three-Dimensional Printing of Food Products: Printing Techniques, Novel Applications, and Printable Food Materials. Handbook of Research on Food Processing and Preservation Technologies: Volume 3: Computer-Aided Food Processing and Quality Evaluation Techniques, 55. Boca Raton, CRC Press\n2.\tUpadhyay, N.*, Harshitha, C. G., Pathak, N. K., & Sharma, R. (2021). Fourier Transform Infrared (FTIR) Spectroscopy with Chemometrics: Evaluation of Food Quality and Safety. Handbook of Research on Food Processing and Preservation Technologies: Volume 5: Emerging Techniques for Food Processing, Quality, and Safety Assurance, 271.\n3.\tNagarajappa, V., Upadhyay, N., Chawla, R., Mishra, S.K., & Nath, S. (2019). Functional Properties of Milk Proteins. In: Engineering Practices for milk products- Dairyceuticals, Novel Technologies, and Quality (pp 3-26). Apple Academic Press.\n4.\tUpadhyay, N., Kumar, M. C. T., Sharma, H., Borad, S., & Singh, A. K. (2019). Pulse Electric Field Processing of Milk and Milk Products. In: Non-thermal Processing of Foods (pp.129-144). Boca Raton, CRC Press\n5.\tUpadhyay, N., Nagaraj, V., & Singh, A. K. (2019). Advances in Fractionation of Milk Lipids: Analysis and Applications of fractions In: Recent Technologies in Dairy Science (pp. 325-344). Today and Tomorrow’s Printers and Publishers.\n6.\tNagaraj, V., Upadhyay, N.*, Nath, B. S., & Singh, A. K. (2018). Advances in Fractionation and Analysis of Milk Carbohydrates. In Technological Approaches for Novel Applications in Dairy Processing (pp. 127-147). IntechOpen. http://dx.doi.org/10.5772/intechopen.76312\n7.\tUpadhyay, N.*, Veena, N., Borad, S., & Singh, A. K. (2017). Application of Natural Antioxidants in Dairy Foods. In Natural Antioxidants (pp. 281-318). London: Apple Academic Press.\nINSTITUTE PUBLICATION\n1.\tDr. T. K. Datta, Dr. Meena Malik and Dr. Neelam Upadhyay (2017). Foundation Programme for Freshers at ICAR-NDRI 2017.\nPOPULAR AND LEAD ARTICLES\n1.\tPatil, A. T., Meena, G. S., Upadhyay, N., & Singh, A.K. (2017). Milk protein concentrates- Their Applications. Indian Dairyman, 69(9), 44-48.\n2.\tUpadhyay, N.* and R.K. Malik (2015). Nutritive Value of Milk. In: In Touch, Heinz Nutrition Foundation of India. Volume 17, Number 2&3, 2-11. (Lead Article). \n3.\tGoyal, A., Sharma, V., Upadhyay, N., Sihag, M. and Kaushik, R. (2013). High Pressure Processing and its impact on milk proteins: A Review. Research and Reviews: Journal of Dairy Science and Technology. 2 (1): 1-9. ISSN: 2319-3409.\n4.\tKumar, A., Upadhyay, N., and Naagar, S. (2012). Allergenicity of Milk Proteins, and its Management. Indian Food Industry. 31 (5&6): 45-50. ISSN: 0972-2610.\n5.\tGoyal, A. and Upadhyay, N. (2012). Nuclear Magnetic Resonance Spectroscopy in Dairy Science. Indian Food Industry. 31(1): 39-45. ISSN: 0972-2610.\n6.\tUpadhyay, N.*, Goyal, A. and Rathod, G. (2011). Microwave Spectroscopy and its applications in online processing. Indian Food Industry. 30(5&6): 63-73. ISSN: 0972-2610.\n7.\tउपाध्याय, नी*. (२०१८) भारत में कुपोषण: स्थिति और इससे निपटने के लिए रणनीतियाँ. दुग्ध—गंगा (आठवाँ अंक). अप्रैल-सितम्बर. २४-२९. \n8.\tउपाध्याय, नी.*, सिंह, आ.कु., गांगुली, स., सबिखी, ल. (२०१८) खाध्य और डेयरी क्षेत्र मे महिला उद्यमिता: कारण, समस्याए एवम उपलब्ध मंच. दुग्ध—गंगा (आठवाँ अंक). अप्रैल-सितम्बर. ६४-६९.\n9.\tउपाध्याय, नी*. (२०१९) ek¡ dk nw/k % f'k'kqvksa ds ekufld] 'kkjhfjd ,oa lkekftd mRFkku gsrq ve`r. दुग्ध—गंगा (नवाँ अंक). अकटूबर –मार्च १०२-१०४.\n10.\tउपाध्याय, नी*, fç;k ;koys (२०१९) [kk| inkFkksaZ esa —f=e ds cnys çk—frd jax o.kZd ds mi;ksx dh vko';drk दुग्ध—गंगा (दसवाँ अंक). अकटूबर –मार्च १०२-१०५.\n11.\tuhye mikè;k;, fuys'k dqekj ikBd (२०१९) d`f\"k] [kk| ,oa Ms;jh m|ksx ds Hkfo\"; eas lkSj ÅtkZ dk egRo दुग्ध—गंगा (दसवाँ अंक). अकटूबर –मार्च १२६-१३०. \n12.\tवैज्ञानिक और तकनीकी विषय के मूल हिंदी लेख जोकि गेहूँ एवम् जौ स्वर्णिमा में प्रकाशित हुए: उपाध्याय, नी*, राकेश कुमार (2020) महिला उद्यमिता के माध्यम से महिला सशक्तिकरण. गेहूँ एवम् जौ स्वर्णिमा (बारहवााँ अंक), पृष्ठ सं. 55-58; भाकृअनुप- भारतीय गेहूँ एवम् जौ अनुसंधान संस्थान, करनाल- १३२००१ द्वारा प्रकाशित\n\n8. Concepts/Processes/Products/Technologies/Patents/Others\n(i)\tConcepts \nCurrently, I am working on the integrated approach of application of green technology for the development of functional foods by utilizing under-utilized/ indigenous fruits and vegetables and/ or bio-waste. In the research projects, I am also keenly working on food chemistry and instrumental food analysis and applications of technologies/ products in dairy and non-dairy products. \nBesides this, I am working on development of functional food for addressing menopausal symptoms in osteopenic mice model. \n(ii)\tProducts/ Technologies ready for commercialization- 5\n1. Production of Milk Protein Concentrate 60 (MPC60), a high protein low lactose powder from buffalo milk (Co-Inventor)\n2. Technology for omega-3 rich mixed fat table spread (Inventor)\n3. Lipid and water soluble yellow natural colouring ingredient from bio-waste (Inventor)\n4. Technology for preparation of encapsulated flaxseed oil for its applications in foods (Inventor)\n5. Production of buffalo milk based Milk Protein Concentrate 60 (MPC60) powder with improved solubility (Co-Inventor)\n(iii) Expertise on\n1.Gas Liquid Chromatography\t5.Thin Layer Chromatography\n2.Fourier Transform Infra-red Spectroscopy\t6. Spectrophotometry\n3.Differential Scanning Calorimetry\t7.Chemical analysis including titration, distillation, etc.\n4.High Pressure Liquid Chromatography\t\n\n\n9. List of completed, on-going and submitted projects\nTitle of Project\tDuration\tRole\tFunding\tStatus\tRemarks\nEffect of storage on Baudouin test, sesamin test and RP-TLC test to detect adulteration of vanaspati and vegetable oils in ghee\t2015-2017\tCo-PI\tICAR-NDRI\n\tCompleted\tTwo research articles on RP-TLC\nPreparation and Characterization of Micro/nano delivery systems for “green” carotenoids\t2016-2019\tPI\t-Do-\t\t3 research articles+ 3 products/ technologies\nTechnology Development for the Production of Milk Protein Concentrate (MPC60) From Buffalo Milk\t2016-2019\tCo-PI\t-Do-\t\t4 research articles+ 2 products/ technologies\nTechnology of Goat Milk based Functional Beverage\t2017-2020\tCo-PI\t-Do-\t\tOne oral presentation\nTechnology for Moringa oleifera enriched cheese spread\t2020-2023\tPI\t-Do-\tOn-going\tCharacterization and incorporation of M. oleifera- pods in cheese spread is complete; shelf life study and animal trial is in progress\nDevelopment of flaxseed-rich probiotic dairy foods to address menopause symptoms\t2020-2023\tCo-PI\tDST\t\tDeveloped method -estimation of phytoestrogen; validation -in progress\nNutritional and therapeutic validation of chhachh and ghee prepared from indigenous cows by traditional method\tThree years (proposed)\tPI\tSEED Division, DST\tSubmitted \n \t\nCharacterization of Moringa oleifera leaves for functional bioactives and its application in table spread as model food system\tThree years (proposed)\tPI\tSYST, DST\t\t\nOther research work: \nDetection of adulteration of goat body fat and pig body fat in ghee using ATR-FTIR coupled with chemometrics; carried out during Professional Attachment Training at ICAR-CIPHET, Ludhiana\n\n\n\n10. Awards & honours \nName of Award\tYear\tAwarding Agency\nBest Paper Award\t2022\tGSAT (Gender Advancement for Transforming Institutions Self-Assessment Team), NDRI\nBest Poster Award\t2021\tNational Conference on Moringa Food Conclave-2021\nYoung Woman Scientist Award\t2020\tAgro Environmental Development Society during International Web-conference \nSecond Best Poster Award\t2020\tIndian Dairy Association\nCommendation certificate for Institute’s Magazine in which I am co-Editor\t2020\tTown Official Language Implementation Committee, Karnal\nLetter of Appreciation to editorial board of Institute’s magazine for receiving ICAR’s Second Prize and Trophy under Ganesh Shankar Vidyarthi Hindi Patrika Puraskar (2018-19)\t2020\tICAR- National Dairy Research Institute, Karnal\nAssociate Fellowship\t2019\tNational Academy of Dairy Science India\nFirst Prize in E-poster \t2018\tIndian Dairy Association\nOne Best oral Presentation\t2018\tHome Science Association of India\nBest Oral Presentation to my Master’s student\t2018\tICMR- National Institute of Nutrition\nBest Poster Award\t2016\tIndian Dairy Association\nSecond Best Paper Award\t2016\tIndian Dairy Association\nICAR-SRF (PGS) with 2nd rank\t2011-12\tICAR\nGATE (Engg Sciences: Food Tech; Thermodynamics)\t2010\tMHRD, GoI\nInstitution level awards\nThird prize in poster presentation \t2021\tICAR- National Dairy Research Institute, Karnal\nInstitute’s Rajbhasha Gaurav Certificate\t2020\t\nFirst prize in Scientific and Technical writing\t2019\t\nConsolation prize in Scientific and Technical writing \t2020, 2019 \t\nFirst prize in Poster Presentation- 2020, 2018, 2017\t\t\nThird prize in poster presentation\t2019\t\nFirst Prize in hindi extempore\t2017\t\nThird, first and second prize in hindi essay writing in consecutive years – 2020, 2019, 2018\t\t\n\n\n11. Teaching Assignments \n(a) Teaching: Actively involved either as course in-charge or associate \nClass\tB.Tech (DT)\tMSc/ MTech\n(FT) (till 2021)\tM.Tech (DT)\tPhD (DT/ DC/ FSQA)\nNo. of courses\t1-2\t2-3\t0-1\t2-3\nDT- Dairy Technology, DC- Dairy Chemistry, FT- Food Technology, FSQA- Food Safety Quality Assurance\n(b) Student’s guided\nDegree\tMajor Advisor \tCo-Advisory\tStatus/ Remarks\nM. Tech (DT)\t8\t2\tCompleted\n\t1\t0\tOn going\nM. Tech/ M Sc (FT/ FSN)\t2\t1\tCompleted\nM. Tech (DC)\t0\t3\tCompleted\nM. Tech (DM)\t0\t1\tCompleted\nPhD (DT)\t2 \t0\tOngoing \n\t0\t2\tCompleted\nPhD (DC)\t0\t1 \tCompleted\n\t\t1\tOn going\ni.\tThree students under my guidance as major advisor and one student as co-advisory member nominated for Best thesis award; \nii.\tOne represented NDRI at zonal-level student research convention ANVESHAN-2018\n\n12. Lectures/ member/convener of committees: \ni.\tLectures: \na.\tEntrepreneurship Development Programme (EDP) (conducted by SINED-TBI/BPD unit, ICAR-NDRI) and Online Training of Master Trainers on Fat and Oilseed processing conducted by SINED-TBI/BPD unit (ICAR-CIPHET); \nb.\tStudent’s Counselling session at SRCASW, University of Delhi, \nc.\tWorkshop conducted at DAV college, Karnal, etc\nd.\tDelivered talks at various villages on the importance of mother’s milk, nutrition in first 1000 days of an infant’s life, nutri-thali, etc\nii.\tTraining Organized: \na.\tTwenty one days Training at Centre for Advanced Faculty Training (DT Division) on ‘R & D strategies and interventions for effective agribusiness and entrepreneurship development in dairy and food sector’; \nb.\tone/two months or shorter duration trainings for students and others under BPD unit and KVK, NDRI, Karnal\nc.\tFive days training on the aspects of dairy processing to the farmers of Karnal district. \niii.\tGeneral Secretary, Staff Club, NDRI, Karnal\niv.\tMember: Student Empowerment Unit, Conferences organized from 2015 till 2018, convocation, credit seminar evaluation committees; Mera Gaon Mera Gaurav program, Farmer’s First Door programme, Swatchh Bharat Abhiyan, coordinator and mentor of different groups for organizing Foundation Program-2017, 2018, Nodal officer of Poshan Maah-2020 etc\nv.\tConvener/ Rapporteur of sessions: Conference, Dr. K. K. Iya Memorial oration; International conference of Proteomics Society of India\nvi.\tOther responsibilities: Management Representative of QMS-IS/ISO 9001:2008 and HACCP- IS 15000:2013 of Experimental Dairy (essential part of institute) until Jan 2019; one of the editors of Institute hindi magazine Dudgh Ganga which also received coveted award from ICAR (until 2019).\nvii.\tResource Generation on account of consultancy provided in field of dairy processing and by conducting sponsored trainings \nMore than ₹ 2 50 000/- (Two lakhs fifty thousand only)\nviii.\tBesides research, teaching and extension activities, I am also involved in promotion of Hindi language and have won several prizes during competitions (like extempore, essay, e-mail writing) organized by Official Language Units.\nix.\tLifetime Member of three scientific bodies: Indian Dairy Association- RE/NZ/LM/10852/HR; Association of Food Scientists & Technologists (INDIA)- AFST/LM/9-2018/KRN/2444; Lifetime member of Home Science Association of India; Membership number: HSAI-2017-HR-127-LF\nx.\tReviewed research papers of Journal of Ayurveda and Integrative Medicine (Elsevier), LWT, International Journal of Food Properties, Indian Journal of Dairy Science, Indian Journal of Natural Products and Resources, United Scientific Group, etc. \n\n\n\n\n\n\n\n\nDated: 12-04-2022\t \nNeelam Upadhyay",institutionString:"National Dairy Research Institute",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"National Dairy Research Institute",institutionURL:null,country:{name:"India"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"5",title:"Agricultural and Biological Sciences",slug:"agricultural-and-biological-sciences"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"444312",firstName:"Sara",lastName:"Tikel",middleName:null,title:"Ms.",imageUrl:"https://mts.intechopen.com/storage/users/444312/images/20015_n.jpg",email:"sara.t@intechopen.com",biography:"As an Author Service Manager, my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review to approval and revision, copyediting and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. 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1. Introduction
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EEG is a common, non-invasive and essential electrophysiological technique used to evaluate and study the brain function. EEG measures and investigates the cerebral electrical impulses by direct application of electrodes to the patient’s scalp. EEG is considered the main neurophysiological study used in Pediatric population especially in children with epilepsy [1, 2] and remains the primary test used to study and assess other clinical conditions such as parasomnia and encephalopathy associated with neurometabolic disorders and post traumatic brain injury [3]. EEG study has been used in the evaluation and assessment of organic brain pathology in patients presented with psychiatric and behavioral disorders and has been also an essential tool to confirm absence of cerebral electrical activity in patients with brain death [4, 5]. Epilepsy diagnosis is primarily made based on the clinical history of the patient and hence it is necessary not to rely completely on the EEG study to confirm the diagnosis of epilepsy [6], however EEG is the major neurophysiological test used in the classification and evaluation of seizures and epilepsy syndrome in Pediatric patients [7].
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1.1 History
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In 1875, Richard Caton an English physician reported a spontaneous electrical variation from exposed cortical brain hemispheres of rabbits and monkeys [8]. Early in the twentieth century, specifically in 1912, Vladimir Vladimirovich Pravdich-Neminsky a Russian Physiologist reported the first electrical brain impulse and evoked response in animals (dog) [8]. However, in 1924 German Neurologist and Psychiatrist Hans Berger recorded the first human EEG in a graph paper which later named an electroencephalogram (EEG) device. Berger subsequently characterized different rhythmic nature and wave patterns of the brain activity based on the different physiological state of the subjects (Figure 1) [8]. The initial description of clinical encephalography was first reported by an American neurologist Frederic Andrews Gibbs in 1935 who initially documented the classical interictal spikes associated with epilepsy and first to demonstrate the typical 3 per second spike and wave discharges associated with absence epilepsy. He also described EEG pattern during impaired consciousness level (Figure 2) [8, 9, 10].
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Figure 1.
Hans Berger, German neurologist and psychiatrist (1873–1941) [11].
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Figure 2.
The classical 3 per second spike and wave discharges was first described by Frederic Gibbs [10].
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2. Analysis and understanding the complex brain network
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The human brain consists of a complete and comprehensive network map of neuronal connections called human connectome. The normal maturation of these interconnected neurons associated with normal development of high cortical functions and motor skill consolidation. The failure of this network maturation can lead to some serious neurodevelopmental disabilities [12].
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The connectivity of this complex brain network can be classified into three types: structural connectivity, functional connectivity and effective connectivity [13]. Structural connectivity can be further subdivided into two types. First the anatomical connections that links a bundle of neural elements and second is the interregional fibers linking cortical to subcortical gray matter areas [13].
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Functional connectivity is obtained from time series analysis and reflects the statistical dependence within neural units. This time sense date can be defined by different methods which include EEG, Functional magnetic resonance imaging (fMRI) and magnetoencephalography (MEG) [13].
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Effective connectivity (EC) defines the casual effects that one neural system exerts over another. EC cannot be assessed directly so several techniques have been used to study the EC. The Dynamic Casual Modeling (DCM) is the main method for evaluating EC by analyzing data from neuroimaging studies such as Functional Magnetic Resonance Imaging (fMRI) [14].
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3. Preparing pediatric patients for EEG study
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Performing electroencephalography (EEG) in children can be quite challenging as most of these children are not cooperative during this study due to the great fear and restlessness during the EEG procedure. It is vitally important to prepare a Pediatric patient for EEG study in order to have better interpretation of the EEG results. The application of psychological technique prior to the study and the availability of the parents during the procedure can be helpful to conduct the study smoothly and minimize the need for premedication drugs. However, the behavioral and psychological techniques are not always successful in a small proportion of children. Different premedication protocols have been proposed in order to alleviate the great distress and anxiety during the study. The ideal pharmacological agents for such procedure should have a minor impact on the EEG tracing with fast onset and few side effects. Benzodiazepine is the most common premedication agent used with Midazolam being the most popular drug to induce sedation for EEG study in children [15].
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Chloralhydrate is another medication which has been used to induce sedation in the Pediatric population during different neurological studies including EEG. Chloralhydrate is a safe, cheap hypnotic non-opiate drug with no major side effects with the exception of vomiting in few cases. Chloralhydrate has been also shown to be effective and more time saving during EEG procedure [16].
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4. Technical aspects of electroencephalography
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Electroencephalography EEG, since it’s first introduction early in the 20th century, has been an essential and the most common neurophysiological device to monitor and study the electrical and functional activity of the brain [17]. EEG is a commonly used non-invasive tool to track and record the electrical field potentials captured by electrodes placed on the patient scalp. These electric field potentials created by dipoles as a result of excitation of the epical dendritic postsynaptic potential at the cortical pyramidal cells [18, 19]. The measurement and assessment of the electric field potentials can be made by attaching conductive electrodes to the human scalp. At the present time the wet electrodes are the gold standard used for EEG study [19]. A conductive paste or gel need to be used during the application of wet electrodes to minimize electrode-skin impedance in order to achieve good conductivity of the electrical impulse. The typical value of skin impedance should be kept between 5 and 20 KΩ. This skin impedance should be continuously monitored during the EEG study to ensure proper and high-quality conductivity between the skin and the EEG electrode. Performing an EEG study is a time consuming process which require an expert EEG technician or neurophysiologist in order to obtain good quality EEG results for proper interpretation and reporting as the reading and analyzing EEG data is a hard task and must be interpreted by expert neurophysiologists. The location site and description of the scalp electrodes is well recognized by the international 10–20 system (Figure 3) [19, 20].
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Figure 3.
The international 10-20 system [21].
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During the first EEG only 20–50% of patients with seizure disorder show interictal epileptiform discharges (IED) so the yield of the EEG study can be enhanced by many activation methods in order to capture the interictal epileptiform discharges which help confirming the diagnosis of epilepsy and seizure disorder [22]. The common activation procedure used in EEG laboratories includes Hyperventilation, intermittent photic stimulation (IPS), sleep and sleep deprived techniques. Hyperventilation (HV) is considered to be the first and oldest activation method used to trigger the interictal epileptiform discharges (IED) especially the one associated with absence epilepsy. HV is more effective in Pediatric population than in adult. A proper effective HV should be carried out for full 3 minutes with continuous recording and monitoring for one-minute post hyperventilation. HV is more efficient in diagnosing generalized seizures than focal epilepsy. The mechanism of HV to trigger interictal epileptiform discharges can be explained by hypocapnia induction which also manifest as background slowing or focal slowing in the EEG [22]. HV is a major provocation technique used to trigger the typical 3-Hz spike-and-wave discharge (SWD) which is characteristic for absence epilepsy as more than 90% of patients who have absence epilepsy show SWD during HV. The non-specific thalamic projection system (NSTPS) which is a part of the thalamocortical networks triggered by respiratory alkalosis and considered to be the major induction of SWD associated with absence epilepsy during the process of HV [23]. HV is an efficient and safe activation method for epilepsy and seizure disorder provocation however there are certain contraindication to perform HV during EEG study which includes patients with cardiopulmonary disease, sickle cell anemia, Moy-Moya disease, subarachnoid and intracerebral bleeding and severe carotid stenosis [22].
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A standard activation procedure used during the routine EEG study is the intermittent photic stimulation. This procedure done in a dimmed light room and application of different light frequencies between 1 and 30 Hz for 5 to 10 seconds during eye closure. The flashing light device should be kept 30 cm form the patient eyes. The response to intermittent photic stimulation (IPS) can be seen as an evoked potentials at frequencies less than 5 Hz seen posteriorly or drive response at the occipital regions or in the form of photoparoxysmal response (PPR) which was previously named photoconvulsive response. The most common types seizure disorder seen with IPS are absence epilepsy, myoclonic and tonic–clonic seizures [22].
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Among the activation techniques used during routine EEG study is the sleep and sleep deprived approach which produce the maximum yield of interictal epileptiform discharges (IED) as compared to the hyperventilation and intermittent photic stimulation procedure. The young age patients tend to have better yield of IED with each activation technique than older patients [24].
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5. Brain computer interface
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A Brain Computer Interface (BCI) which also named as Brain –machine Interface (BMI) is a computer- build network system that allow direct communication between cerebral brain activity and external recordable machine without using human muscles or peripheral nervous system. BCI utilize and analyzes the brain signals to collect information and send them to output system. BCI network consists of five phases: Signal Acquisition, Signal Magnification, Feature Extraction, Categorization and Control Interface. BCI assesses and analyze brain activity through mainly electrophysiological and hemodynamic studies. The electrophysiological study consists mainly of EEG, electrocorticography and magnetoencephalography. The hemodynamic study measures glucose uptake by an active neurons and this can be evaluated by procedures like functional magnetic resonance and infrared spectroscopy. BCIs commonly used EEG to gain details from brain activity. The design of BCI is complex due to restricted resolution and data reliability detected by the brain [25, 26].
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6. Different types of EEG study
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The American Clinical Neurophysiology Society suggest at least 20 minutes’ time duration for routine outpatient study. However, the International League against Epilepsy suggests a minimum 30 minute for routine EEG recording. Currently most routine EEG studies are done with an average time between 20 and 30 minutes. The abnormal epileptiform discharges found in 29–55% in patients with epilepsy on their first routine EEG study. Ambulatory prolonged EEG study is considered to be helpful diagnostic technique to capture interictal epileptiform discharges (IEDs) in epilepsy patients whom their first routine EEG studies reported normal. Prolonged ambulatory EEG study is considered to be superior to routine EEG in identifying IEDs specially during the natural sleep state. This procedure is also helpful to differentiate epileptic from non-epileptic psychogenic events. The duration of the ambulatory EEG study usually between 24 to 96 hours [27, 28].
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Epilepsy Monitoring Unit (EMU) is an important and crucial part of the neurophysiological work up for the diagnosis and classification of epilepsy and evaluation of psychogenic non-epileptic seizures (PNES). EMU is also essential for patients with intractable epilepsy resistant to antiepileptic medications and for evaluating candidates for possible epilepsy surgery [29].
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EMU is strongly recommended for children with unclear history of paroxysmal episodes in order to differentiate between epileptic and non-epileptic events as this can be quite challenging in pediatric population. EMU is also important in evaluating different types of epilepsy syndromes in children. One of the vital advantages of the video-EEG telemetry is the monitoring and recording the ictal events especially in patients with partial epilepsy. EMU is a highly selective study should be done for carefully selected patients as this is an expensive and time consuming procedure [30]. The process of monitoring and recording video-EEG telemetry can range from 24 hours to 7 days. In some situation antiepileptic drugs need to be tapered in order to induce seizure activity for better evaluation of seizure semiology and localization of the epileptogenic zone [31].
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The Amplitude-Integrated EEG (aEEG) is another continuous electrophysiological modality used in both term and preterm newborns in the neonatal intensive care units (NICUs). Since it’s first introduction late in 1980s. the aEEG considered to be the gold standard to monitor and assess neonatal brain background activity, diagnose and manage newborn seizure disorders and help in selecting newborns who might be benefit from cooling therapy. The aEEG also plays a major role in predicting the neurodevelopmental outcomes for term and preterm newborn babies. The application and recording of the aEEG is done by using two or four scalp electrodes applied to C3, P3, C4 and P4 positions of the newborn head according to the international 10–20 system. aEEG is a safe procedure which has a major limitation as it covers only small area of the head surface and hence focal epileptiform activity cannot be monitored during the aEEG recording [32, 33, 34].
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EEG is considered to be the commonest procedure used for intraoperative neurophysiological and cerebral perfusion monitoring [35]. EEG is also considered to be the gold standard modality for evaluating patients for possible epilepsy surgery to localize and define different epileptogenic foci. EEG also plays an important role in understanding the nature and pathophysiology of epilepsy and presurgical evaluation of functional cortical mapping. However, routine EEG monitoring might not be always sufficient to evaluate certain types of epilepsy such as non-lesional temporal lobe epilepsy which necessitate the need of more interventional procedure such as the invasive electroencephalography (iEEG) [36, 37].
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7. Basic EEG interpretation
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A proper and detailed history taking is more reliable and important in diagnosing epilepsy and seizure disorders than EEG study. A solid and classical history of seizure even with the presence of normal EEG finding make the diagnosis of epilepsy is more likely as the sensitivity of single routine EEG study is only about 50% in diagnosing seizure disorders [38].
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A single EEG study provides extensive data for interpretation. The main initial description of the EEG recording includes the amplitude, frequency and wave morphology. Hans Berger described two characteristic EEG wave frequencies during awake state: The alpha rhythm (8–12 Hz) which is more prominent in the arousable stage with eye closure and beta rhythm (13–30 Hz) commonly seen with mind focus state. In most people eye closure will result in frequency transfer from beta to alpha rhythms. Subsequent wave frequencies were identified the theta rhythm (4–7 Hz) and the delta rhythm (0.5–3 Hz) which are predominant during sleep in adults, and the gamma rhythm (> 30 Hz) which is associated with memory, information processing and cognitive skill (Figure 4) [39].
\n
Figure 4.
Different EEG waveforms [39].
\n
It is vitally important to ensure proper education and gain enough experience to read and interpret EEG recording in order to avoid misdiagnosis of epilepsy and to provide better care to the patient. It is also essential to appreciate the common benign variations of normal EEG study [40, 41].
\n
A common normal patterns seen in EEG study which can be falsely interpreted as abnormal epileptiform discharges include multifocal sharp waves and spikes, generalized slowing with hyperventilation, hypnagogic hypersynchrony and most commonly is the background alteration at the temporal area (Figures 5 and 6) [38].
\n
Figure 5.
Hypnagogic hypersynchrony. A normal EEG variant [42].
\n
Figure 6.
High amplitude rhythmic slowing with hyperventilation [43].
\n
Over interpretation of normal EEG tracing is the main factor for misdiagnosis of epilepsy and seizure disorders. Improper neurophysiological training and inadequate experience is the major reason for over interpretation of normal EEG study. Conservative EEG interpretation and avoiding biased history are strongly recommended by all epileptologists [38].
\n
\n
\n
8. Common clinical applications of EEG in children
\n
Although the diagnosis of epilepsy is primarily made by clinical history, EEG remains an essential investigational tool to differentiate between epileptic and non-epileptic events, it’s also important in the classification of different types of epilepsy and epilepsy syndromes [44, 45, 46]. Frequent classical epileptiform abnormalities seen in Pediatric population are hypsarrhythmia associated with infantile spasm, 3 Hz spike and wave discharges in absence epilepsy and burst suppression (Figures 7 and 8) [46].
\n
Figure 7.
EEG tracing showing bilateral, diffuse, high amplitude slow waves seen in hypsarrhythmia [47].
\n
Figure 8.
EEG with burst suppression [48].
\n
According to the American Academy of Neurology and Child Neurology Society, EEG is recommended in children presented with their first attack of unprovoked seizure [49]. EEG is indicated in children with atypical febrile convulsion or prolonged febrile seizure and it is an essential investigational study in patients with newly diagnosed epilepsy and in classification of common childhood epilepsy syndromes such as centrotemporal spikes associated with benign rolandic epilepsy and Panayiotopoulos syndrome (idiopathic childhood epilepsy). EEG is also important in recording continuous spike-waves during slow-wave sleep (CSWS) in epileptic encephalopathies (Figures 9 and 10) [50].
\n
Figure 9.
EEG showing left centrotemporal epileptiform spike and wave discharges in patients with benign rolandic epilepsy [51].
\n
Figure 10.
Occipital spike and wave discharges seen in panayiotopoulos syndrome [52].
\n
Pediatric patients diagnosed with autistic spectrum disorder (ASD) with positive history of epilepsy and abnormal findings in the neurological examination, EEG study is indicated as a part of their screening tests. EEG is also recommended in monitoring antiepileptic medication in patients with confirmed diagnosis of epilepsy [50].
\n
The background EEG monitoring has been also used in children with traumatic brain injury which is helpful in evaluating prognosis in these patients [50, 53]. EEG study with poor reactivity, prolonged discontinuity and burst suppression associated with poor prognosis, whereas EEG with good reactivity and normal sleep rhythm favor a good prognosis [53]. A prolonged EEG recording is also essential in children admitted to the PICU (Pediatric Intensive Care Unit) with suspected non-convulsive seizures (NCS). It has been also important in monitoring Pediatric patients underwent surgery for congenital cardiac anomalies as they are at risk to have seizure post-surgery [53].
\n
Viral encephalitis is an inflammatory infectious neurological disease that affects the central nervous system (CNS) which triggers an immune response by the viral antigen causing damage to the brain parenchyma and associated with electrical disturbance of the brain activity [54]. Viral encephalitis is common in children with Herpes Simplex Virus (HSV) being the commonest agent for encephalitis in Pediatric population [54, 55]. EEG study is considered to be a part in the investigational work up in patients with viral encephalitis [56]. Patients with Herpes Simplex Encephalitis (HSE) found to have significant EEG changes in the early stage of the diagnosis. Unilateral Periodic Lateralized Epileptiform Discharges (PLED) is considered to be the most typical EEG finding which correlate with diagnosis of HSE [57] and found to have a good outcome as compared to bilateral periodic lateralized epileptiform discharges which associated with unfavorable prognosis (Figure 11) [58].
\n
Figure 11.
Periodic lateralized epileptiform discharges (PLED) over the right central-temporal head regions seen in HSE [59].
\n
EEG study can be also used as an ancillary test to support the diagnosis of brain death. Although positive diagnosis of brain death can be made by two separate settings of clinical examination, The American Neurological Association strongly suggest the use of EEG study to confirm the diagnosis of brain death. Hypothermia and hypotension should be avoided when applying EEG for brain death assessment [60]. Isoelectric encephalogram is confirmed when 30 minutes of EEG recording reveals complete absence of cerebral activity with sensitivity over 2 μV/mm in the absence of electrolyte disturbance and sedative medications (Figure 12) [61].
\n
Figure 12.
Isoelectric EEG. No cerebral brain activity with sensitivity over 2 μV/mm [62].
\n
\n
\n
9. Conclusion
\n
EEG is considered to be save non-invasive procedure since its first application early in the 20th century. This procedure is done by trained EEG technicians and it should be interpreted by Neurologist or expert Neurophysiologists in order to obtain a high quality report to reach a proper diagnosis and provide optimal management to the patient.
\n
Performing EEG study in children can be a difficult task because of the great fear and anxiety in this age group patients, so its vitally important to properly prepare these patients to minimize EEG artifacts for better interpretation of the EEG report.
\n
EEG is an essential neurophysiological study especially in Pediatric patients to differentiate epileptic form and non-epileptic events as the differential diagnosis for paroxysmal episodes in children is wide and varies according to certain age group.
\n
Although the diagnosis of brain death is primarily made on clinical basis, EEG remains an important ancillary test for diagnostic confirmation of brain death.
\n
\n
Conflict of interest
The author declares no conflict of interest.
\n
Funding
\n
None.
\n
Abbreviations
EEG
electroencephalography
fMRI
functional magnetic resonance imaging
MEG
magnetoencephalography
IED
interictal epileptiform discharges
IPS
intermittent photic stimulation
BCI
brain computer interface
EMU
epilepsy monitoring unit
aEEG
amplitude-integrated EEG
ASD
autistic Spectrum disorder
\n',keywords:"electroencephalography, epilepsy, neuropsychiatric, ancillary, electrophysiological, pediatric, encephalopathy",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/73674.pdf",chapterXML:"https://mts.intechopen.com/source/xml/73674.xml",downloadPdfUrl:"/chapter/pdf-download/73674",previewPdfUrl:"/chapter/pdf-preview/73674",totalDownloads:541,totalViews:0,totalCrossrefCites:0,totalDimensionsCites:2,totalAltmetricsMentions:0,impactScore:1,impactScorePercentile:52,impactScoreQuartile:3,hasAltmetrics:0,dateSubmitted:"July 15th 2020",dateReviewed:"September 29th 2020",datePrePublished:"October 29th 2020",datePublished:"April 7th 2021",dateFinished:"October 19th 2020",readingETA:"0",abstract:"Electroencephalography (EEG) is a non-invasive neurophysiological study that monitors electrical activity of the brain. EEG is an essential investigational tool to analyze and record electrical impulses of the brain and considered to be the gold standard electrophysiological test which can be used to help diagnose epilepsy. EEG can also be used to diagnose and evaluate other conditions such as sleep disorders, neurometabolic diseases with encephalopathy and neuropsychiatric disorders. It is also an essential ancillary test in other conditions such as brain death assessment. However, it is essential not to entirely rely on EEG for an absolute diagnosis of epilepsy as the main indication of EEG in general and in Pediatric age group in particular is to categorize different types of seizure and epilepsy syndromes for further evaluation and management.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/73674",risUrl:"/chapter/ris/73674",book:{id:"9629",slug:"electroencephalography-from-basic-research-to-clinical-applications"},signatures:"Raafat Hammad Seroor Jadah",authors:[{id:"314907",title:"Dr.",name:"Raafat Hammad Seroor",middleName:null,surname:"Jadah",fullName:"Raafat Hammad Seroor Jadah",slug:"raafat-hammad-seroor-jadah",email:"nader212@hotmail.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_1_2",title:"1.1 History",level:"2"},{id:"sec_3",title:"2. Analysis and understanding the complex brain network",level:"1"},{id:"sec_4",title:"3. Preparing pediatric patients for EEG study",level:"1"},{id:"sec_5",title:"4. Technical aspects of electroencephalography",level:"1"},{id:"sec_6",title:"5. Brain computer interface",level:"1"},{id:"sec_7",title:"6. Different types of EEG study",level:"1"},{id:"sec_8",title:"7. Basic EEG interpretation",level:"1"},{id:"sec_9",title:"8. Common clinical applications of EEG in children",level:"1"},{id:"sec_10",title:"9. Conclusion",level:"1"},{id:"sec_14",title:"Conflict of interest",level:"1"},{id:"sec_11",title:"Funding",level:"1"},{id:"sec_14",title:"Abbreviations",level:"1"}],chapterReferences:[{id:"B1",body:'\nGregory A Light, Lisa E Williams, Falk Minow, Joyce Sprock, Anthony Rissling, Richard Sharp, Neal R Swerdlow, David L Braff. Electroencephalography (EEG) and event-related potentials (ERPs) with human particpants. Curr protoc Nuerosci.2010 Jul; Chapter 6: unit6.25.1-24. 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DOI: 10.1016/j.neucli.2014.11.005.\n'},{id:"B62",body:'\nMatthew A Koenig, Peter W Kaplan. Brain Death. Handb Clin Neurol .2019; 161: 89-102. DOI: 10.1016/B978-0-444-64142-7.00042-4.\n'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"Raafat Hammad Seroor Jadah",address:"nader212@hotmail.com",affiliation:'
Department of Paediatric, Bahrain Defence Force Hospital, Royal Medical Services, Kingdom of Bahrain
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1. Introduction
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Erythrocytes contain the hemoglobin (Hb) protein that carries oxygen from the lungs to the rest of the body. During the development, the hemoglobin structure gradually changes. The fetal hemoglobin HbF (α2γ2) is a major hemoglobin in the human fetus during the last 7 months of development in the uterus. The adult hemoglobin contains two components, the major hemoglobin, Hb A (α2β2), and the minor hemoglobin, Hb A2 (α2δ2) [1, 2]. The composition of heme and heterodimeric forms of globin protein, α-globin and β-globin, is encoded by the α gene and the β gene, which are in chromosome 16 and 11, respectively. The inherited hemoglobin disorder is a common monogenic disease that could be identified into two main groups, the hemoglobinopathy which is abnormal structure hemoglobin variants and the recessive inheritance allele which is the defective hemoglobin production, the thalassemia syndromes [3, 4]. More than 200 point mutations and 80 different deletions within the β-globin-encoding gene are related to inherited hemoglobin disorder of β-thalassemia that represent in population worldwide [5]. In Southeast Asia, especially Thailand, hemoglobin E (HbE) thalassemia accounts for about one-half of all cases, with the highest frequencies observed. Approximately 35,000 patients are living with β-thalassemia syndrome in Thailand, 7% with a β-thalassemia trait, and 17% with an HbE trait within a population of 65 millions of Thai people [6].
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Pathophysiology of β-thalassemia/HbE is strongly associated with the excess of unmatched α-globin chain and mutation of hemoglobin variants which are apparently observed inside the bone marrow, as well as peripheral tissues including the liver and spleen [7, 8]. These phenomena are believed to be the etiological factors of ineffective erythropoiesis. However, these conditions are found in certain hereditary blood disorders and are often associated with β-thalassemia/HbE [9]. This disease is characterized by apoptosis of erythroid precursors and inhibited erythroid differentiation and maturation [10]. These lead to an insufficient number of red blood cells. Consequently, a decreased oxygen-carrying capacity of the blood is tightly linked to the compensatory mechanism of the elevated erythropoietin (EPO) production that later causes the deleterious effects [11].
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Erythropoiesis is a complex orchestrated process involving self-renewal, proliferation, differentiation, and mobilization of HSCs that gives rise to erythroid lineages [12]. These processes are governed by heterogeneous regulatory factors, cytokines, signaling molecules, and various cellular interactions. Erythropoiesis is extensively studied in mice model, although there are several species-specific differences of erythroid differentiation [13]. Many in vitro studies focused on cultures of human hematopoietic stem cells (HSCs), and erythroid progenitor cells have been elucidated the pathogenesis of β-thalassemia/HbE [14, 15, 16, 17, 18, 19, 20]. However, studying of homeostatic imbalance inside the bone marrow regarding ineffective erythropoiesis is challenged by limited human samples.
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The emergence of “OMIC” approach, especially proteomics, has accelerated our understanding of pathobiology of the β-thalassemia/HbE disease, which will have a substantial impact in medicine. Technological advances of proteomic analysis tools, for example, mass spectrometry, allow high sensitivity, reduced sample requirement, increased throughput, and dissect posttranslational modifications of limited clinical specimens [21, 22]. The use of these technologies continues to expand substantially, particularly to meet the need for better diagnostics and to shorten timeline of effective therapy development. Interestingly, in combination with optimized ex vivo HSCs to erythroid culture or freshly isolated samples, MS-based proteomic approach has revealed a more comprehensive understanding of ineffective erythropoiesis in β-thalassemia/HbE.
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2. Pathophysiology of β-thalassemia/HbE
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β-Thalassemia is characterized by insufficient β-globin chain production due to decreased production (β+) or null production (β0) of β-globin chain, which is the main component of adult hemoglobin. This condition leads to variable clinical symptoms. β-Thalassemia major is characterized by severe anemia. Individuals with homozygous β-thalassemia may develop β-thalassemia major or β-thalassemia intermedia. The concentration of hemoglobin could distinguish types of β-thalassemia [3, 4, 23, 24]. β-Thalassemia major has low levels of hemoglobin of 3–4 g/dL, whereas the mild-to-moderate anemia show hemoglobin concentration at 7–10 g/dL. Clinical complications of β-thalassemia major include growth retardation, pallor, jaundice, poor musculature, genu valgum, hepatosplenomegaly, and leg ulcers. A severe anemia is accompanied by ineffective erythropoiesis with bone expansion and extramedullary erythropoiesis in the liver, spleen, and other sites such as paravertebral masses. These lead to the skeletal changes including deformities in the long bones of the legs and typical craniofacial changes [3, 25]. Typical treatment for β-thalassemia major is primarily blood transfusion which causes another complication, posttransfusional iron overload. In some cases, chelation therapy could be implemented.
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β-Thalassemia/HbE has extremely diverse clinical phenotypes because of various genetic lesions of the gene affecting different impaired globin chain synthesis and abnormal forms of hemoglobin variants [3, 4]. The genetic mutation of the β-globin-encoding gene at codon 26 (GAG to AAG) contributes to the activation of cryptic splice site that cause abnormal mRNA processing. The βE-chain are produced at a reduced level resulting in a mild β-thalassemic phenotype [26]. Each year in Thailand, approximately 3000 infants are born with β-thalassemia/HbE either a mild β-thalassemia or a severe transfusion-requiring β-thalassemia major. HbE/β-thalassemia patients have remarkable variation in terms of severity reflecting the heterogeneity of the β-thalassemic mutations in the HbE gene and other modulation factors. Newborns carrying HbE/β-thalassemia mutations are usually asymptomatic because they rely on the HbF hemoglobin rather than the HbE. After 6–12 month of birth, anemia with abdominal enlargement due to hepatosplenomegaly could be observed [27, 28, 29, 30]. Although the defect in β-globin production could be explained by the mutations or the absence of the β-globin gene or other modification factors, the variable severity of β-thalassemia is also involved in an imbalance of β- and α-chains, particularly in maturing erythroid cells [31]. The accumulating unmatched free α-globin chain is unstable and could precipitate in the erythroid precursors in the bone marrow as well as in peripheral blood. A severe accumulation of the α-chain forms hemichromes which cause uncontrollable oxidative damages in erythroid precursor and erythroid cells. The hemichromes can generate reactive oxygen species (ROS) that potentially damage important proteins, DNA, and other cellular components and trigger signaling cascades of programmed cell death [10, 32, 33, 34, 35, 36]. The destruction of erythroid cells is an onset of dramatic amelioration cycles inside the bone marrow and peripheral organ due to the ineffective erythropoiesis in β-thalassemia/HbE patients.
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3. Ineffective erythropoiesis
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Erythropoiesis is a progressive orchestrated process involving heterogeneous regulatory factors such as cytokines, signaling molecules, and various cellular interactions which play important roles in self-renewal, proliferation, differentiation, and mobilization of HSCs to become erythroid lineage [13, 37]. The ineffective erythropoiesis is the hallmark pathophysiological condition having seen in β-thalassemia/HbE. In β-thalassemia/HbE, the oxidative damage caused by the accumulation of hemichromes and the generation of ROS in red blood cells (RBCs) and erythroid progenitors are an etiologic factor perturbing the homeostasis of erythropoiesis [8]. In vitro and in vivo studies of mice model and ex vivo studies of human HSCs and erythroid progenitors have elucidated the molecular pathogenesis of the ineffective erythropoiesis of β-thalassemia. The excess of α-chain is believed to accelerate apoptotic cell death in erythroid precursors [10], while the inhibited processes involving differentiation of erythroid maturation have been observed during polychromatophilic stage [34]. Both detrimental processes lead to an insufficient number of RBCs and decreased oxygen-carrying capacity of blood and ultimately cause hypoxia condition. The lack of mature RBCs stimulates a compensatory mechanism of erythropoiesis that triggers the overproduction of EPO from the kidney. The increased EPO could induce erythropoiesis in the bone marrow by inducing proliferation of HSCs and erythroid progenitors. The EPO also triggers survival mechanism under stress condition and supports differentiation of mature RBCs. However, the dramatic oxidative damages inside the bone marrow are the key factor that generates a homeostatic imbalance of erythropoiesis. This is linked to an erythroid expansion leading to extramedullary hematopoiesis [37]. Dysregulated hemoglobin synthesis and hemolysis are major factors of the ineffective erythropoiesis and determine the severity of the disease [38]. Another clinical complication is an iron overload in severe patients that are treated by regular blood transfusions which is not required for thalassemia intermedia patients. Blood transfused patients usually develop elevated body iron load due to an increased gastrointestinal iron absorption. Consequently, the accumulation of iron also causes oxidative stress because they produce highly reactive hydroxyl radicals that could not be naturally degraded by enzymatic reaction. Altogether, the accumulation of unstable free α-globin, heme, and iron all contributes to destruction of cellular compartments in the bone marrow of β-thalassemia patients [7, 39, 40]. Previous studies attempted to identify molecular and cellular mechanisms associated with the ineffective erythropoiesis in β-thalassemia patients. However, the bone marrow is tightly linked to other vital organs and complicates the deciphering of ineffective erythropoiesis of β-thalassemia.
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Although there are well-established genetic manipulation techniques in model organisms such as mice and zebrafish and extensive enrichment methods of specific cell stage of hematopoietic progenitors make functional study of hematopoiesis possible, many components of the process act differently in human due to the evolutionary distance of hematopoietic genes, transcription, and epigenetic regulations [13]. Ex vivo human model using primary cell cultures of HSCs obtained from the peripheral blood, cord blood, and bone marrow or fetal liver of donor remains a gold standard of erythropoiesis study. Notably, involving multifactors could be determined in very proliferated and differentiated cells in different culture systems [41]. However, in expansion and differentiation steps, primary cell culture system may not provide sufficient amounts of analytes for some downstream techniques such as Western blot. While most techniques have their limitation to systematically analyze the bone marrow, its microenvironment and other neighboring cellular interactions during pathological conditions of ineffective erythropoiesis of β-thalassemia/HbE. Alternative approaches could be implemented to analyze the limited isolated primary cells of thalassemia patients and potentially other dyserythropoietic diseases. Here, we discuss advantages of OMIC approaches especially proteomics for studying molecular pathogenesis of β-thalassemia/HbE.
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4. Clinical proteomics of β-thalassemia/HbE
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One of the goals of proteomic study is to characterize the flow of information through complex protein networks in a particular disease model, where the changes of proteins in the whole proteome can be identified in the pathophysiological conditions at different disease developmental stages. Comparative proteome profiling of patient and healthy subjects may help to provide new clinical conceptualization for systemic pathophysiology including root causes, biomarkers, and applicable treatment regimes. Clinical proteomics is an exciting sub-discipline of proteomics that will integrate the application of proteomic technology to identify problems at the bedside [42]. Conventional analysis methods, such as Western blot, are difficult because of limited amounts of clinical samples in many disease models. In the field of biomedical research, nonetheless, the cause of the disease could not be thoroughly explained due to the complexity of various molecular and cellular pathways in many types of cells and tissues. Therefore, elucidation of protein network alteration in clinical samples is an advantage strategy for deciphering interaction between proteins and their expression profiles which are related to cellular physiology [43]. Despite high-throughput genomic technology can identify differential gene expression in disease samples, proteome alterations still occur in many ways not predictable from genomic analysis. A better understanding of these alterations will have a substantial impact in medicine [44, 45]. Moreover, clinical proteomic is a very promising tool for identifying various posttranslational modifications, such as phosphorylation and glycosylation. The recent advance proteomic analysis provides high sensitivity, reduced sample requirement, increased throughput, and is able to uncover various posttranslational modifications which are available for disease-related applications [46]. The use of these technologies will likely expand substantially, particularly to meet the need for better diagnostics and to shorten the path for developing effective therapy.
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Proteomic analysis of blood samples has become an interesting method in hematological studies. The extremely rich spectrum of proteins in blood and blood components serves various cellular activities including coagulation, transport, immune system and cell signaling, as well as by-products of cellular damage and proteins from other tissues [47]. Whereas, the identification of originality related hematopoiesis from HSCs in some clinical respects such as leukemia and anemia are very challenging [48]. Since the key candidate proteins belonging to any disease status are in the low-abundance level, to overcome these problems, protein samples are fractionated to allow effective detection and quantification by mass spectrometry (MS) [21]. Different protein separation methods influence MS results. Many previous clinical proteomic studies of β-thalassemia/HbE employed gel-based technique and shotgun proteomic to analyze posttranslational modifications of the thalassemic proteome. Most comparative protein profiles of β-thalassemia/HbE between patients with normal subjects from various types of clinical specimens including plasma serum, platelets, platelet-free plasma-derived microvesicles, and circulating extracellular vesicles (EVs) have been reported [49, 50]. Interestingly, a few studies have directly investigated proteomic changes inside the bone marrow or isolated the HSCs of thalassemic samples, where are the major site of erythropoiesis and could identify relevant proteins in the ineffective erythropoiesis. HSCs were isolated from bone marrow cells and peripheral blood using antibody specific to CD34, the transmembrane glycoprotein. Both peripheral blood- and bone marrow-derived CD34+/HSCs showed differentially regulated proteomes during ineffective erythropoiesis in β-thalassemia/HbE [15, 18]. Recently reports have revealed the nature of the bone marrow plasma proteome and the roles of microenvironment in the bone marrow niche and linked to the dyserythropoiesis of β-thalassemia/HbE [51].
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4.1 Gel-based technique
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Gel-based proteome analysis method involves a separation of proteins using either one-dimensional (1-D) or two-dimensional electrophoresis (2-DE). Since 2-DE separates proteins by their isoelectric points and by molecular weight, it is a standard choice for protein separation. After the proteins are resolved, the gel is visualized by staining with visible dyes, such as Coomassie Blue or silver nitrate or with fluorescent dyes such as Sypro Ruby. The gel is imaged and analyzed by software to identify protein spot that show altered intensity. Selected protein spots are excised and subjected to in-gel digestion typically by trypsin, resulting in peptides that can be further analyzed by mass spectrometry (MS) or tandem mass spectrometry (MS/MS). One of the drawbacks of the conventional 2-DE is gel-to-gel variability. For many proteomic studies, multiple gels of many samples have to be run, and spots at a certain location have to match between gels to reduce variability, but this still cannot fully eliminate the problem. Apart from variability, 2-DE also has poor reproducibility and provides relatively lower sensitivity. To circumvent these problems, two-dimensional difference gel electrophoresis (2-DIGE) has been developed. By labeling different samples with different fluorescent dyes and separating them in the same gel, 2-DIGE enables better comparison of up to three protein samples [22, 52, 53]. However, there are some proteins cannot be resolved on 2-D gels due to their physicochemical properties. These include highly basic or acidic proteins, proteins with extremely high or low molecular weight, and membrane proteins that are inherently insoluble in gel matrices [21].
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Two-dimensional gel electrophoresis (2-DE) coupled with mass spectrometry or tandem mass spectrometry (MS and MS/MS) has been used for the investigation of β-thalassemic proteomes. The majority of differential expressed proteins between β-thalassemia patients and normal clinical specimens have been identified and characterized their functions in different metabolic processes in response to inorganic substances using an online DAVID gene ontological analysis [54]. Several enzymes in metabolic processes are usually abundant and easily found on the 2-DE, whereas low-abundant proteins involve in gene regulation and signal transduction cascades are difficult to detect. However, 1D-SDS-PAGE may be used as a standard separation method for complex protein mixtures based on their molecular weight prior MS analysis. Gel-enhanced liquid chromatography coupled with tandem mass spectrometry (GeLC-MS/MS) is a direct intensive methodology that provides high coverage of the proteome. GeLC-MS/MS is applicable to reduce gel-to-gel variation and inconsistency of protein spots in a 2-DE and to increase sensitivity of detection of low-abundant proteins [55]. Current study of bone marrow plasma proteome profile using GeLC-MS/MS technique has reported differentially expressed proteins between patients and normal donors and showed that many of which have functions in intracellular signaling and metabolic pathways associated with ineffective erythropoiesis [51]. GeLC-MS/MS has been used to analyze the CD34+/HSCs’ thalassemic proteome during the in vitro differentiation of erythroid lineages and identified dysregulation of many signaling protein of differentiation processes in thalassemia patients (unpublished data).
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4.2 LC-based technique
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LC-based technique or shotgun proteomic analysis is an advanced and widely used approach for protein identification and characterization of sequence variants and posttranslational modifications [56]. Shotgun proteomics is considered as a bottom-up approach, by which short peptides are prepared by proteolytic digestion, usually by trypsin, and subjected to protein sequencing via tandem mass spectrometry (MS/MS) and automated protein database searching. After proteolytic digestion by trypsin, short peptide mixture is fractionated by hydrophobicity and charged using multidimensional liquid chromatography. Eluted peptides from the column are then ionized and separated by m/z in the first stage of MS/MS. Fragmentation is initiated when the peptide ions undergo collision-induced dissociation (CID) within inert gas. The ionized fragments are then separated by m/z in the second stage of MS/MS, and the corresponding peptide ions generate fragment ion spectral fingerprints for peptide identification. The process continues until all peptides are eluted from the chromatography column. Peptide identification is accomplished by comparing the fragmentation spectra derived from peptide fragmentation with theoretical MS/MS spectra based on in silico protein database. Protein inference is achieved by allocating peptide sequences to proteins [56, 57, 58]. Shotgun proteomics has a relatively high throughput compared to other MS-based proteomic technologies. This gel-free approach involves proteolytic digestion of proteins into short peptides (1–3 kDa) as they are easier to fragment than intact proteins simplifying MS/MS sequencing [21].
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Erythropoiesis involves posttranslational modifications of proteins associated with cell-cell communications and cell interactions inside the bone marrow. Phosphorylation is mediated by kinase enzymes which have different target specificities. Different phosphorylation sites on the same protein usually serve different protein activities. Shotgun proteomic strategy becomes the widely used for studying phosphoproteomes. The CD34+/HSCs’ isolation from the bone marrow is a good representative model for elucidation signaling proteins using phosphoproteomic analysis comparing with thalassemia patient and normal donor. The workflow includes an enrichment of phosphoproteins among patient and donor samples using immobilized metal affinity chromatography (IMAC), followed by ESI-LC-MS/MS. This approach detects upregulation of signaling proteins of apoptosis pathway linked to ineffective erythropoiesis in β-thalassemic CD34+/HSCs [15].
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5. Alteration of proteome profiles in hematopoietic stem cells (HSCs) derived from β-thalassemia/HbE patients
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The hallmarks of stem cells include self-renewal and differentiation ability to give rise different types of mature cells. Stem cell biology is an important field of biomedical science and holds promise in clinical applications. The hematopoietic stem cells (HSCs) are multipotent progenitor cells located in adult bone marrow, responsible for blood cell production. Multipotency or multi-lineage differentiation potential of the HSCs defines as the capacity to give rise to several differentiated cell types including myeloid progenitor cells, erythroid-megakaryocyte progenitor cells, and lymphoid progenitor cells [13]. In addition, the proliferation and differentiation of HSCs into the erythroid lineage are the acquisition of functional and structural properties associated with erythrocyte physiology [37, 59]. The cell isolation technique of the primitive HSCs’ population expressing specific cell surface markers, CD34 and CD133, is a gold standard method widely used for investigating of erythropoiesis in vivo [60]. Using antibody-conjugated magnetic particles is the first step after the isolation of mononuclear cells from bone marrow aspirate or from peripheral blood. Optimized culture condition for in vivo erythroid development requires defined medium supplemented with cytokines, such as erythropoietin (EPO), to modulate erythroid cell development from HSCs/CD34+. Erythroid differentiation is a multistep process starting when a subset of HSCs/CD34+ commits to differentiate to the megakaryocyte-erythrocyte progenitors (MEPs). The differentiation of MEPs into the most immature erythroid progenitors, namely, a burst-forming unit erythroid (BFU-Es), involves a number of transcriptional regulators. The BFU-Es generate colony-forming units-erythroid cells (CFU-Es) which strictly depends on the erythropoietin to induce differentiation via erythropoietin receptor (EPOR). Subsequently, the CFU-Es develop into proerythroblasts (the first erythroid precursors) through the basophilic, the polychromatophilic, and the orthochromatic stages. During this differentiation process, the hemoglobin synthesis, cellular content modification, and nuclear condensation gradually take place, followed by the enucleation step generating reticulocytes which are immature red blood cells (RBCs). In addition to the macrophage-induced cellular death pathways, autophagy is the key mechanism of the biconcave formation of mature RBCs [13]. Conversely, in β-thalassemia/HbE patients, the ineffective erythropoiesis has dramatic effects in the erythroid lineage development, resulting in hyperproliferation, increased apoptosis, and inhibited terminal erythroid differentiation. To study the pathogenesis of β-thalassemia/HbE, our strategies include the isolation of CD34+/HSCs, in vitro erythroid differentiation, and bone marrow plasma enrichment followed by the MS-based analysis to comprehensively understand the early molecular basis of β-thalassemia/HbE. This method revealed the bona fide proteome alterations of ineffective erythropoiesis from CD34+/HSCs, the dynamic differentiation of CD34+/HSCs in the erythroid lineage, and bone marrow microenvironment (Figure 1A). The bioinformatic approach has also been applied to analyze integrated thalassemia-specific proteomes in a range of patient specimens. We report interesting imbalance signaling landscapes which may contribute to ineffective erythropoiesis found in β-thalassemia/HbE patients.
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Figure 1.
Diagram showed the sample preparation from bone marrow-derived CD34+/HSCs and bone marrow plasma prior to MS-based proteomic approaches. The three sources of proteomes for investigating ineffective erythropoiesis include CD34+/HSCs’ phosphoproteome, dynamic differential proteome during erythroid development, and bone marrow plasma proteome (A). Schematic diagram of identified proteins and proposed signaling pathway for ineffective erythropoiesis in β-thalassemia/HbE (B).
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5.1 Metabolic enzymes
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Leecharoenkiat et al. reported the first differential 2-DE proteome between β0-thalassemia/HbE and control erythroblasts isolated from peripheral CD34+/HSCs. Many differentially expressed proteins identified in this study were constituents of the glycolysis and TCA pathways and were correlated with the degree of erythroid expansion [18]. Our investigation of bone marrow microenvironment proteome has shown increased level of ATP citrate lyase (ACLY) in β-thalassemia patients. ACLY is primarily responsible for synthesis of acetyl CoA in TCA cycle. Consequentially, hyperproliferation of erythroblast during ineffective erythropoiesis might be related with the increase of ACLY indicating a high metabolic flux governed by acetyl-CoA production. ACLY can support sufficient energy to drive the TCA cycle and mitochondrial oxidative phosphorylation [51]. Therefore, the comparative proteome profiling of peripheral blood CD34+/HSCs and bone marrow plasma proteome indicated the similar target metabolic protein biomarkers associated with ineffective erythropoiesis.
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5.2 Oxidative damage and antioxidant proteins
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An imbalance between oxidative damage and antioxidant enzymes is associated with cellular pathology inside HSCs and differentiated erythroid precursors in β-thalassemia patients. Comparative proteome analysis during differentiation of CD34+/HSCs through erythroid lineage for 7 days in β-thalassemia patients compared with normal showed many proteins differentially expressed; these include superoxide dismutase (SOD), peroxiredoxin 6 (PXD6), and peroxiredoxin 2 (PXD2). An increased level of PXD2 was found in differentiated thalassemic CD34+/HSCs at day 0 through day 7 (unpublished data). In addition, PXD2 has function in stress response in the protective system during stress erythropoiesis in thalassemic mice model [61]. PXD2 is an abundant protein mostly identified in many proteomic studies from various clinical specimens of β-thalassemia [50, 54, 62]. An increased oxidative damage from alpha excess and iron overload thus triggers the cellular defensive mechanism, including antioxidative responses. Nevertheless, thalassemic stem cells could not prolong survival pathways to prevent cell death. Moreover, comparative bone marrow plasma proteome from patients and normal showed a decreased level of an antioxidant secretory or extracellular exosomal protein, namely, apolipoprotein D (ApoD), in patients who have an impairment of bone marrow microenvironment to dyserythropoietic condition [51].
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5.3 Heat shock protein
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Recent studies have suggested that the molecular chaperone or the heat shock protein maintains cellular homeostasis during erythropoiesis. Regulated by the GATA-1, the master transcriptional machinery of erythropoiesis, the heat shock protein 70 (HSP70) plays an important role in protecting from caspase-3-mediated GATA-1 degradation [63]. Conversely, in β-thalassemia major, the alleviated free alpha globin exacerbates the oxidative damage inside erythroblast which induces the translocation of heat shock protein 70 from the nucleus to cytoplasm, leaving GATA1 unprotected [63]. The expression of heat shock protein 70 in patient group was dramatically significantly increased from day 0 to day 7, suggesting it as a contributing factor of ineffective erythropoiesis (unpublished data). Furthermore, the heat shock protein 90 that has a similar expression pattern as heat shock protein 70 and has been identified over expression from platelet-free plasma-derived microparticles proteome in β-thalassemia/HbE patients [50].
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5.4 Apoptotic pathway
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Erythroid progenitors undergoing terminal erythroid differentiation to generate sufficient erythroblasts and reticulocytes are impaired during ineffective erythropoiesis of β-thalassemia involving the acceleration of apoptotic cell death in erythroid precursors. The apoptotic proteins of intrinsic and extrinsic pathways have been firstly identified from the phosphoproteomic analysis of β-thalassemia CD34+/HSCs. This might explain why even freshly isolated HSCs of β-thalassemia bone marrow showed less survival compared to HSCs from normal donors. Phosphoproteome analysis of β-thalassemia HSCs identified an increased expression of cytochrome C (CytC), apoptosis-inducing factor (AIF), and caspase 6 (CASP6) [15]. Moreover, extrinsic apoptotic pathway plays important roles during erythroid differentiation rather than the progenitor or HSCs’ stages. The analysis of thalassemia HSCs’ phosphoproteome during in vitro differentiation to erythroid lineage of CD34+/HSCs revealed very high expression of death receptor proteins, such as TNF receptor-associated factor 2 (TRAF2), at day 7 but was undetectable at day 0 (unpublished data), as well as the downregulations of tumor necrosis factor ligand superfamily member 6 (FASL) and tumor necrosis factor receptor superfamily member 12A [15]. Thus, we propose that the imbalance of death signaling pathway could have a predominant effect during erythroid proliferation and differentiation in β-thalassemia. However, few studies explained how ROS and oxidative stress are related to an ineffective erythropoiesis. It remains to investigate whether ROS signaling could provoke apoptotic pathway of ineffective erythropoiesis.
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5.5 The AKT/FOXO3/14-3-3 axis
\n
After the finding of the imbalance cell death protein in CD34+/HSCs’ proteomes from both fresh isolated and erythroid differentiated condition in vitro. The 14-3-3 protein was found upregulated in HSCs of β-thalassemia/HbE patients. This identified a molecular linkage between both survival and death signaling pathways [15]. An elevated ROS level in β-thalassemia erythroid cells plays an important role in the activation of AKT, potentially resulting in the repression of FOXO3 activity and reducing the cellular responses to oxidative stress. Nevertheless, AKT-mediated FOXO3 phosphorylation at Ser253 could not maintain the activation of FOXO3 activity to induce downstream gene expression of stress responses in β-thalassemia/HbE [14]. This leads to a premature apoptosis of erythroid cells. In this circumstance, activation of AKT and the translocation of FOXO3 from the nucleus to cytoplasm involve the activation of 14-3-3 which binds to FOXO3 and induces FOXO3 degradation by ubiquitination/proteasome pathway [64]. In addition to the signaling crosstalk of AKT and 14-3-3 modulated FOXO3 function, c-Jun N-terminal kinase (JNK) pathway and other posttranslational modifications, especially acetylation, promote FOXO3 transcriptional activity inside the nucleus [64, 65]. However, the regulation of 14-3-3 among AKT and JNK signaling-mediated FOXO3 function through involving imbalance of death and survival signaling during ineffective erythropoiesis remains to be investigated (Figure 1B).
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6. Conclusions
\n
Proteomic analysis by MS has become an efficient tool for investigating pathophysiology of β-thalassemia/HbE overcoming limiting factors of stem cell samples, especially hematopoietic stem cells (HSCs). Integrated proteome profiling using shotgun-based and gel-based proteomic analyses of clinical bone marrow or peripheral blood samples shed light on the molecular mechanisms on ineffective erythropoiesis in β-thalassemia. Better understanding of these molecular mechanisms will help the development of novel treatment of the disease.
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Acknowledgments
\n
The authors gratefully acknowledge the financial support provided by Thammasat University under the TU New Research Scholar, Contract No. 1/2015, and National Research Council of Thailand, Contract Nos. 3949 and 43000.
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Conflict of interest
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The authors have no potential conflict of interest to disclose.
\n
\n',keywords:"β-thalassemia/HbE, hematopoietic stem cells (HSCs), ineffective erythropoiesis and proteomics",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/66612.pdf",chapterXML:"https://mts.intechopen.com/source/xml/66612.xml",downloadPdfUrl:"/chapter/pdf-download/66612",previewPdfUrl:"/chapter/pdf-preview/66612",totalDownloads:1005,totalViews:0,totalCrossrefCites:2,dateSubmitted:"November 5th 2018",dateReviewed:"March 15th 2019",datePrePublished:"April 19th 2019",datePublished:"September 25th 2019",dateFinished:"April 8th 2019",readingETA:"0",abstract:"β-Thalassemia/HbE is highly prevalent in Southeast Asian countries, especially Thailand. It is a severe hereditary anemia disease involving ineffective erythropoiesis in the bone marrow and peripheral tissues. The excess of alpha globin and iron overload contribute to elevated oxidative damages leading to a premature cell death of erythroid cells and a diminished terminal differentiation of reticulocytes. Although proteomic approach would gain a comprehensive picture of the complex pathophysiology of human bone marrow and hematopoietic stem cells (HSCs), obtaining sufficient clinical specimens remains an important issue. The employment of mass spectrometry (MS)-based proteomic profiling could overcome these constrains and provide useful insights into the cellular constituents and microenvironment in bone marrow milieu. In this chapter, we summarize the comparative proteomic studies analyzing CD34+/HSCs and bone marrow niche proteins. Under ineffective erythropoiesis, in-depth analyses of various proteome profiles revealed many of which have putative functions. Importantly, dysregulated cell death and survival signaling pathways could explain the deleterious pathogenesis of β-thalassemia/HbE.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/66612",risUrl:"/chapter/ris/66612",signatures:"Saranyoo Ponnikorn, Siripath Peter Kong, Sasipim Thitivirachawat, Chanawin Tanjasiri, Sumalee Tungpradabkul and Suradej Hongeng",book:{id:"6914",type:"book",title:"Proteomics Technologies and Applications",subtitle:null,fullTitle:"Proteomics Technologies and Applications",slug:"proteomics-technologies-and-applications",publishedDate:"September 25th 2019",bookSignature:"Ibrokhim Y. Abdurakhmonov",coverURL:"https://cdn.intechopen.com/books/images_new/6914.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",isbn:"978-1-78984-611-9",printIsbn:"978-1-78984-610-2",pdfIsbn:"978-1-83962-221-2",isAvailableForWebshopOrdering:!0,editors:[{id:"213344",title:"Prof.",name:"Ibrokhim Y.",middleName:null,surname:"Abdurakhmonov",slug:"ibrokhim-y.-abdurakhmonov",fullName:"Ibrokhim Y. Abdurakhmonov"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:null,sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Pathophysiology of β-thalassemia/HbE",level:"1"},{id:"sec_3",title:"3. Ineffective erythropoiesis",level:"1"},{id:"sec_4",title:"4. Clinical proteomics of β-thalassemia/HbE",level:"1"},{id:"sec_4_2",title:"4.1 Gel-based technique",level:"2"},{id:"sec_5_2",title:"4.2 LC-based technique",level:"2"},{id:"sec_7",title:"5. Alteration of proteome profiles in hematopoietic stem cells (HSCs) derived from β-thalassemia/HbE patients",level:"1"},{id:"sec_7_2",title:"5.1 Metabolic enzymes",level:"2"},{id:"sec_8_2",title:"5.2 Oxidative damage and antioxidant proteins",level:"2"},{id:"sec_9_2",title:"5.3 Heat shock protein",level:"2"},{id:"sec_10_2",title:"5.4 Apoptotic pathway",level:"2"},{id:"sec_11_2",title:"5.5 The AKT/FOXO3/14-3-3 axis",level:"2"},{id:"sec_13",title:"6. Conclusions",level:"1"},{id:"sec_14",title:"Acknowledgments",level:"1"},{id:"sec_14",title:"Conflict of interest",level:"1"}],chapterReferences:[{id:"B1",body:'Thein SL, Menzel S, Lathrop M, Garner C. Control of fetal hemoglobin: New insights emerging from genomics and clinical implications. Human Molecular Genetics. 2009;18(R2):R216-R223'},{id:"B2",body:'Thein SL. Genetic modifiers of the beta-haemoglobinopathies. British Journal of Haematology. 2008;141(3):357-366'},{id:"B3",body:'Fucharoen S, Weatherall DJ. The hemoglobin E thalassemias. 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The "O" class: Crafting clinical care with FoxO transcription factors. Advances in Experimental Medicine and Biology. 2009;665:242-260'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"Saranyoo Ponnikorn",address:"saranyoo@tu.ac.th",affiliation:'
Chulabhorn International College of Medicine, Thammasat University Rangsit Campus, Thailand
'},{corresp:null,contributorFullName:"Siripath Peter Kong",address:null,affiliation:'
Chulabhorn International College of Medicine, Thammasat University Rangsit Campus, Thailand
Department of Pediatrics, Faculty of Medicine Ramathibodi Hospital, Mahidol University, Thailand
'}],corrections:null},book:{id:"6914",type:"book",title:"Proteomics Technologies and Applications",subtitle:null,fullTitle:"Proteomics Technologies and Applications",slug:"proteomics-technologies-and-applications",publishedDate:"September 25th 2019",bookSignature:"Ibrokhim Y. Abdurakhmonov",coverURL:"https://cdn.intechopen.com/books/images_new/6914.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",isbn:"978-1-78984-611-9",printIsbn:"978-1-78984-610-2",pdfIsbn:"978-1-83962-221-2",isAvailableForWebshopOrdering:!0,editors:[{id:"213344",title:"Prof.",name:"Ibrokhim Y.",middleName:null,surname:"Abdurakhmonov",slug:"ibrokhim-y.-abdurakhmonov",fullName:"Ibrokhim Y. Abdurakhmonov"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}}},profile:{item:{id:"176024",title:"Dr.",name:"Mustafa",middleName:null,surname:"Can",email:"mustafacan80@yahoo.com",fullName:"Mustafa Can",slug:"mustafa-can",position:null,biography:null,institutionString:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",totalCites:0,totalChapterViews:"0",outsideEditionCount:0,totalAuthoredChapters:"4",totalEditedBooks:"0",personalWebsiteURL:null,twitterURL:null,linkedinURL:null,institution:null},booksEdited:[],chaptersAuthored:[{id:"48439",title:"The Role of Hydrophobicity in the Development of Aluminum and Copper Alloys for Industrial Applications",slug:"the-role-of-hydrophobicity-in-the-development-of-aluminum-and-copper-alloys-for-industrial-applicati",abstract:"Improvement of corrosion resistance is a main challenge in surface and corrosion engineering. Water is a main part of corrosion mechanism, and the omission of this part will be helpful. By mimicking from nature, superhydrophobicity is a helpful method to decrease corrosion and water presence on the surface. Superhydrophobic surface and coating is a new type of coating that extension in recent decade and increase application of this area every day. These type of coatings are using on widespread of applications such as solar panels, displays, windows, paints and fabrics to obtain water-proof, anticorrosive, self-cleaning and stain-resistant surfaces. Many different studies have been reported to produce superhydrophobic surfaces from many diverse materials (polymers, metals and other inorganic materials, composites, textiles, paper). In this chapter, recent developments in the application of superhydrophobic coatings for corrosion protection of aluminum and copper alloys will be discussed. This chapter includes new production methods, theoretical works, and the limitations of superhydrophobic coatings.",signatures:"Amir Farzaneh, Zaki Ahmad, Mustafa Can, Salih Okur, Omer\nMermer and Ali Kemal Havare",authors:[{id:"52898",title:"Prof.",name:"Zaki",surname:"Ahmad",fullName:"Zaki Ahmad",slug:"zaki-ahmad",email:"zakiahmad100@gmail.com"},{id:"52910",title:"Dr.",name:"Amir",surname:"Farzaneh",fullName:"Amir Farzaneh",slug:"amir-farzaneh",email:"amir.frz@gmail.com"},{id:"173467",title:"Prof.",name:"Salih",surname:"Okur",fullName:"Salih Okur",slug:"salih-okur",email:"salih.okur@gmail.com"},{id:"176024",title:"Dr.",name:"Mustafa",surname:"Can",fullName:"Mustafa Can",slug:"mustafa-can",email:"mustafacan80@yahoo.com"},{id:"176155",title:"Dr.",name:"Omer",surname:"Mermer",fullName:"Omer Mermer",slug:"omer-mermer",email:"omermermer@gmail.com"},{id:"176463",title:"Dr.",name:"Ali",surname:"Kemal Havare",fullName:"Ali Kemal Havare",slug:"ali-kemal-havare",email:"alikemal.havare@toros.edu.tr"}],book:{id:"4590",title:"New Trends in Alloy Development, Characterization and Application",slug:"new-trends-in-alloy-development-characterization-and-application",productType:{id:"1",title:"Edited Volume"}}},{id:"52374",title:"Recent Progresses in Perovskite Solar Cells",slug:"recent-progresses-in-perovskite-solar-cells",abstract:"Perovskite solar cell (PSC) can be regarded as a continuation of dye sensitized solar cell (DSSC) in terms of the sensitization phenomena that occurred in the functioning molecules. In 2012, a breakthrough propose has been made for the sensitization of PSCs, in which a solid‐state structure is offered as an equivalent sensitizer used in DSSC. The power conversion efficiency (PCE) of those solid‐state cells reached about twofold of its initial value during the past several years. Immediately after, the researchers followed this propose worldwide. They have introduced an improved efficiency of as much as 20%, which was originally started from its initial value of 4%, just in 4 years. Thus, the new concept, solid perovskite molecules, has eliminated the need for the liquid electrolyte in DSSC while still carrying the advantages of organic solar cells (OSCs). Therefore, the distinctive material of PSC—the organometallic halide molecules (also known as OMH or organic‐inorganic trihalides)—inclined an unexpected reputation for solar cell (SC) researches. Hence, it seems that we will witness a new age for solar conversion devices depending on the recent hopeful progresses on PSCs. The high rate of photovoltaic (PV) conversion capacity in PSC is generally expressed by the basic properties possessed by the organic‐inorganic perovskite crystal, such as better optical properties and well diffused charges along huge distances during the charge transport. In addition, a low temperature processing is applicable during its production. Moreover, the perovskite layer provides a tunable band gap. Therefore, depending on better developments on designed molecules, PSC may gain extreme performances compared to the other competitors, such as OSC or DSSC devices. This chapter starts with a general discussion on the need for an affordable clean energy conversion device that is urgent for the future of humanity, due to publicly well‐known global warming issue. In Section 2, basic properties of PSC are mentioned together with their structure and working principles. Section 3 continues with an overview on organometallic perovskite molecules after a brief introductory history is presented. The absorption and band gap properties are also discussed. Since most perovskite materials need a hole transporting material (HTMs) within the PSC, the kinds of HTMs that are designed for PSCs are described in Section 3. The rendering of long‐term stabilization has special importance for PSCs since the instability issue remained idle in spite of those recent increased efficiency values attained by various research groups. Therefore, the stability issues are discussed in a separate part in Section 4. We finally close the chapter discussing the challenges and opportunities relying on the chapter content. We note that the recent investigations on PSCs have special importance for its large‐scale realization in order to make them ready for the photovoltaic industry of the future. Hence, there are various announced meetings focusing on its mass production due to the unexpected sharp rise of the perovskite efficiency in the last 6 years. Hence, all the new cutting‐edge scientific findings are also dealt with commercialization issues now, in order to attain the desired low cost fabrication, including the yield of high purity and the formation of smooth films during the continual manufacture of perovskite layers.",signatures:"Serafettin Demic, Ahmet Nuri Ozcivan, Mustafa Can, Cebrail Ozbek\nand Merve Karakaya",authors:[{id:"176024",title:"Dr.",name:"Mustafa",surname:"Can",fullName:"Mustafa Can",slug:"mustafa-can",email:"mustafacan80@yahoo.com"},{id:"193591",title:"Prof.",name:"Serafettin",surname:"Demic",fullName:"Serafettin Demic",slug:"serafettin-demic",email:"serafettin.demic@gmail.com"},{id:"193592",title:"Dr.",name:"Ahmet Nuri",surname:"Ozcivan",fullName:"Ahmet Nuri Ozcivan",slug:"ahmet-nuri-ozcivan",email:"ahmetnuri.ozcivan@ikc.edu.tr"},{id:"193593",title:"Mr.",name:"Cebrail",surname:"Özbek",fullName:"Cebrail Özbek",slug:"cebrail-ozbek",email:"cebrailozbek@gmail.com"},{id:"193594",title:"Mrs.",name:"Merve",surname:"Karakaya",fullName:"Merve Karakaya",slug:"merve-karakaya",email:"cnrkarakaya@gmail.com"}],book:{id:"5347",title:"Nanostructured Solar Cells",slug:"nanostructured-solar-cells",productType:{id:"1",title:"Edited Volume"}}},{id:"68995",title:"Applications of Graphene Modified by Self-Assembled Monolayers",slug:"applications-of-graphene-modified-by-self-assembled-monolayers",abstract:"Self-assembled monolayers (SAMs) are well-oriented molecular structures that are formed by the adsorption of an active site of a surfactant onto a substrate’s surface. Aromatic SAMs were used to modify anode/hole transport layer interface in order to achieve preferable barrier alignment and charge carrier injection from anode to an organic-based thin film material. Other functions of SAMs include current blocking layers or moisture penetration blocking layers, dipolar surface layers for enhanced charge injection, and modification of work function of a material such as graphene acting as a spacer to physically separate and electrically decouple it from the substrate. Additionally, SAM modification of graphene leads to its electronic passivation at layers’ edges, elimination of defects, and enhanced adhesion and stability. The surface modification with molecules capable of forming SAM is a fast, simple, low-cost, and effective technique for the development of novel materials especially for the production of electronic devices. The ability to modify its properties by SAM technique has opened up a wide range of applications in electronic and optoelectronic devices.",signatures:"Gulsum Ersu, Yenal Gokpek, Mustafa Can, Ceylan Zafer and Serafettin Demic",authors:[{id:"176024",title:"Dr.",name:"Mustafa",surname:"Can",fullName:"Mustafa Can",slug:"mustafa-can",email:"mustafacan80@yahoo.com"},{id:"193591",title:"Prof.",name:"Serafettin",surname:"Demic",fullName:"Serafettin Demic",slug:"serafettin-demic",email:"serafettin.demic@gmail.com"},{id:"280559",title:"MSc.",name:"Gulsum",surname:"Ersu",fullName:"Gulsum Ersu",slug:"gulsum-ersu",email:"gulsumersu@gmail.com"},{id:"280560",title:"M.Sc.",name:"Yenal",surname:"Gokpek",fullName:"Yenal Gokpek",slug:"yenal-gokpek",email:"yenalgokpek@gmail.com"},{id:"280563",title:"Prof.",name:"Ceylan",surname:"Zafer",fullName:"Ceylan Zafer",slug:"ceylan-zafer",email:"ceylan.zafer@ege.edu.tr"}],book:{id:"9414",title:"Advances in Condensed-Matter and Materials Physics",slug:"advances-in-condensed-matter-and-materials-physics-rudimentary-research-to-topical-technology",productType:{id:"1",title:"Edited Volume"}}},{id:"74453",title:"Perovskite Nanoparticles",slug:"perovskite-nanoparticles",abstract:"2D perovskite nanoparticles have a great potential for using in optoelectronic devices such as Solar Cells and Light Emitting Diodes within their tuneable optic and structural properties. In this chapter, it is aimed to express “relation between chemical structures and photo-physical behaviours of perovskite nanoparticles and milestones for their electronic applications”. Initially, general synthesis methods of perovskite nanoparticles have been explained. Furthermore, advantages and disadvantages of the methods have been discussed. After the synthesis, formation of 2D perovskite crystal and effects on shape factor, particle size and uniformity of perovskite have been explained in detail. Beside these, optic properties of luminescent perovskite nanoparticles have been summarized a long with spectral band tuning via size and composition changes. In addition, since their different optical properties and relatively more stable chemical structure under ambient conditions, a comprehensive compilation of opto-electronic applications of 2D perovskite nanoparticles have been prepared.",signatures:"Burak Gultekin, Ali Kemal Havare, Shirin Siyahjani, Halil Ibrahim Ciftci and Mustafa Can",authors:[{id:"176024",title:"Dr.",name:"Mustafa",surname:"Can",fullName:"Mustafa Can",slug:"mustafa-can",email:"mustafacan80@yahoo.com"},{id:"205447",title:"Dr.",name:"Ali Kemal",surname:"Havare",fullName:"Ali Kemal Havare",slug:"ali-kemal-havare",email:"alikemal.havare@gmail.com"},{id:"323709",title:"Dr.",name:"Burak",surname:"Gültekin",fullName:"Burak Gültekin",slug:"burak-gultekin",email:"burakgultekin@gmail.com"},{id:"323944",title:"Mrs.",name:"Shirin",surname:"Siyahjani",fullName:"Shirin Siyahjani",slug:"shirin-siyahjani",email:"s_siahjani@yahoo.com"},{id:"323946",title:"Dr.",name:"Halilibrahim",surname:"Çiftçi",fullName:"Halilibrahim Çiftçi",slug:"halilibrahim-ciftci",email:"hiciftci@kumamoto-u.ac.jp"}],book:{id:"9881",title:"Perovskite and Piezoelectric Materials",slug:"perovskite-and-piezoelectric-materials",productType:{id:"1",title:"Edited Volume"}}}],collaborators:[{id:"7187",title:"Dr.",name:"Harutaka",surname:"Mekaru",slug:"harutaka-mekaru",fullName:"Harutaka Mekaru",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"National Institute of Advanced Industrial Science and Technology",institutionURL:null,country:{name:"Japan"}}},{id:"52898",title:"Prof.",name:"Zaki",surname:"Ahmad",slug:"zaki-ahmad",fullName:"Zaki Ahmad",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/52898/images/1942_n.jpg",biography:"Professor Dr. Zaki Ahmad worked at King Fahd University of Petroleum and Minerals for thirty years in rendered distinguished services in teaching and research. He obtained his PhD from LEEDS University, UK. He was a chartered metallurgical engineer (C.Eng) from engineering council UK. He was a fellow of the institute of Materials, Minerals and Mining(FIMMM). He was a member of the European federation of corrosion and a fellow of institute of Metal Finishing. He substantially contributed to the founding activities in material science, corrosion engineering and nanotechnology at KFUPM and in Iran. He worked on international projects on aluminum with Aluminum, Ranshofen, Austria and Forschungzentrum, Geethscht, Germany and with Metallgesselscheft, Germany. He worked on international projects with Ministry of Technology, Germany. He was a founder contributor of center of excellence in corrosion at KFUPM, Dhahran, Saudi Arabia. He worked on the foundation and development of nanotechnology in Saudi Arabia in 2004. He was the author of “Principles of Corrosion Engineering and Corrosion Control” published by Elsevier in 2006. He has written over 95 research papers and international journals and over forty papers in international research conferences. His research activities included development of Al/SC alloys, Nanostructured superhydrophrobic surfaces, Nanocoatings and self-healing techniques. He was nominated for best researcher award in the Middle East by Energy Exchange in 2011. He was a consultant of several research organizations.",institutionString:null,institution:{name:"COMSATS University Islamabad",institutionURL:null,country:{name:"Pakistan"}}},{id:"52910",title:"Dr.",name:"Amir",surname:"Farzaneh",slug:"amir-farzaneh",fullName:"Amir Farzaneh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/52910/images/3665_n.jpg",biography:null,institutionString:null,institution:{name:"University of Maragheh",institutionURL:null,country:{name:"Iran"}}},{id:"169994",title:"Dr.",name:"Sebastian",surname:"Feliu Batlle",slug:"sebastian-feliu-batlle",fullName:"Sebastian Feliu Batlle",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Barcelona",institutionURL:null,country:{name:"Spain"}}},{id:"173467",title:"Prof.",name:"Salih",surname:"Okur",slug:"salih-okur",fullName:"Salih Okur",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"176155",title:"Dr.",name:"Omer",surname:"Mermer",slug:"omer-mermer",fullName:"Omer Mermer",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"176463",title:"Dr.",name:"Ali",surname:"Kemal Havare",slug:"ali-kemal-havare",fullName:"Ali Kemal Havare",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"177746",title:"Dr.",name:"Amir A.",surname:"El hadad",slug:"amir-a.-el-hadad",fullName:"Amir A. El hadad",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"177747",title:"Dr.",name:"Violeta",surname:"Barranco",slug:"violeta-barranco",fullName:"Violeta Barranco",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"177748",title:"Dr.",name:"Irene",surname:"Llorente",slug:"irene-llorente",fullName:"Irene Llorente",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null}]},generic:{page:{slug:"our-story",title:"Our story",intro:"
The company was founded in Vienna in 2004 by Alex Lazinica and Vedran Kordic, two PhD students researching robotics. While completing our PhDs, we found it difficult to access the research we needed. So, we decided to create a new Open Access publisher. A better one, where researchers like us could find the information they needed easily. The result is IntechOpen, an Open Access publisher that puts the academic needs of the researchers before the business interests of publishers.
",metaTitle:"Our story",metaDescription:"The company was founded in Vienna in 2004 by Alex Lazinica and Vedran Kordic, two PhD students researching robotics. While completing our PhDs, we found it difficult to access the research we needed. So, we decided to create a new Open Access publisher. A better one, where researchers like us could find the information they needed easily. The result is IntechOpen, an Open Access publisher that puts the academic needs of the researchers before the business interests of publishers.",metaKeywords:null,canonicalURL:"/page/our-story",contentRaw:'[{"type":"htmlEditorComponent","content":"
We started by publishing journals and books from the fields of science we were most familiar with - AI, robotics, manufacturing and operations research. Through our growing network of institutions and authors, we soon expanded into related fields like environmental engineering, nanotechnology, computer science, renewable energy and electrical engineering, Today, we are the world’s largest Open Access publisher of scientific research, with over 4,200 books and 54,000 scientific works including peer-reviewed content from more than 116,000 scientists spanning 161 countries. Our authors range from globally-renowned Nobel Prize winners to up-and-coming researchers at the cutting edge of scientific discovery.
\\n\\n
In the same year that IntechOpen was founded, we launched what was at the time the first ever Open Access, peer-reviewed journal in its field: the International Journal of Advanced Robotic Systems (IJARS).
\\n\\n
The IntechOpen timeline
\\n\\n
2004
\\n\\n
\\n\\t
Intech Open is founded in Vienna, Austria, by Alex Lazinica and Vedran Kordic, two PhD students, and their first Open Access journals and books are published.
\\n\\t
Alex and Vedran launch the first Open Access, peer-reviewed robotics journal and IntechOpen’s flagship publication, the International Journal of Advanced Robotic Systems (IJARS).
\\n
\\n\\n
2005
\\n\\n
\\n\\t
IntechOpen publishes its first Open Access book: Cutting Edge Robotics.
\\n
\\n\\n
2006
\\n\\n
\\n\\t
IntechOpen publishes a special issue of IJARS, featuring contributions from NASA scientists regarding the Mars Exploration Rover missions.
\\n
\\n\\n
2008
\\n\\n
\\n\\t
Downloads milestone: 200,000 downloads reached
\\n
\\n\\n
2009
\\n\\n
\\n\\t
Publishing milestone: the first 100 Open Access STM books are published
\\n
\\n\\n
2010
\\n\\n
\\n\\t
Downloads milestone: one million downloads reached
\\n\\t
IntechOpen expands its book publishing into a new field: medicine.
\\n
\\n\\n
2011
\\n\\n
\\n\\t
Publishing milestone: More than five million downloads reached
\\n\\t
IntechOpen publishes 1996 Nobel Prize in Chemistry winner Harold W. Kroto’s “Strategies to Successfully Cross-Link Carbon Nanotubes”. Find it here.
\\n\\t
IntechOpen and TBI collaborate on a project to explore the changing needs of researchers and the evolving ways that they discover, publish and exchange information. The result is the survey “Author Attitudes Towards Open Access Publishing: A Market Research Program”.
\\n\\t
IntechOpen hosts SHOW - Share Open Access Worldwide; a series of lectures, debates, round-tables and events to bring people together in discussion of open source principles, intellectual property, content licensing innovations, remixed and shared culture and free knowledge.
\\n
\\n\\n
2012
\\n\\n
\\n\\t
Publishing milestone: 10 million downloads reached
\\n\\t
IntechOpen holds Interact2012, a free series of workshops held by figureheads of the scientific community including Professor Hiroshi Ishiguro, director of the Intelligent Robotics Laboratory, who took the audience through some of the most impressive human-robot interactions observed in his lab.
\\n
\\n\\n
2013
\\n\\n
\\n\\t
IntechOpen joins the Committee on Publication Ethics (COPE) as part of a commitment to guaranteeing the highest standards of publishing.
\\n
\\n\\n
2014
\\n\\n
\\n\\t
IntechOpen turns 10, with more than 30 million downloads to date.
\\n\\t
IntechOpen appoints its first Regional Representatives - members of the team situated around the world dedicated to increasing the visibility of our authors’ published work within their local scientific communities.
\\n
\\n\\n
2015
\\n\\n
\\n\\t
Downloads milestone: More than 70 million downloads reached, more than doubling since the previous year.
\\n\\t
Publishing milestone: IntechOpen publishes its 2,500th book and 40,000th Open Access chapter, reaching 20,000 citations in Thomson Reuters ISI Web of Science.
\\n\\t
40 IntechOpen authors are included in the top one per cent of the world’s most-cited researchers.
\\n\\t
Thomson Reuters’ ISI Web of Science Book Citation Index begins indexing IntechOpen’s books in its database.
\\n
\\n\\n
2016
\\n\\n
\\n\\t
IntechOpen is identified as a world leader in Simba Information’s Open Access Book Publishing 2016-2020 report and forecast. IntechOpen came in as the world’s largest Open Access book publisher by title count.
\\n
\\n\\n
2017
\\n\\n
\\n\\t
Downloads milestone: IntechOpen reaches more than 100 million downloads
\\n\\t
Publishing milestone: IntechOpen publishes its 3,000th Open Access book, making it the largest Open Access book collection in the world
We started by publishing journals and books from the fields of science we were most familiar with - AI, robotics, manufacturing and operations research. Through our growing network of institutions and authors, we soon expanded into related fields like environmental engineering, nanotechnology, computer science, renewable energy and electrical engineering, Today, we are the world’s largest Open Access publisher of scientific research, with over 4,200 books and 54,000 scientific works including peer-reviewed content from more than 116,000 scientists spanning 161 countries. Our authors range from globally-renowned Nobel Prize winners to up-and-coming researchers at the cutting edge of scientific discovery.
\n\n
In the same year that IntechOpen was founded, we launched what was at the time the first ever Open Access, peer-reviewed journal in its field: the International Journal of Advanced Robotic Systems (IJARS).
\n\n
The IntechOpen timeline
\n\n
2004
\n\n
\n\t
Intech Open is founded in Vienna, Austria, by Alex Lazinica and Vedran Kordic, two PhD students, and their first Open Access journals and books are published.
\n\t
Alex and Vedran launch the first Open Access, peer-reviewed robotics journal and IntechOpen’s flagship publication, the International Journal of Advanced Robotic Systems (IJARS).
\n
\n\n
2005
\n\n
\n\t
IntechOpen publishes its first Open Access book: Cutting Edge Robotics.
\n
\n\n
2006
\n\n
\n\t
IntechOpen publishes a special issue of IJARS, featuring contributions from NASA scientists regarding the Mars Exploration Rover missions.
\n
\n\n
2008
\n\n
\n\t
Downloads milestone: 200,000 downloads reached
\n
\n\n
2009
\n\n
\n\t
Publishing milestone: the first 100 Open Access STM books are published
\n
\n\n
2010
\n\n
\n\t
Downloads milestone: one million downloads reached
\n\t
IntechOpen expands its book publishing into a new field: medicine.
\n
\n\n
2011
\n\n
\n\t
Publishing milestone: More than five million downloads reached
\n\t
IntechOpen publishes 1996 Nobel Prize in Chemistry winner Harold W. Kroto’s “Strategies to Successfully Cross-Link Carbon Nanotubes”. Find it here.
\n\t
IntechOpen and TBI collaborate on a project to explore the changing needs of researchers and the evolving ways that they discover, publish and exchange information. The result is the survey “Author Attitudes Towards Open Access Publishing: A Market Research Program”.
\n\t
IntechOpen hosts SHOW - Share Open Access Worldwide; a series of lectures, debates, round-tables and events to bring people together in discussion of open source principles, intellectual property, content licensing innovations, remixed and shared culture and free knowledge.
\n
\n\n
2012
\n\n
\n\t
Publishing milestone: 10 million downloads reached
\n\t
IntechOpen holds Interact2012, a free series of workshops held by figureheads of the scientific community including Professor Hiroshi Ishiguro, director of the Intelligent Robotics Laboratory, who took the audience through some of the most impressive human-robot interactions observed in his lab.
\n
\n\n
2013
\n\n
\n\t
IntechOpen joins the Committee on Publication Ethics (COPE) as part of a commitment to guaranteeing the highest standards of publishing.
\n
\n\n
2014
\n\n
\n\t
IntechOpen turns 10, with more than 30 million downloads to date.
\n\t
IntechOpen appoints its first Regional Representatives - members of the team situated around the world dedicated to increasing the visibility of our authors’ published work within their local scientific communities.
\n
\n\n
2015
\n\n
\n\t
Downloads milestone: More than 70 million downloads reached, more than doubling since the previous year.
\n\t
Publishing milestone: IntechOpen publishes its 2,500th book and 40,000th Open Access chapter, reaching 20,000 citations in Thomson Reuters ISI Web of Science.
\n\t
40 IntechOpen authors are included in the top one per cent of the world’s most-cited researchers.
\n\t
Thomson Reuters’ ISI Web of Science Book Citation Index begins indexing IntechOpen’s books in its database.
\n
\n\n
2016
\n\n
\n\t
IntechOpen is identified as a world leader in Simba Information’s Open Access Book Publishing 2016-2020 report and forecast. IntechOpen came in as the world’s largest Open Access book publisher by title count.
\n
\n\n
2017
\n\n
\n\t
Downloads milestone: IntechOpen reaches more than 100 million downloads
\n\t
Publishing milestone: IntechOpen publishes its 3,000th Open Access book, making it the largest Open Access book collection in the world
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After almost 32 years of teaching at the University of Trás-os-Montes and Alto Douro, she recently moved to the University of Évora, Department of Veterinary Medicine, where she teaches in the field of Animal Reproduction and Clinics. Her primary research areas include the molecular markers of the endometrial cycle and the embryo–maternal interaction, including oxidative stress and the reproductive physiology and disorders of sexual development, besides the molecular determinants of male and female fertility. She often supervises students preparing their master's or doctoral theses. She is also a frequent referee for various journals.",institutionString:null,institution:{name:"University of Évora",country:{name:"Portugal"}}},{id:"283019",title:"Dr.",name:"Oudessa",middleName:null,surname:"Kerro Dego",slug:"oudessa-kerro-dego",fullName:"Oudessa Kerro Dego",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/283019/images/system/283019.png",biography:"Dr. Kerro Dego is a veterinary microbiologist with training in veterinary medicine, microbiology, and anatomic pathology. Dr. Kerro Dego is an assistant professor of dairy health in the department of animal science, the University of Tennessee, Institute of Agriculture, Knoxville, Tennessee. He received his D.V.M. (1997), M.S. (2002), and Ph.D. (2008) degrees in Veterinary Medicine, Animal Pathology and Veterinary Microbiology from College of Veterinary Medicine, Addis Ababa University, Ethiopia; College of Veterinary Medicine, Utrecht University, the Netherlands and Western College of Veterinary Medicine, University of Saskatchewan, Canada respectively. He did his Postdoctoral training in microbial pathogenesis (2009 - 2015) in the Department of Animal Science, the University of Tennessee, Institute of Agriculture, Knoxville, Tennessee. Dr. Kerro Dego’s research focuses on the prevention and control of infectious diseases of farm animals, particularly mastitis, improving dairy food safety, and mitigation of antimicrobial resistance. Dr. Kerro Dego has extensive experience in studying the pathogenesis of bacterial infections, identification of virulence factors, and vaccine development and efficacy testing against major bacterial mastitis pathogens. Dr. Kerro Dego conducted numerous controlled experimental and field vaccine efficacy studies, vaccination, and evaluation of immunological responses in several species of animals, including rodents (mice) and large animals (bovine and ovine).",institutionString:"University of Tennessee at Knoxville",institution:{name:"University of Tennessee at Knoxville",country:{name:"United States of America"}}},{id:"251314",title:"Dr.",name:"Juan Carlos",middleName:null,surname:"Gardón",slug:"juan-carlos-gardon",fullName:"Juan Carlos Gardón",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/251314/images/system/251314.jpeg",biography:"Juan Carlos Gardón Poggi received University degree from the Faculty of Agrarian Science in Argentina, in 1983. Also he received Masters Degree and PhD from Córdoba University, Spain. He is currently a Professor at the Catholic University of Valencia San Vicente Mártir, at the Department of Medicine and Animal Surgery. He teaches diverse courses in the field of Animal Reproduction and he is the Director of the Veterinary Farm. He also participates in academic postgraduate activities at the Veterinary Faculty of Murcia University, Spain. His research areas include animal physiology, physiology and biotechnology of reproduction either in males or females, the study of gametes under in vitro conditions and the use of ultrasound as a complement to physiological studies and development of applied biotechnologies. Routinely, he supervises students preparing their doctoral, master thesis or final degree projects.",institutionString:"Catholic University of Valencia San Vicente Mártir, Spain",institution:null},{id:"125292",title:"Dr.",name:"Katy",middleName:null,surname:"Satué Ambrojo",slug:"katy-satue-ambrojo",fullName:"Katy Satué Ambrojo",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/125292/images/system/125292.jpeg",biography:"Katy Satué Ambrojo received her Veterinary Medicine degree, Master degree in Equine Technology and doctorate in Veterinary Medicine from the Faculty of Veterinary, CEU-Cardenal Herrera University in Valencia, Spain. She is a Full Professor at the Department of Medicine and Animal Surgery at the same University. She developed her research activity in the field of Endocrinology, Hematology, Biochemistry and Immunology of horses. She is a scientific reviewer of several international journals : American Journal of Obstetrics and Gynecology, Comparative Clinical Pathology, Veterinary Clinical Pathology, Journal of Equine Veterinary Science, Reproduction in Domestic Animals, Research Veterinary Science, Brazilian Journal of Medical and Biological Research, Livestock Production Science and Theriogenology. Since 2014, she has been the Head of the Clinical Analysis Laboratory of the Hospital Clínico Veterinario from the Faculty of Veterinary, CEU-Cardenal Herrera University.",institutionString:"CEU-Cardenal Herrera University",institution:{name:"CEU Cardinal Herrera University",country:{name:"Spain"}}},{id:"309529",title:"Dr.",name:"Albert",middleName:null,surname:"Rizvanov",slug:"albert-rizvanov",fullName:"Albert Rizvanov",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/309529/images/9189_n.jpg",biography:'Albert A. Rizvanov is a Professor and Director of the Center for Precision and Regenerative Medicine at the Institute of Fundamental Medicine and Biology, Kazan Federal University (KFU), Russia. He is the Head of the Center of Excellence “Regenerative Medicine” and Vice-Director of Strategic Academic Unit \\"Translational 7P Medicine\\". Albert completed his Ph.D. at the University of Nevada, Reno, USA and Dr.Sci. at KFU. He is a corresponding member of the Tatarstan Academy of Sciences, Russian Federation. Albert is an author of more than 300 peer-reviewed journal articles and 22 patents. He has supervised 11 Ph.D. and 2 Dr.Sci. dissertations. Albert is the Head of the Dissertation Committee on Biochemistry, Microbiology, and Genetics at KFU.\nORCID https://orcid.org/0000-0002-9427-5739\nWebsite https://kpfu.ru/Albert.Rizvanov?p_lang=2',institutionString:"Kazan Federal University",institution:{name:"Kazan Federal University",country:{name:"Russia"}}},{id:"210551",title:"Dr.",name:"Arbab",middleName:null,surname:"Sikandar",slug:"arbab-sikandar",fullName:"Arbab Sikandar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/210551/images/system/210551.jpg",biography:"Dr. Arbab Sikandar, PhD, M. Phil, DVM was born on April 05, 1981. He is currently working at the College of Veterinary & Animal Sciences as an Assistant Professor. He previously worked as a lecturer at the same University. \nHe is a Member/Secretory of Ethics committee (No. CVAS-9377 dated 18-04-18), Member of the QEC committee CVAS, Jhang (Regr/Gen/69/873, dated 26-10-2017), Member, Board of studies of Department of Basic Sciences (No. CVAS. 2851 Dated. 12-04-13, and No. CVAS, 9024 dated 20/11/17), Member of Academic Committee, CVAS, Jhang (No. CVAS/2004, Dated, 25-08-12), Member of the technical committee (No. CVAS/ 4085, dated 20,03, 2010 till 2016).\n\nDr. Arbab Sikandar contributed in five days hands-on-training on Histopathology at the Department of Pathology, UVAS from 12-16 June 2017. He received a Certificate of appreciation for contributions for Popularization of Science and Technology in the Society on 17-11-15. He was the resource person in the lecture series- ‘scientific writing’ at the Department of Anatomy and Histology, UVAS, Lahore on 29th October 2015. He won a full fellowship as a principal candidate for the year 2015 in the field of Agriculture, EICA, Egypt with ref. to the Notification No. 12(11) ACS/Egypt/2014 from 10 July 2015 to 25th September 2015.; he received a grant of Rs. 55000/- as research incentives from Director, Advanced Studies and Research, UVAS, Lahore upon publications of research papers in IF Journals (DR/215, dated 19-5-2014.. He obtained his PhD by winning a HEC Pakistan indigenous Scholarship, ‘Ph.D. fellowship for 5000 scholars – Phase II’ (2av1-147), 17-6/HEC/HRD/IS-II/12, November 15, 2012. \n\nDr. Sikandar is a member of numerous societies: Registered Veterinary Medical Practitioner (life member) and Registered Veterinary Medical Faculty of Pakistan Veterinary Medical Council. The Registration code of PVMC is RVMP/4298 and RVMF/ 0102.; Life member of the University of Veterinary and Animal Sciences, Lahore, Alumni Association with S# 664, dated: 6-4-12. ; Member 'Vets Care Organization Pakistan” with Reference No. VCO-605-149, dated 05-04-06. :Member 'Vet Crescent” (Society of Animal Health and Production), UVAS, Lahore.",institutionString:"University of Veterinary & Animal Science",institution:{name:"University of Veterinary and Animal Sciences",country:{name:"Pakistan"}}},{id:"311663",title:"Dr.",name:"Prasanna",middleName:null,surname:"Pal",slug:"prasanna-pal",fullName:"Prasanna Pal",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/311663/images/13261_n.jpg",biography:null,institutionString:null,institution:{name:"National Dairy Research Institute",country:{name:"India"}}},{id:"202192",title:"Dr.",name:"Catrin",middleName:null,surname:"Rutland",slug:"catrin-rutland",fullName:"Catrin Rutland",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/202192/images/system/202192.png",biography:"Catrin Rutland is an Associate Professor of Anatomy and Developmental Genetics at the University of Nottingham, UK. She obtained a BSc from the University of Derby, England, a master’s degree from Technische Universität München, Germany, and a Ph.D. from the University of Nottingham. She undertook a post-doctoral research fellowship in the School of Medicine before accepting tenure in Veterinary Medicine and Science. Dr. Rutland also obtained an MMedSci (Medical Education) and a Postgraduate Certificate in Higher Education (PGCHE). She is the author of more than sixty peer-reviewed journal articles, twelve books/book chapters, and more than 100 research abstracts in cardiovascular biology and oncology. She is a board member of the European Association of Veterinary Anatomists, Fellow of the Anatomical Society, and Senior Fellow of the Higher Education Academy. Dr. Rutland has also written popular science books for the public. https://orcid.org/0000-0002-2009-4898. www.nottingham.ac.uk/vet/people/catrin.rutland",institutionString:null,institution:{name:"University of Nottingham",country:{name:"United Kingdom"}}},{id:"283315",title:"Prof.",name:"Samir",middleName:null,surname:"El-Gendy",slug:"samir-el-gendy",fullName:"Samir El-Gendy",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRduYQAS/Profile_Picture_1606215849748",biography:"Samir El-Gendy is a Professor of anatomy and embryology at the faculty of veterinary medicine, Alexandria University, Egypt. Samir obtained his PhD in veterinary science in 2007 from the faculty of veterinary medicine, Alexandria University and has been a professor since 2017. Samir is an author on 24 articles at Scopus and 12 articles within local journals and 2 books/book chapters. His research focuses on applied anatomy, imaging techniques and computed tomography. Samir worked as a member of different local projects on E-learning and he is a board member of the African Association of Veterinary Anatomists and of anatomy societies and as an associated author at local and international journals. Orcid: https://orcid.org/0000-0002-6180-389X",institutionString:null,institution:{name:"Alexandria University",country:{name:"Egypt"}}},{id:"246149",title:"Dr.",name:"Valentina",middleName:null,surname:"Kubale",slug:"valentina-kubale",fullName:"Valentina Kubale",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/246149/images/system/246149.jpg",biography:"Valentina Kubale is Associate Professor of Veterinary Medicine at the Veterinary Faculty, University of Ljubljana, Slovenia. Since graduating from the Veterinary faculty she obtained her PhD in 2007, performed collaboration with the Department of Pharmacology, University of Copenhagen, Denmark. She continued as a post-doctoral fellow at the University of Copenhagen with a Lundbeck foundation fellowship. She is the editor of three books and author/coauthor of 23 articles in peer-reviewed scientific journals, 16 book chapters, and 68 communications at scientific congresses. Since 2008 she has been the Editor Assistant for the Slovenian Veterinary Research journal. She is a member of Slovenian Biochemical Society, The Endocrine Society, European Association of Veterinary Anatomists and Society for Laboratory Animals, where she is board member.",institutionString:"University of Ljubljana",institution:{name:"University of Ljubljana",country:{name:"Slovenia"}}},{id:"258334",title:"Dr.",name:"Carlos Eduardo",middleName:null,surname:"Fonseca-Alves",slug:"carlos-eduardo-fonseca-alves",fullName:"Carlos Eduardo Fonseca-Alves",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/258334/images/system/258334.jpg",biography:"Dr. Fonseca-Alves earned his DVM from Federal University of Goias – UFG in 2008. He completed an internship in small animal internal medicine at UPIS university in 2011, earned his MSc in 2013 and PhD in 2015 both in Veterinary Medicine at Sao Paulo State University – UNESP. Dr. Fonseca-Alves currently serves as an Assistant Professor at Paulista University – UNIP teaching small animal internal medicine.",institutionString:null,institution:{name:"Universidade Paulista",country:{name:"Brazil"}}},{id:"245306",title:"Dr.",name:"María Luz",middleName:null,surname:"Garcia Pardo",slug:"maria-luz-garcia-pardo",fullName:"María Luz Garcia Pardo",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/245306/images/system/245306.png",biography:"María de la Luz García Pardo is an agricultural engineer from Universitat Politècnica de València, Spain. She has a Ph.D. in Animal Genetics. Currently, she is a lecturer at the Agrofood Technology Department of Miguel Hernández University, Spain. Her research is focused on genetics and reproduction in rabbits. The major goal of her research is the genetics of litter size through novel methods such as selection by the environmental sensibility of litter size, with forays into the field of animal welfare by analysing the impact on the susceptibility to diseases and stress of the does. Details of her publications can be found at https://orcid.org/0000-0001-9504-8290.",institutionString:null,institution:{name:"Miguel Hernandez University",country:{name:"Spain"}}},{id:"41319",title:"Prof.",name:"Lung-Kwang",middleName:null,surname:"Pan",slug:"lung-kwang-pan",fullName:"Lung-Kwang Pan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/41319/images/84_n.jpg",biography:null,institutionString:null,institution:null},{id:"201721",title:"Dr.",name:"Beatrice",middleName:null,surname:"Funiciello",slug:"beatrice-funiciello",fullName:"Beatrice Funiciello",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/201721/images/11089_n.jpg",biography:"Graduated from the University of Milan in 2011, my post-graduate education included CertAVP modules mainly on equines (dermatology and internal medicine) and a few on small animal (dermatology and anaesthesia) at the University of Liverpool. After a general CertAVP (2015) I gained the designated Certificate in Veterinary Dermatology (2017) after taking the synoptic examination and then applied for the RCVS ADvanced Practitioner status. After that, I completed the Postgraduate Diploma in Veterinary Professional Studies at the University of Liverpool (2018). My main area of work is cross-species veterinary dermatology.",institutionString:null,institution:null},{id:"291226",title:"Dr.",name:"Monica",middleName:null,surname:"Cassel",slug:"monica-cassel",fullName:"Monica Cassel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/291226/images/8232_n.jpg",biography:'Degree in Biological Sciences at the Federal University of Mato Grosso with scholarship for Scientific Initiation by FAPEMAT (2008/1) and CNPq (2008/2-2009/2): Project \\"Histological evidence of reproductive activity in lizards of the Manso region, Chapada dos Guimarães, Mato Grosso, Brazil\\". Master\\\'s degree in Ecology and Biodiversity Conservation at Federal University of Mato Grosso with a scholarship by CAPES/REUNI program: Project \\"Reproductive biology of Melanorivulus punctatus\\". PhD\\\'s degree in Science (Cell and Tissue Biology Area) \n at University of Sao Paulo with scholarship granted by FAPESP; Project \\"Development of morphofunctional changes in ovary of Astyanax altiparanae Garutti & Britski, 2000 (Teleostei, Characidae)\\". She has experience in Reproduction of vertebrates and Morphology, with emphasis in Cellular Biology and Histology. She is currently a teacher in the medium / technical level courses at IFMT-Alta Floresta, as well as in the Bachelor\\\'s degree in Animal Science and in the Bachelor\\\'s degree in Business.',institutionString:null,institution:null},{id:"442807",title:"Dr.",name:"Busani",middleName:null,surname:"Moyo",slug:"busani-moyo",fullName:"Busani Moyo",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Gwanda State University",country:{name:"Zimbabwe"}}},{id:"423023",title:"Dr.",name:"Yosra",middleName:null,surname:"Soltan",slug:"yosra-soltan",fullName:"Yosra Soltan",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Alexandria University",country:{name:"Egypt"}}},{id:"349788",title:"Dr.",name:"Florencia Nery",middleName:null,surname:"Sompie",slug:"florencia-nery-sompie",fullName:"Florencia Nery Sompie",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Sam Ratulangi University",country:{name:"Indonesia"}}},{id:"345713",title:"Dr.",name:"Csaba",middleName:null,surname:"Szabó",slug:"csaba-szabo",fullName:"Csaba Szabó",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Debrecen",country:{name:"Hungary"}}},{id:"345719",title:"Mrs.",name:"Márta",middleName:null,surname:"Horváth",slug:"marta-horvath",fullName:"Márta Horváth",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Debrecen",country:{name:"Hungary"}}},{id:"420151",title:"Prof.",name:"Novirman",middleName:null,surname:"Jamarun",slug:"novirman-jamarun",fullName:"Novirman Jamarun",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Andalas University",country:{name:"Indonesia"}}},{id:"420149",title:"Dr.",name:"Rusmana",middleName:"Wijaya Setia",surname:"Wijaya Setia Ningrat",slug:"rusmana-wijaya-setia-ningrat",fullName:"Rusmana Wijaya Setia Ningrat",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Andalas University",country:{name:"Indonesia"}}},{id:"339759",title:"Mr.",name:"Abu",middleName:null,surname:"Macavoray",slug:"abu-macavoray",fullName:"Abu Macavoray",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Njala University",country:{name:"Sierra Leone"}}},{id:"339758",title:"Prof.",name:"Benjamin",middleName:null,surname:"Emikpe",slug:"benjamin-emikpe",fullName:"Benjamin Emikpe",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Ibadan",country:{name:"Nigeria"}}},{id:"339760",title:"Mr.",name:"Moinina Nelphson",middleName:null,surname:"Kallon",slug:"moinina-nelphson-kallon",fullName:"Moinina Nelphson Kallon",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Njala University",country:{name:"Sierra Leone"}}}]}},subseries:{item:{id:"17",type:"subseries",title:"Metabolism",keywords:"Biomolecules Metabolism, Energy Metabolism, Metabolic Pathways, Key Metabolic Enzymes, Metabolic Adaptation",scope:"Metabolism is frequently defined in biochemistry textbooks as the overall process that allows living systems to acquire and use the free energy they need for their vital functions or the chemical processes that occur within a living organism to maintain life. Behind these definitions are hidden all the aspects of normal and pathological functioning of all processes that the topic ‘Metabolism’ will cover within the Biochemistry Series. Thus all studies on metabolism will be considered for publication.",coverUrl:"https://cdn.intechopen.com/series_topics/covers/17.jpg",hasOnlineFirst:!0,hasPublishedBooks:!0,annualVolume:11413,editor:{id:"138626",title:"Dr.",name:"Yannis",middleName:null,surname:"Karamanos",slug:"yannis-karamanos",fullName:"Yannis Karamanos",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002g6Jv2QAE/Profile_Picture_1629356660984",biography:"Yannis Karamanos, born in Greece in 1953, completed his pre-graduate studies at the Université Pierre et Marie Curie, Paris, then his Masters and Doctoral degree at the Université de Lille (1983). He was associate professor at the University of Limoges (1987) before becoming full professor of biochemistry at the Université d’Artois (1996). He worked on the structure-function relationships of glycoconjugates and his main project was the investigations on the biological roles of the de-N-glycosylation enzymes (Endo-N-acetyl-β-D-glucosaminidase and peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidase). From 2002 he contributes to the understanding of the Blood-brain barrier functioning using proteomics approaches. He has published more than 70 papers. His teaching areas are energy metabolism and regulation, integration and organ specialization and metabolic adaptation.",institutionString:null,institution:{name:"Artois University",institutionURL:null,country:{name:"France"}}},editorTwo:null,editorThree:null,series:{id:"11",title:"Biochemistry",doi:"10.5772/intechopen.72877",issn:"2632-0983"},editorialBoard:[{id:"243049",title:"Dr.",name:"Anca",middleName:null,surname:"Pantea Stoian",slug:"anca-pantea-stoian",fullName:"Anca Pantea Stoian",profilePictureURL:"https://mts.intechopen.com/storage/users/243049/images/system/243049.jpg",institutionString:null,institution:{name:"Carol Davila University of Medicine and Pharmacy",institutionURL:null,country:{name:"Romania"}}},{id:"203824",title:"Dr.",name:"Attilio",middleName:null,surname:"Rigotti",slug:"attilio-rigotti",fullName:"Attilio Rigotti",profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institutionString:null,institution:{name:"Pontifical Catholic University of Chile",institutionURL:null,country:{name:"Chile"}}},{id:"300470",title:"Dr.",name:"Yanfei (Jacob)",middleName:null,surname:"Qi",slug:"yanfei-(jacob)-qi",fullName:"Yanfei (Jacob) Qi",profilePictureURL:"https://mts.intechopen.com/storage/users/300470/images/system/300470.jpg",institutionString:null,institution:{name:"Centenary Institute of Cancer Medicine and Cell Biology",institutionURL:null,country:{name:"Australia"}}}]},onlineFirstChapters:{paginationCount:0,paginationItems:[]},publishedBooks:{paginationCount:1,paginationItems:[{type:"book",id:"10654",title:"Brain-Computer Interface",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/10654.jpg",slug:"brain-computer-interface",publishedDate:"May 18th 2022",editedByType:"Edited by",bookSignature:"Vahid Asadpour",hash:"a5308884068cc53ed31c6baba756857f",volumeInSeries:9,fullTitle:"Brain-Computer Interface",editors:[{id:"165328",title:"Dr.",name:"Vahid",middleName:null,surname:"Asadpour",slug:"vahid-asadpour",fullName:"Vahid Asadpour",profilePictureURL:"https://mts.intechopen.com/storage/users/165328/images/system/165328.jpg",institutionString:"Kaiser Permanente Southern California",institution:null}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null}]},testimonialsList:[{id:"27",text:"The opportunity to work with a prestigious publisher allows for the possibility to collaborate with more research groups interested in animal nutrition, leading to the development of new feeding strategies and food valuation while being more sustainable with the environment, allowing more readers to learn about the subject.",author:{id:"175967",name:"Manuel",surname:"Gonzalez Ronquillo",institutionString:null,profilePictureURL:"https://mts.intechopen.com/storage/users/175967/images/system/175967.png",slug:"manuel-gonzalez-ronquillo",institution:{id:"6221",name:"Universidad Autónoma del Estado de México",country:{id:null,name:"Mexico"}}}},{id:"8",text:"I work with IntechOpen for a number of reasons: their professionalism, their mission in support of Open Access publishing, and the quality of their peer-reviewed publications, but also because they believe in equality.",author:{id:"202192",name:"Catrin",surname:"Rutland",institutionString:null,profilePictureURL:"https://mts.intechopen.com/storage/users/202192/images/system/202192.png",slug:"catrin-rutland",institution:{id:"134",name:"University of Nottingham",country:{id:null,name:"United Kingdom"}}}},{id:"18",text:"It was great publishing with IntechOpen, the process was straightforward and I had support all along.",author:{id:"71579",name:"Berend",surname:"Olivier",institutionString:"Utrecht University",profilePictureURL:"https://mts.intechopen.com/storage/users/71579/images/system/71579.png",slug:"berend-olivier",institution:{id:"253",name:"Utrecht University",country:{id:null,name:"Netherlands"}}}}]},submityourwork:{pteSeriesList:[],lsSeriesList:[],hsSeriesList:[],sshSeriesList:[],subseriesList:[],annualVolumeBook:{},thematicCollection:[],selectedSeries:null,selectedSubseries:null},seriesLanding:{item:null},libraryRecommendation:{success:null,errors:{},institutions:[]},route:{name:"profile.detail",path:"/profiles/176024",hash:"",query:{},params:{id:"176024"},fullPath:"/profiles/176024",meta:{},from:{name:null,path:"/",hash:"",query:{},params:{},fullPath:"/",meta:{}}}},function(){var e;(e=document.currentScript||document.scripts[document.scripts.length-1]).parentNode.removeChild(e)}()