Structural and functional comparison of AU-rich and GU-rich elements.
\\n\\n
IntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
\\n\\nBy listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
\\n\\nAll three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
\\n\\n"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
\\n\\n"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
\\n\\nIn conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\\n\\n“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\\n\\nWe invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\\n\\nFeel free to share this news on social media and help us mark this memorable moment!
\\n\\n\\n"}]',published:!0,mainMedia:{caption:"",originalUrl:"/media/original/237"}},components:[{type:"htmlEditorComponent",content:'
After years of being acknowledged as the world's leading publisher of Open Access books, today, we are proud to announce we’ve successfully launched a portfolio of Open Science journals covering rapidly expanding areas of interdisciplinary research.
\n\n\n\nIntechOpen was founded by scientists, for scientists, in order to make book publishing accessible around the globe. Over the last two decades, this has driven Open Access (OA) book publishing whilst levelling the playing field for global academics. Through our innovative publishing model and the support of the research community, we have now published over 5,700 Open Access books and are visited online by over three million academics every month. These researchers are increasingly working in broad technology-based subjects, driving multidisciplinary academic endeavours into human health, environment, and technology.
\n\nBy listening to our community, and in order to serve these rapidly growing areas which lie at the core of IntechOpen's expertise, we are launching a portfolio of Open Science journals:
\n\nAll three journals will publish under an Open Access model and embrace Open Science policies to help support the changing needs of academics in these fast-moving research areas. There will be direct links to preprint servers and data repositories, allowing full reproducibility and rapid dissemination of published papers to help accelerate the pace of research. Each journal has renowned Editors in Chief who will work alongside a global Editorial Board, delivering robust single-blind peer review. Supported by our internal editorial teams, this will ensure our authors will receive a quick, user-friendly, and personalised publishing experience.
\n\n"By launching our journals portfolio we are introducing new, dedicated homes for interdisciplinary technology-focused researchers to publish their work, whilst embracing Open Science and creating a unique global home for academics to disseminate their work. We are taking a leap toward Open Science continuing and expanding our fundamental commitment to openly sharing scientific research across the world, making it available for the benefit of all." Dr. Sara Uhac, IntechOpen CEO
\n\n"Our aim is to promote and create better science for a better world by increasing access to information and the latest scientific developments to all scientists, innovators, entrepreneurs and students and give them the opportunity to learn, observe and contribute to knowledge creation. Open Science promotes a swifter path from research to innovation to produce new products and services." Alex Lazinica, IntechOpen founder
\n\nIn conclusion, Natalia Reinic Babic, Head of Journal Publishing and Open Science at IntechOpen adds:
\n\n“On behalf of the journal team I’d like to thank all our Editors in Chief, Editorial Boards, internal supporting teams, and our scientific community for their continuous support in making this portfolio a reality - we couldn’t have done it without you! With your support in place, we are confident these journals will become as impactful and successful as our book publishing program and bring us closer to a more open (science) future.”
\n\nWe invite you to visit the journals homepage and learn more about the journal’s Editorial Boards, scope and vision as all three journals are now open for submissions.
\n\nFeel free to share this news on social media and help us mark this memorable moment!
\n\n\n'}],latestNews:[{slug:"intechopen-supports-asapbio-s-new-initiative-publish-your-reviews-20220729",title:"IntechOpen Supports ASAPbio’s New Initiative Publish Your Reviews"},{slug:"webinar-introduction-to-open-science-wednesday-18-may-1-pm-cest-20220518",title:"Webinar: Introduction to Open Science | Wednesday 18 May, 1 PM CEST"},{slug:"step-in-the-right-direction-intechopen-launches-a-portfolio-of-open-science-journals-20220414",title:"Step in the Right Direction: IntechOpen Launches a Portfolio of Open Science Journals"},{slug:"let-s-meet-at-london-book-fair-5-7-april-2022-olympia-london-20220321",title:"Let’s meet at London Book Fair, 5-7 April 2022, Olympia London"},{slug:"50-books-published-as-part-of-intechopen-and-knowledge-unlatched-ku-collaboration-20220316",title:"50 Books published as part of IntechOpen and Knowledge Unlatched (KU) Collaboration"},{slug:"intechopen-joins-the-united-nations-sustainable-development-goals-publishers-compact-20221702",title:"IntechOpen joins the United Nations Sustainable Development Goals Publishers Compact"},{slug:"intechopen-signs-exclusive-representation-agreement-with-lsr-libros-servicios-y-representaciones-s-a-de-c-v-20211123",title:"IntechOpen Signs Exclusive Representation Agreement with LSR Libros Servicios y Representaciones S.A. de C.V"},{slug:"intechopen-expands-partnership-with-research4life-20211110",title:"IntechOpen Expands Partnership with Research4Life"}]},book:{item:{type:"book",id:"8170",leadTitle:null,fullTitle:"Chemical Properties of Starch",title:"Chemical Properties of Starch",subtitle:null,reviewType:"peer-reviewed",abstract:"This book is about the chemical properties of starch. The book is a rich compendium driven by the desire to address the unmet needs of biomedical scientists to respond adequately to the controversy on the chemical properties and attendant reactivity of starch. It is a collective endeavor by a group of editors and authors with a wealth of experience and expertise on starch to aggregate the influence of qualitative and quantitative morphological, chemical, and genetic properties of starch on its functionalities, use, applications, and health benefits. The chemical properties of starch are conferred by the presence, amount and/or quality of amylose and amylopectin molecules, granule structure, and the nature and amounts of the lipid and protein molecules. The implication of this is comprehensively dealt with in this book.",isbn:"978-1-83880-116-8",printIsbn:"978-1-83880-115-1",pdfIsbn:"978-1-78985-697-2",doi:"10.5772/intechopen.78119",price:119,priceEur:129,priceUsd:155,slug:"chemical-properties-of-starch",numberOfPages:164,isOpenForSubmission:!1,isInWos:null,isInBkci:!1,hash:"0aedfdb374631bb3a33870c4ed16559a",bookSignature:"Martins Emeje",publishedDate:"March 11th 2020",coverURL:"https://cdn.intechopen.com/books/images_new/8170.jpg",numberOfDownloads:13945,numberOfWosCitations:20,numberOfCrossrefCitations:41,numberOfCrossrefCitationsByBook:0,numberOfDimensionsCitations:91,numberOfDimensionsCitationsByBook:1,hasAltmetrics:0,numberOfTotalCitations:152,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"March 25th 2019",dateEndSecondStepPublish:"September 4th 2019",dateEndThirdStepPublish:"November 3rd 2019",dateEndFourthStepPublish:"January 22nd 2020",dateEndFifthStepPublish:"March 22nd 2020",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"94311",title:"Prof.",name:"Martins",middleName:"Ochubiojo",surname:"Ochubiojo Emeje",slug:"martins-ochubiojo-emeje",fullName:"Martins Ochubiojo Emeje",profilePictureURL:"https://mts.intechopen.com/storage/users/94311/images/system/94311.jpeg",biography:"Martins Emeje obtained a BPharm with distinction from Ahmadu Bello University, Nigeria, and an MPharm and Ph.D. from the University of Nigeria (UNN), where he received the best Ph.D. award and was enlisted as UNN’s “Face of Research.” He established the first nanomedicine center in Nigeria and was the pioneer head of the intellectual property and technology transfer as well as the technology innovation and support center. Prof. Emeje’s several international fellowships include the prestigious Raman fellowship. He has published more than 150 articles and patents. He is also the head of R&D at NIPRD and holds a visiting professor position at Nnamdi Azikiwe University, Nigeria. He has a postgraduate certificate in Project Management from Walden University, Minnesota, as well as a professional teaching certificate and a World Bank certification in Public Procurement. Prof. Emeje was a national chairman of academic pharmacists in Nigeria and the 2021 winner of the May & Baker Nigeria Plc–sponsored prize for professional service in research and innovation.",institutionString:"National Institute for Pharmaceutical Research and Development",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"6",totalChapterViews:"0",totalEditedBooks:"2",institution:{name:"National Institute for Pharmaceutical Research and Development",institutionURL:null,country:{name:"Nigeria"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"324",title:"Food Chemistry",slug:"agricultural-and-biological-sciences-bromatology-food-chemistry"}],chapters:[{id:"68278",title:"Chemically Modified Starches as Excipients in Pharmaceutical Dosage Forms",doi:"10.5772/intechopen.88210",slug:"chemically-modified-starches-as-excipients-in-pharmaceutical-dosage-forms",totalDownloads:629,totalCrossrefCites:0,totalDimensionsCites:2,hasAltmetrics:0,abstract:"Excipients play a great role in ensuring that pharmaceutical dosage form meets the required specifications of quality approved by the relevant authorities. Starches are the most widely used excipients in dosage form development, but their use is enhanced by several modification methods (such as chemical degradation, physical alteration, enzymatic modifications or crystalline-genetic transformation), all aimed at restructuring the starch granules, thus ensuring that the reactive polymers are accessible to reactants. Chemical modification of starch usually follows the pathway of substitution, degradation or cross-linking. The most common approaches to chemical modification of starches for pharmaceutical use include oxidation, esterification and etherification, which are employed to optimize the structural and nutritional properties for targeted applications. The oxidant type, botanical origin of starch, and process conditions are all determinants of how effective the oxidation is. Esterification improves the hydrophobicity of starch usually via acetylation and phosphorylation, while etherification is a derivatization technique that involves the use of various alkylation agents such as dimethyl sulphate, diethyl sulphate, alkylene oxides (epoxides) and alkyl halides. Chemically modified starch enhances thermoplasticity, solubility and flow properties. In conclusion, chemically modified starches have shown excellent potentials and are, thus, incorporated as core excipients in several pharmaceutical drug formulations.",signatures:"Oladapo Adewale Adetunji",downloadPdfUrl:"/chapter/pdf-download/68278",previewPdfUrl:"/chapter/pdf-preview/68278",authors:[{id:"299661",title:"Dr.",name:"Oladapo",surname:"Adetunji",slug:"oladapo-adetunji",fullName:"Oladapo Adetunji"}],corrections:null},{id:"68720",title:"Physical and Chemical Modifications in Starch Structure and Reactivity",doi:"10.5772/intechopen.88870",slug:"physical-and-chemical-modifications-in-starch-structure-and-reactivity",totalDownloads:2314,totalCrossrefCites:13,totalDimensionsCites:23,hasAltmetrics:0,abstract:"Starch is a naturally occurring glucose homo-polysaccharide of nutritional, pharmaceutical, and industrial importance. The complex polymeric structure and poor solubility of native starch in water limits their importance at pharmaceutical and industrial level. The structure, reactivity, and functionality of the native starch can be modified by physical, chemical, enzymatic, and biotechnological methods. Various physical modifications techniques, including the thermal, radio-thermal, freezing and thawing, annealing, high-pressure, ultrasonic, and pulsed electric field treatment, and chemical modifications, including oxidation, etherification, esterification, cationization, cross-linking, and graft polymerization, have been found to change the surface properties, polarity and linearity of the molecular chains, the degree of substitution, the polymeric, granular, and crystalline structure, amylose to amylopectin ratio, solubility, viscosity, pasting, gelatinization, swelling, water absorption, and emulsifying properties of starch. The structural changes have resulted in the improvement of thermal and freeze-thaw stability, viscosity, solubility, water binding capacity, swelling power, gelling ability, and enzymatic digestibility of starch. The exposure of reactive functional groups after physical or chemical modification modifies the reactivity of starch toward water, oil, acids, enzymes, and other chemical species. These modification techniques have led to some revolutionary changes in reactivity, functionality, and application of starch in various fields.",signatures:"Haq Nawaz, Rashem Waheed, Mubashir Nawaz and Dure Shahwar",downloadPdfUrl:"/chapter/pdf-download/68720",previewPdfUrl:"/chapter/pdf-preview/68720",authors:[{id:"230900",title:"Mr.",name:"Haq",surname:"Nawaz",slug:"haq-nawaz",fullName:"Haq Nawaz"},{id:"301871",title:"Ms.",name:"Rashem",surname:"Waheed",slug:"rashem-waheed",fullName:"Rashem Waheed"},{id:"301872",title:"Mr.",name:"Mubashir",surname:"Nawaz",slug:"mubashir-nawaz",fullName:"Mubashir Nawaz"},{id:"309769",title:"Ms.",name:"Dure",surname:"Shahwar",slug:"dure-shahwar",fullName:"Dure Shahwar"}],corrections:null},{id:"70289",title:"Starch Source and Its Impact on Pharmaceutical Applications",doi:"10.5772/intechopen.89811",slug:"starch-source-and-its-impact-on-pharmaceutical-applications",totalDownloads:1308,totalCrossrefCites:4,totalDimensionsCites:7,hasAltmetrics:0,abstract:"Starch can be obtained from a variety of plant sources. The specific source of starch, the environmental conditions during starch maturation, and the age of the plant affect the physicochemical composition of the starch. This is because of the effect they have on critical factors especially the amylose amylopectin content of the starch as well as their relative quantities. These factors also affect the starch granule size and size distribution and the levels of minor components such as phosphates, lipids, and the nature of these interactions with amylose and amylopectin. In its wide use as a pharmaceutical excipient especially as binder and disintegrant, unmodified starch is affected in its functionality by the physicochemical properties of the starch. These factors especially by their influence on the swelling power and gelatinization as well as granule size and shape determine the properties of dosage forms in which the starches are used. This results in dosage forms that, although meeting compendial standards, differ in specific properties. The source of starches therefore affects the properties of pharmaceutical dosage forms. This should be taken into consideration in the choice of excipients in drug formulation and before the substitution of one starch for another in a formulation.",signatures:"Olobayo O. Kunle",downloadPdfUrl:"/chapter/pdf-download/70289",previewPdfUrl:"/chapter/pdf-preview/70289",authors:[{id:"308617",title:"Prof.",name:"Olobayo",surname:"Kunle",slug:"olobayo-kunle",fullName:"Olobayo Kunle"}],corrections:null},{id:"70548",title:"Studies on the Property and Application of Starch Sugar Ester Dodecenylsuccinic",doi:"10.5772/intechopen.89744",slug:"studies-on-the-property-and-application-of-starch-sugar-ester-dodecenylsuccinic",totalDownloads:601,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"In this study, we have prepared starch and Brown algae sugar ester dodecenylsuccinic, and by using infrared rays, scanning electron microscopy (SEM), and differential scanning calorimetry (DSC), we studied the structures and properties of the starch and Brown algae sugar ester dodecenylsuccinic. In addition, we studied the possibility of using this modified starch and Brown algae as emulsifier that can be used in ice cream.",signatures:"Liu Zhongdong, Liu Boxiang, Wei Guohua, Zhu Xin and Wang Huabin",downloadPdfUrl:"/chapter/pdf-download/70548",previewPdfUrl:"/chapter/pdf-preview/70548",authors:[{id:"56574",title:"Prof.",name:"Liu",surname:"Zhongdong",slug:"liu-zhongdong",fullName:"Liu Zhongdong"},{id:"58697",title:"Mr.",name:"Liu",surname:"Boxiang",slug:"liu-boxiang",fullName:"Liu Boxiang"}],corrections:null},{id:"68437",title:"Chemical Properties of Starch and Its Application in the Food Industry",doi:"10.5772/intechopen.87777",slug:"chemical-properties-of-starch-and-its-application-in-the-food-industry",totalDownloads:4817,totalCrossrefCites:19,totalDimensionsCites:50,hasAltmetrics:0,abstract:"Starch is an important food product and a versatile biomaterial used world-wide for different purposes in many industrial sectors including foods, health, textile, chemical and engineering sector. Starch versatility in industrial applications is largely defined by its physicochemical properties and functionality. Starch in its native form has limited functionality and application. But advancements in biotechnology and chemical technological have led to wide-range modification of starch for different purposes. The objective of this chapter is to examine the different chemical reactions of starch and expose the food applications of the modification products. Several literatures on starch and reaction chemistry including online journals and books were analyzed, harmonized and rationalized. The reactions and mechanisms presented are explained based on the principles of reaction chemistry. Chemical modification of starch is based on the chemical reactivity of the constituent glucose monomers which are polyhydroxyl and can undergo several reactions. Starch can undergo reactions such as hydrolysis, esterification, etherification and oxidation. These reactions give modified starches which can be used in baked foods, confectionaries, soups and salad dressings. This chapter discusses the different chemical reactions of starch, the associated changes in functionality, as well as the applications of chemically modified starches in the food industry.",signatures:"Henry Omoregie Egharevba",downloadPdfUrl:"/chapter/pdf-download/68437",previewPdfUrl:"/chapter/pdf-preview/68437",authors:[{id:"300976",title:"Associate Prof.",name:"Henry",surname:"O. Egharevba",slug:"henry-o.-egharevba",fullName:"Henry O. Egharevba"}],corrections:null},{id:"68410",title:"Application of Starch and Starch Derivatives in Pharmaceutical Formulation",doi:"10.5772/intechopen.88273",slug:"application-of-starch-and-starch-derivatives-in-pharmaceutical-formulation",totalDownloads:1049,totalCrossrefCites:1,totalDimensionsCites:3,hasAltmetrics:0,abstract:"Starch is a homo-glucose unit connected with glycosidic linkage. It is well known for its biodegradability, renewability, low cost, flexibility, and availability. However, to reach its potential in the pharmaceutical application, modification is necessary to solve the problem of solubility, retrogradation, and loss of viscosity. In this chapter, we discuss the different physical, chemical, enzymatic, and biotechnological modifications and their subsequent pharmaceutical application both as an excipient and directly as drug delivery vehicles. Overall, there were different characteristics conferred in a modification which were exploited in pharmaceutics, drug delivery, and antimicrobial preparation. We, however, believe that collation of the data on modification would go a long way toward standardizing the application of the modified products.",signatures:"Christian Chibuogwu, Ben Amadi, Zikora Anyaegbunam, Benjamin Emesiani and Sabinus Ofoefule",downloadPdfUrl:"/chapter/pdf-download/68410",previewPdfUrl:"/chapter/pdf-preview/68410",authors:[{id:"302049",title:"Mr.",name:"Ben",surname:"Amadi",slug:"ben-amadi",fullName:"Ben Amadi"},{id:"302052",title:"Mr.",name:"Christian",surname:"Chibuogwu",slug:"christian-chibuogwu",fullName:"Christian Chibuogwu"},{id:"302053",title:"Ms.",name:"Zikora",surname:"Anyaegbunam",slug:"zikora-anyaegbunam",fullName:"Zikora Anyaegbunam"},{id:"302054",title:"Mr.",name:"Emesiani",surname:"Benjamin",slug:"emesiani-benjamin",fullName:"Emesiani Benjamin"},{id:"302055",title:"Prof.",name:"Ofoefule",surname:"Sabinus",slug:"ofoefule-sabinus",fullName:"Ofoefule Sabinus"}],corrections:null},{id:"68679",title:"Resistant Starch from Exotic Fruit and Its Functional Properties: A Review of Recent Research",doi:"10.5772/intechopen.88816",slug:"resistant-starch-from-exotic-fruit-and-its-functional-properties-a-review-of-recent-research",totalDownloads:934,totalCrossrefCites:0,totalDimensionsCites:1,hasAltmetrics:0,abstract:"Resistant starch is a functional food ingredient that can resist enzymatic digestion in the small intestine and fermentation in large intestine. Resistant starch has many benefits to human health by promoting a balanced blood sugar and beneficial gut bacteria. This review highlighted the sources of different exotic fruit starch, such as banana, jackfruit, cempedak, durian, and breadfruit. The functional properties of these exotic fruit resistant starches were covered in this review. The effect of resistant starch on glycaemic index of food was revealed. This review also discussed on the applications of resistant starch in the production of food products and their effects on food quality. The provided information through the overall review could especially benefit the food industry in producing functional food products with great consumer acceptability.",signatures:"Lee-Hoon Ho and Shi-Yun Wong",downloadPdfUrl:"/chapter/pdf-download/68679",previewPdfUrl:"/chapter/pdf-preview/68679",authors:[{id:"305265",title:"Dr.",name:"Lee Hoon",surname:"Ho",slug:"lee-hoon-ho",fullName:"Lee Hoon Ho"}],corrections:null},{id:"70196",title:"Resistant Starch",doi:"10.5772/intechopen.90159",slug:"resistant-starch",totalDownloads:756,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Not all starch that is ingested into the human body is digested into D-glucose – the portion that defies this process is referred to as resistant starch (RS) where chemically and mechanically, five different forms have been identified. Regardless of the form, an extensive breadth of health benefits has been associated with the consumption of RS. These include the potential of RS becoming part of weight and diabetes management plans as well as improved colon health and prevention of colon cancer. Therefore, in the past decade, there has been a significant amount of research into how RS concentrations can be increased in various food systems, which have had varying degrees of success; however, are limited to either enzymatic, thermal, or acidic alterations to starch. In a similar fashion, chemical methods of RS measurement have also received a considerable amount of change and enhancement over time, though with most of them to some extent attempting to replicate human carbohydrate digestion.",signatures:"William Russell Sullivan",downloadPdfUrl:"/chapter/pdf-download/70196",previewPdfUrl:"/chapter/pdf-preview/70196",authors:[{id:"303498",title:"Dr.",name:"William",surname:"Sullivan",slug:"william-sullivan",fullName:"William Sullivan"}],corrections:null},{id:"68959",title:"Value of Starch in Indian Traditional Food System",doi:"10.5772/intechopen.89086",slug:"value-of-starch-in-indian-traditional-food-system",totalDownloads:685,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"In India, food habit is profoundly influenced by traditions, cultural choices, and religions. For years traditional Indian foods have been prepared, and preparation varies across the country. The wisdom about processing of food, its preservation techniques, and their therapeutic effects has been established for many generations. Starch is the most commonly consumed type of carbohydrate which is found deposited in many crops, such as wheat, corn, rice, and potato, and it serves as the most important source of energy for humans. Starch is classified as complex carbohydrates, and traditionally, complex carbohydrates have been viewed as healthier options. India harbors many plants, out of which traditional starchy tubers and roots which have the potential to be used as sources of flours and starch are also recognized as functional foods because of the presence of functional components such as body-healing chemicals, antioxidants, dietary fibers, and probiotics.",signatures:"Shyamalima Gogoi",downloadPdfUrl:"/chapter/pdf-download/68959",previewPdfUrl:"/chapter/pdf-preview/68959",authors:[{id:"304810",title:"Dr.",name:"Shyamalima",surname:"Gogoi",slug:"shyamalima-gogoi",fullName:"Shyamalima Gogoi"}],corrections:null},{id:"70335",title:"Micrometrics and Morphological Properties of Starch",doi:"10.5772/intechopen.90286",slug:"micrometrics-and-morphological-properties-of-starch",totalDownloads:853,totalCrossrefCites:4,totalDimensionsCites:5,hasAltmetrics:0,abstract:"Starch occurs in form of granules and constitutes a primary manner in which of carbohydrates are stored chiefly in seeds and underground organs and sparingly in other morphological parts such as leaf and bark parts of plants. Grains of transitional starch can be found in the stroma of chloroplast and cytoplasm in leaf parts when exposed to the sun and transferred to organs for storage at dark times. The shape and size, ratio of amylose and amylopectin content of starch grains are peculiar to different biological sources. A literature survey was carried out using various search engines. Journals were searched for using keywords such as microscopy, amylopectin, starch granules etc. The relative qualitative and quantitative properties of starches from various morphological parts of 35 species from 15 families were studied. The qualitative features of shape and size as observed from microscopy were not specific or peculiar to each genus and family as similar shapes and sizes cut across different species. Amylopectin and amylose contents varied considerably among all the species and can be used as one of the means of identification for medicinal plants and the delineation of plant species along with other genetic and physicochemical properties.",signatures:"Omolola Temitope Fatokun",downloadPdfUrl:"/chapter/pdf-download/70335",previewPdfUrl:"/chapter/pdf-preview/70335",authors:[{id:"301098",title:"Mrs.",name:"Omolola",surname:"Fatokun",slug:"omolola-fatokun",fullName:"Omolola Fatokun"}],corrections:null}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},subseries:{id:"15",series:{id:"11",title:"Biochemistry",issn:"2632-0983",editor:{id:"31610",title:"Dr.",name:"Miroslav",middleName:null,surname:"Blumenberg",slug:"miroslav-blumenberg",fullName:"Miroslav Blumenberg",profilePictureURL:"https://mts.intechopen.com/storage/users/31610/images/system/31610.jpg",biography:"Miroslav Blumenberg, Ph.D., was born in Subotica and received his BSc in Belgrade, Yugoslavia. He completed his Ph.D. at MIT in Organic Chemistry; he followed up his Ph.D. with two postdoctoral study periods at Stanford University. Since 1983, he has been a faculty member of the RO Perelman Department of Dermatology, NYU School of Medicine, where he is codirector of a training grant in cutaneous biology. Dr. Blumenberg’s research is focused on the epidermis, expression of keratin genes, transcription profiling, keratinocyte differentiation, inflammatory diseases and cancers, and most recently the effects of the microbiome on the skin. 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\r\n\tGustatory receptor cells housed in taste organs are responsible for processing and coding taste stimuli. These cells constitute a sensory filter for environmental taste signals and transfer information about taste stimuli directly to taste centers in the brain. These cells form the first layer of a decision-making process that ultimately determines whether a food is accepted or rejected by the animal. Similarly, olfactory stimuli play an important role in the orientation of many animals in their environment, including insects. Both invertebrates and vertebrates can detect and discriminate among many odorants that differ in size, shape, and complexity. In many animals, olfaction is the principal sensory modality by which it locates its food sources, mates, and egg-laying sites. For foraging purposes, animals must be able to detect food-related odorants, which may then influence odor-mediated orientation behavior and the discrimination and processing of these odorants in the animal’s brain. This book focuses on the morphology and physiology of both gustatory and olfactory systems in animals, with respect to peripheral chemosensory receptors and their organization, as well as neural circuits and pathways. In addition, clinical and industrial gustatory and olfactory applications and perspectives are discussed.
",isbn:"978-1-83768-302-4",printIsbn:"978-1-83768-301-7",pdfIsbn:"978-1-83768-303-1",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,isSalesforceBook:!1,isNomenclature:!1,hash:"6ee31032ea51909b6995f41e16d254b2",bookSignature:"Dr. Vonnie D.C. Shields",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/12169.jpg",keywords:"Cell Types, Organization, Chemosensory Receptor Cells, Sensory Coding, Multisensory Integration, Chemosensory Association Learning, Gustatory Circuits, Olfactory Circuits, Disorders, Diseases, Flavor and Fragrance, Food and Beverage Industries",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"June 2nd 2022",dateEndSecondStepPublish:"June 30th 2022",dateEndThirdStepPublish:"August 29th 2022",dateEndFourthStepPublish:"November 17th 2022",dateEndFifthStepPublish:"January 16th 2023",dateConfirmationOfParticipation:null,remainingDaysToSecondStep:"a month",secondStepPassed:!0,areRegistrationsClosed:!1,currentStepOfPublishingProcess:3,editedByType:null,kuFlag:!1,biosketch:"Vonnie D.C. Shields, Ph.D., is Associate Dean, Fisher College of Science and Mathematics and a full professor in the Biological Sciences Department, Towson University, Towson, Maryland, USA. Dr. Shields’ research explores gustatory, olfactory, and visual cues in insects.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"82613",title:"Dr.",name:"Vonnie D.C.",middleName:null,surname:"Shields",slug:"vonnie-d.c.-shields",fullName:"Vonnie D.C. Shields",profilePictureURL:"https://mts.intechopen.com/storage/users/82613/images/system/82613.png",biography:"Vonnie D.C. Shields, Ph.D., is Associate Dean, Fisher College of Science and Mathematics and a full professor in the Biological Sciences Department, Towson University, Towson, Maryland, USA. Dr. Shields’ research explores gustatory, olfactory, and visual cues in insects. Her laboratory employs morphological, behavioral, and electrophysiological techniques to better understand sensory mechanisms by which larval and adult insects find host plants and detect plant-associated volatiles. Dr. Shields received a BS and Ph.D. from the University of Regina, Regina, Saskatchewan, Canada. A portion of her Ph.D. studies was carried out at the University of Alberta, Edmonton, Alberta, Canada. After graduating, she accepted a research associate position to conduct postdoctoral studies at the Arizona Research Laboratories Division of Neurobiology, University of Arizona, Tucson, Arizona, USA, before she joined the faculty at Towson University where she rose through the ranks from assistant to full professor.",institutionString:"Towson University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"3",totalChapterViews:"0",totalEditedBooks:"5",institution:{name:"Towson University",institutionURL:null,country:{name:"United States of America"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"18",title:"Neuroscience",slug:"life-sciences-neuroscience"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"466998",firstName:"Dragan",lastName:"Miljak",middleName:"Anton",title:"Mr.",imageUrl:"https://mts.intechopen.com/storage/users/466998/images/21564_n.jpg",email:"dragan@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, copy-editing and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. A unique name with a unique work ethic right at your service."}},relatedBooks:[{type:"book",id:"6048",title:"Insect Physiology and Ecology",subtitle:null,isOpenForSubmission:!1,hash:"741de9c4e0846c950ac20888e4f437c2",slug:"insect-physiology-and-ecology",bookSignature:"Vonnie D.C. Shields",coverURL:"https://cdn.intechopen.com/books/images_new/6048.jpg",editedByType:"Edited by",editors:[{id:"82613",title:"Dr.",name:"Vonnie D.C.",surname:"Shields",slug:"vonnie-d.c.-shields",fullName:"Vonnie D.C. 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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3092",title:"Anopheles mosquitoes",subtitle:"New insights into malaria vectors",isOpenForSubmission:!1,hash:"c9e622485316d5e296288bf24d2b0d64",slug:"anopheles-mosquitoes-new-insights-into-malaria-vectors",bookSignature:"Sylvie Manguin",coverURL:"https://cdn.intechopen.com/books/images_new/3092.jpg",editedByType:"Edited by",editors:[{id:"50017",title:"Prof.",name:"Sylvie",surname:"Manguin",slug:"sylvie-manguin",fullName:"Sylvie Manguin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"57922",title:"Mammalian Cis-Acting RNA Sequence Elements",doi:"10.5772/intechopen.72124",slug:"mammalian-cis-acting-rna-sequence-elements",body:'\nThe control of gene expression is fundamental to mammalian cell life. Although much of this control occurs at the level of transcription, posttranscriptional control is both prevalent and momentous [1]. Work over the past quarter century has resulted in the identification of unifying concepts in posttranscriptional regulation. One unifying concept states that posttranscriptional regulation is mediated by two major molecular components: cis-acting regulatory sequence elements and trans-acting factors. Cis-acting regulatory sequence elements are subsequences contained in the 5′ untranslated region (UTR), 3′ UTR, introns, and coding regions of precursor RNA and mature mRNA that are selectively recognized by a complementary set of one or more trans-acting factors to regulate posttranscriptional gene expression. The lists of conserved cis-elements have been expanding over the past decade, but the mechanisms of the precise assembly of RNA-binding complexes in an orchestrated temporal and spatial manner have not been comprehensively described. Conserved sequences within pre-mRNAs play a major role in determining the mRNA’s configuration, stability, and ultimately the posttranslational fate of protein products. Mammalian pre-mRNAs contain almost as much conserved sequence as that ascribed to transcriptional regulatory elements, and many of these cis-elements can be attributed to known molecular functions, as described in the following paragraphs.
\nTrans-acting factors include RNA-binding proteins (RNA-BPs) and microRNAs (miRNAs), which are able to influence the fate of mRNA by controlling processes such as translation and mRNA degradation (reviewed in Refs. [2, 3, 4, 5]). The combinatorial interplay between RNA-BPs, various miRNAs, and a given mRNA allows for the transcript-specific regulation critical to many cellular decisions during cell division, cell quiescence, or cell senescence [6]. RNA-BP classification is growing and becoming more defined as more structural data become available. Significant progress has been made in defining RNA-binding domains, such as an RNA recognition motif (RRM), zinc fingers, double-stranded RNA-binding domains, K homology domains, pumilio homology domains, and others, that were recently reviewed in [7, 8].
\nIn the pre-genomic era, very few cis-acting RNA sequences had been discovered, for example, AU-rich elements (AREs) in the 3′ UTR of cytokine mRNAs [9]. Advances in genomic methodologies escalated the discoveries and functional identifications of cis-acting sequences. Microarray-based studies that evaluated mRNA stability and translation on a genome-wide basis have provided valuable information about the role of posttranscriptional regulation of a wide variety of transcripts that have an important physiological function [10, 11, 12]. Genome-wide measurements of mRNA decay and bioinformatic sequence motif discovery methods were used to identify the GU-rich element (GRE) as a highly conserved sequence that was enriched in the 3′ UTR and other regions of mRNA transcripts [13]. Various experimental approaches have been developed to understand the functional importance of cis-acting sequence interactions and the network of transcripts that they regulate. One of the most widely used techniques involves immunopurification of specific RNA-binding proteins from cellular extracts followed by a high-throughput analysis of the co-purified RNA species [14]. The coupling of this technique to powerful bioinformatic analysis has led researchers to understand the binding specificity of cis-acting elements [15]. The advent of new technology such as next generation sequencing (NGS) and chemical cross-linking procedures has allowed for fine-scale mapping of cis-binding motifs as well as for the refinement of RNA-binding protein-binding sites. A variety of methods have been developed to identify the
This chapter focuses on mammalian cis-acting regulatory elements that have been recently discovered in different regions of mRNA: preprocessed and mature. First, we summarize recent observations of two large networks of mRNAs that contain conserved AREs or GREs in their pre-mRNA splicing sites, polyadenylation sites, and 3′/5′ UTRs. We outline the known roles for ARE and GRE in regulation of mRNA stability or translation and their role in mammalian cell physiology, with a particular emphasis on their role in the dynamic response toward environmental and developmental signals. Second, we describe advances in the identification of other conserved cis-acting elements and their functional role in different steps of RNA maturation and metabolism. We briefly outline the molecular characteristics of pathological cis-acting sequences raised from gene mutation or transcriptional aberration and overview novel approaches to restore normal gene expression. We conclude with an overview of a concise predictive model of the function of posttranscriptional regulatory networks within different cellular compartments.
\nIt was noted over a quarter of a century ago that mRNAs exhibit substantial variations in turnover rate upon exposure to different cell stimuli [23, 24, 25]. Of the prominent discoveries in the mammalian cis-acting elements field, the AU-rich element was the most notable as it was the most robust determinant of mRNA instability in cytokines and early response genes [26]. Insight into the biological significance and physiological function of ARE as a coordinate regulator of posttranscriptional network was revealed through the experimental identification of ELAVL1 (HuR) and ZNF36 (TTP) proteins [27, 28, 29]. The structure of AREs is defined as a repeating pentamer (AUUUA) with 1 or 2 A to U substitutions [9]. Bioinformatic searches throughout the human transcriptome have provided computational estimation of sequence characteristics and nucleotide lengths of ARE sequences required for mRNA to be unstable [30, 31]. The number of pentamers has an additive effect on mRNA decay and deadenylation processes. AREs are classified into five clusters depending on their sequence content and position of A or U. Cluster I AREs contain up to five copies of AUUUA motifs with a nearby U-rich region and cause synchronous RNA deadenylation [32]. Cluster II AREs are composed of at least two overlapping copies of the AUUUA with an adjacent (U/A) nonamer region and cause asynchronous deadenylation. Clusters III through V AREs were identified to contain more U-rich regions and were rather ‘poorly structured’ (\nTable 1\n), with an inconsistent deadenylation pattern. This classification system has proved to be helpful in understanding the observed behavior and function of ARE-containing transcripts [25].
\nTrans-acting factors | \nFunctional categories | \nARE sequences | \nCluster | \nGRE sequences | \nFunctional categories | \nTrans-acting factors | \n
---|---|---|---|---|---|---|
ELAVL1 ELAVL2 ZFP36 KSRP TIA1, TIAL1 HNRNPC1 HNRNPD GAPDH | \nCytokines, Chemokines Growth factors; Cell signaling; Apoptosis | \n\n | \n\n | \n\n | \nTranscription factors; Cell cycle; Cell metabolism; Cell–cell communication regulators | \nCELF1 CELF2 ELAVL4 RBM38 TARDBP FUS | \n
\n | \n\n | \n\n | \n||||
\n | \n\n | \n\n | \n||||
\n | \n\n | \n\n | \n||||
\n | \n\n | \n\n | \n
Structural and functional comparison of AU-rich and GU-rich elements.
ARE and GRE mRNAs were clustered (with allowance for one mismatch) into five subclasses based on the number of pentameric repeats (AUUUA or GUUUG) and surrounding sequences. W indicates A or U. K indicates G or U. This table was made based on previous publications [33, 47, 74, 75, 77]. ARE- or GRE-containing transcripts in clusters I and II contain four or more overlapping AUUUA or GUUUG pentamers and are each represented by only a few hundred transcripts. Most of the transcripts in these clusters are cytokines, transcription factors, and early response genes. Clusters III through V contain shorter sequences with less sequence repetition and contain up to several thousand members.
Trans-acting factors that bind to ARE (far left column) or GRE (far right column) are: ELAVL1,2,4 (embryonic lethal, abnormal vision)-like 1,2,4; ZFP36, zinc finger protein 36; TIA1, T-cell intracellular antigen 1; TIAL1, TIA1-cytotoxic granule associated RNA-binding protein like 1; KSRP, KH-type splicing regulatory protein; HNRNP C1,D, heterogeneous nuclear ribonucleoprotein C1, D; GAPDH, Glyceraldehyde 3-phosphate dehydrogenase; CELF1,2, CUGBP-ELAV-like family member 1,2; RBM38, RNA-binding protein 38; TARDBP, Tat RNA regulatory element (TAR) DNA-binding protein; FUS, fused in sarcoma.
Genome-wide analyses of mRNA transcript half-lives showed that many labile transcripts contain conserved ARE sequence elements in their 3′ UTRs [21]. Overall, 3′ UTR-ARE-containing transcripts represent approximately 5% of the transcriptome [33]. Human mRNAs encoding cytokines and members of the NFkB cascade are particularly enriched for AREs (\nTable 1\n). AREs play decisive roles in regulating the effects of cytokines on inflammatory responses since mutation of the ARE in cytokines such as TNF-alpha, IFNG, or IRF5 [34] resulted in profound autoimmune-like inflammatory syndrome [35, 36]. In general, transcripts containing functional AREs have short half-lives, although they can be rapidly stabilized in different cell types or stimulation conditions through complex posttranscriptional mechanisms involving trans-acting factors [10, 37]. Numerous trans-binding factors interact with AREs (e.g., ELAVLs, ZFP36, KSRP, TIA1, TIAL1, HRNPC1, and others, which are described in other chapters of this book) and determine the outcomes for harboring ARE transcripts. The majority of these proteins shuttle between the cytoplasm and the nucleus, where they can affect RNA splicing and 3′-end processing, in addition to altering the rate of decay in the cytoplasm [38]. In this respect, it is interesting to note that AREs are also found in intronic regions of pre-mRNAs [39, 40, 41, 42]. This observation leads to the speculation that trans-acting factors could bind ARE in the nucleus and fulfill a function that is different from their cytoplasmic one. Furthermore, a considerable overlap in the binding sites for ARE-BP with other cis-elements, such as GU-rich and poly-U sequences, warrants further investigation since the formation of secondary RNA structure might involve all of the above and subsequently rule the coordinate behavior of RNA-BPs in different cellular compartments or under different cellular stimuli [43, 44, 45].
\nGU-rich elements (GREs) are recognized as essential regulators of mRNA splicing, stability, and translation in mammalian cells [11, 46]. GU-rich containing RNAs represent approximately 8% of transcripts of the human transcriptome [47]. Genome-wide analyses of mRNA decay rates allowed for discovery of non-ARE-containing cohorts of mRNAs that exhibited rapid turnover. Computational
Using whole genome microarrays and high-throughput NGS methodologies, GRE targets have been identified in a number of mammalian cells, for example, resting and activated human T cells, mouse brain cells, and myoblasts or human malignant cell lines [48, 58, 59, 60, 61]. The majority of studies extensively characterized GREs as binding sites located predominantly in 3′ UTRs and caused mRNA decay (or stabilization) depending upon the cellular and environmental context [62]. These UG-rich sequences serve as binding sites for the family of CELF and ELAVL proteins. Interestingly, these two families of RNA-binding proteins share over 80% of sequence conservation within RNA recognition motifs but cause opposite outcomes: the CELF family binding to GRE leads to mRNA degradation, but the ELAVL family function as mRNA stabilizers [63]. In addition, several studies reported that UGU repeat sequences were enriched in introns, with the same frequency as AREs [64, 65]. The authors found significant enrichment of short UG-rich motifs in intronic regions flanking exons, supporting a role for GRE in alternative splicing [66, 67], which activate or repress the splicing of pre-mRNA targets through a competitive binding by MBNL and CELF proteins. This is not surprising, as an estimated 90% of human genes produce alternatively spliced mRNA transcripts [68, 69]. Alignment of the genomic regions adjacent to canonical and alternative polyadenylation sites identified UUCUG and UGUU as conserved cis-elements, which are essential for mRNA maturation and polyadenylation site utilization [70, 71, 72, 73].
\nThus, ARE and GRE can regulate pre-mRNA splicing, translation, and/or mRNA deadenylation or decay depending on the repertoire of proteins they interact with in different intracellular settings. The classification of AREs and GREs has been described in multiple manuscripts [74, 75, 76, 77], and an overview is shown in \nTable 1\n. Single nucleotide polymorphism studies in humans demonstrated that SNPs in ARE and GRE sites are associated with higher risk of human diseases that involve adaptive immune response; mutations in these conserved cis-acting elements resulted in changes in RNA stability and binding preferences for RNA-BPs (reviewed in ref. [44, 63, 78, 79]). The opposing effects of RNA-BP on mRNA turnover may have important implications for the role of posttranscriptional regulation in proliferative diseases such as cancer. Most existing data suggest that the unbalanced expression and function of ARE-BPs appears to drive neoplastic growth and proliferation and contribute to cancer pathogenesis [44, 80]. A definitive causal connection, that is clinically relevant to human pathology, has not yet been demonstrated.
\nThe addition and removal of the poly(A) tail are the rate-limiting steps of maturation and degradation processes that the majority of mammalian mRNAs undergo [81, 82, 83]. Two tightly coupled reactions – cleavage and polyadenylation – involve a large number of protein components. Alternative polyadenylation of RNA is a posttranscriptional modification that plays an important role in gene expression, as it produces mRNAs that share the same coding region, but differ in their 3′ UTRs. This process is highly tissue specific and results in the generation of alternative mRNA isoforms with different stability rates and translational efficiency and even subcellular localization [84, 85, 86]. In mammals, the poly(A) cleavage/polyadenylation site is composed of three sets of consensus cis-elements: the highly conserved AAUAAA hexamer and less conserved U/GU-rich and UGUA elements. A bioinformatics analysis showed that an overwhelming majority of mammalian mRNAs harbor a conserved AAUAAA or a close canonical variant, AUUAAA, sequences [87, 88]. Flanking sequences are very important for the poly(A) site to function [89]. For example, two downstream U/GU-rich regions are both necessary for binding of the specific cleavage polyadenylation complex [90, 91]. A number of trans-binding factors regulate poly(A) site utilization and the efficiency of pre-mRNA processing in the nucleus, including five large families of CPSF, HNRNP, CF, MBNL, and CSTF proteins as well as snoRNAs [92, 93, 94, 95]. These families have opposing effects on polyadenylation site utilization in nascent RNAs, determining the final pool of mature mRNA isoforms and subsequent choreography and activity of trans-binding factors in the cytoplasm (reviewed in [96, 97]). Immediately after cleavage, poly(A) polymerases (PAPs) promote lengthening of the poly(A) tail, completing the mRNA maturation process [98, 99]. Genome-wide polyadenylation site (PAS) analysis in mammalian cells identified a great diversity of PAS utilization in different tissues and organs [73, 100]. Mutations can cause the loss of the canonical adenylation signal and subsequent switch to alternative PAS utilization [101].
\nAnother conserved regulatory cis-element is the cytoplasmic polyadenylation element (CPE). Many mammalian RNAs contain a CPE, a UUUUA/U sequence, located in the 3′ UTR. The CPE serves as a binding site for cytoplasmic polyadenylation element-binding (CPEBs) proteins 1–4 [102]. The most obtrusive differences in the CPE usage have been described under conditions of stress [103].
\nThe nuclear poly(A)-binding proteins (PABPs) act as poly(A) keepers during the mRNA processing through first binding to newly added (A)12 nucleotides and allowing the poly(A) tail to grow up to 250 nucleotides before the mRNA is exported into the cytoplasm [104, 105]. In the cytoplasm, the poly(A) tail acts as a cis-regulatory element and mediates mRNA translation. Recently developed methodologies make it affordable to count differentially polyadenylated mRNAs and assess the length of the poly(A) tail [106, 107, 108]. In somatic cells, mRNA deadenylation can lead to the degradation or stabilization of translationally silent transcripts; however, the importance of the poly(A) tail length in these processes is currently under scrutiny as there is an evidence that the translation is regulated independently of their poly(A) tail length in the somatic cell cycle [109]. As for embryonic developmental processes, translationally repressed mRNAs can be reactivated by cytoplasmic poly(A) tail elongation at the precise time when their encoded proteins are needed to be translated [108, 110].
\nA number of ARE-like transcripts have been identified in several mammalian systems to regulate important posttranscriptional networks of gene expression.
\nPoly (U) sequences are the third most conserved cis-element after ARE and GRE, which have been recently found within sequence composition at cross-link nucleotides site using the CLIP assay [111]. Frequencies of poly(U) are most highly enriched for UUUUU pentanucleotides. The HNRNPC and HNRNPD (AUF1) can recognize and bind to U sequences in pre-mRNAs, mature mRNAs, and non-coding RNAs and influence target transcript diversity in the nucleus through pre-mRNA splicing and the stability in the cytoplasm [41]. It is interesting to note that clusters V of ARE and GRE elements (see \nTable 1\n) include hundreds of mRNAs harboring U-pentanucleotides in the 3′ UTR, suggesting that CELF and ELAVL families can also bind to poly(U) tracts under certain conditions, perhaps with lower affinity [112].
\nUridylation is an independent biochemical process that is facilitated by uridylation enzymes such as ZCCHC11 and ZCCHC6. In mammalian cells, uridylation readily occurs on deadenylated mRNAs through the recognition of short poly(A) tails (<25 nt). Protein PABPC1 antagonizes uridylation of polyadenylated mRNAs, contributing to changes in mRNA half-lives [113]. MicroRNA can also induce uridylation of its targets; however, selectivity of mRNA uridylation has not been decisively demonstrated. The development of novel methods, such as TAIL-Seq, allows for genome-wide discovery of alternative mRNA tailing processes such as uridylation and guanylation at downstream sites of shortened poly(A) tails [114]. Dynamic control of mRNA tailing is implicated in turnover and translational control and is fundamental for early embryonic development [115].
\nGC-rich sequences were also found to be conserved in coding and non-coding regions of mammalian mRNAs. Classified as GC-rich elements (GCREs), these were identified in NCL (nucleolin), PCBP1 and UPF protein-binding complexes [116]. GCREs regulate mRNA stability, decay, and translational efficiency [117]. Several lines of evidence establish primary function for GCRE as regulators of mRNA transcription [118].
\nThe CU-rich element (CURE) is a target for several RNA- or DNA-binding proteins, for example, PCBP1 [119] and PTBP1 [120, 121] and regulates gene expression via a broad, but poorly defined spectrum of posttranslational mechanisms.
\nOligonucleotides (T/C)nGGG/G from four separate strands can be folded into stacked tertiary structures known as G-quadruplexes, forming polymorphic loops of three G-quartet layers with four G-tracts [122, 123, 124]. Folded G-structures (Gs)2–7 are found in 3′ and 5′ UTRs, but are very rare in coding and intergenic regions, and could influence all aspects of RNA metabolism [125, 126]. Studies have shown that 3′ UTR G-quadruplexes can bind more than two dozen proteins that interact with the Gs structure and serve as regulators of transcription, splicing, processing, localization, and stability and have been recently discussed in excellent reviews [127, 128]. Moreover, bioinformatics and computational scans have shown the prevalence of intermolecular DNA–RNA G-quadruplexes and (Gs)4 pairing with miRNA in mammalian cells [129, 130]. These observations imply almost endless possibilities of intermolecular interactions, which undoubtedly would have significant impact on our understanding of transcriptional and posttranscriptional gene expression and regulation in mammalian cells.
\nInternal ribosome entry sites (IRESs) are heterogeneous cis-acting regulatory elements located primarily in 5′ untranslated regions of mammalian mRNAs. IRESs facilitate alternative mRNA translation, skipping the need for the m7GpppN cap structure and many translation initiation trans-acting factors in the recognition process of the translation initiation codon (e.g., AUG) by ribosomal subunits [131]. Since the length of IRES can be several hundred nucleotides long, it was difficult to identify IRES’ structural elements that are important for the common secondary structures or functions [132, 133]. In depth sequence scans through the human transcriptome identified a variety of poly-U, poly-A, and CU-rich
Pumilio response element (PRE) is another cis-element that is well defined in nonmammalian systems. A consensus 5′- UGUANAUA was derived from gel shift, RIP, PAR-CLIP, and crystal structure approaches [137]. It is present in almost 3000 mammalian mRNAs and serves as a cis-element for the PUM family of proteins [138, 139]. PUMs exert two modes of mRNA translational repression: deadenylation-mediated repression and a deadenylation-independent mechanism [140].
\nAnother novel 3′ UTR motif (UAAC/GUUAU) is also prevalent (7% of mammalian 3′ UTRs contain one or more copies) and has strong species conservation [141]. This motif is a binding target for HNRNP A2/B1 and A1 and is involved in mRNA deadenylation. A fundamental role of UAAC/GUUAU and similar elements as regulators of the mammalian mRNA translational activation or repression is yet to be demonstrated [142].
\nMapping mammalian pre-mRNA positional enrichment of short intronic splicing regulatory elements (ISREs) is another example of the identification of cis-acting elements that are most important for pre-mRNA splicing.
MicroRNAs are conserved regulatory sequences that pervasively act, in trans, toward mRNA. miRNA-binding sites are important regulators of mRNA half-life and activity. The majority of miRNAs influence mRNA life span through biochemical interactions with mRNA and/or RNA-BPs [149]. This could be achieved through direct competition for a shared binding site or through remodeling of the mRNA structure to favor (or impede) miRNA association nearby [150]. In support of this, a recent bioinformatics analysis determined that UUUGUUU motifs, which bear an uncanny resemblance to GRE-binding sites, are enriched in the adjacent to many miRNA-binding sites, and their presence tends to augment miRNA activity [151]. On the other hand, any miRNA that contains a UGUKUGU or UAUKUAU seed sequences (K represents G or U) could in theory bind and occlude GRE-BP- or ARE-BP-binding motifs, which prevent any interaction with cis-elements within mRNA. For example, the mir-122 interaction with CELF1 has been demonstrated, proposing that CELF1 can play a role in the degradation of GRE-containing miRNAs [152]. It has been computed that the proximity of RNA-BP-binding sites and residues pairing to miRNA can quantitatively predict mRNA cis-element performance for several intensely studied RNA-BPs and miRNAs [153, 154, 155]. Although mechanistic details of interplay between cis-acting elements, RNA-BPs, and miRNAs are understudied, they perhaps should be a high priority, given recent observations that miRNA expression and/or processing are affected in many human diseases and disorders [156, 157, 158]. Significant progress has been made by bioinformaticians and biologists to better understand system biology of the RNA life cycle; several useful metadata hubs were created, which incorporate existing experimental data and computational approaches [159, 160]. The comprehensive list of available software and websites has been recently reviewed in Ref. [161]. However, we are still far from having a comprehensive understanding of mechanisms of RNA biogenesis and its relevance in physiological and pathological conditions.
\nThe human genome contains a large number of short repetitive sequences that are prone to higher than average mutation rates and transcriptional errors [162], which can engender a tandem repeat expansion in cis-acting elements of 3′ or 5′ UTR, introns, or coding regions, and cause a large variety of inherited human diseases. For example, endogenous nucleotide repeat expansions are implicated in many human autosomal dominant diseases and have emerged as new groups of repeat expansion disorder associated with tri- or pentanucleotide repeat expansion pathogenesis. Pathological repeats can elicit toxicity that is triggered by toxic RNA or abnormally translated protein dipeptide or homopolymeric peptides [163]. Disorders as such include, but are not limited to the following conditions:
Spinocerebellar ataxia (SCAs types 1–37) is the largest and the most diverse group of inherited neurological diseases in which neurological dysfunction is driven by defects known as ataxias. Several mutations in tandem repeat expansions were discovered, including coding (CAG)n mutations in SCA1, 2, 3, 6, 7, and 17 genes; non-coding (CTG)n in
Myotonic dystrophies (DM), where (DM1) is associated with >300 CUG, repeats in the DMPK mRNA; and (DM2) – with >CCUG repeats in ZF9 mRNA [165].
Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia are associated with GGGGCC/CCCCGG repeat expansion in the non-coding region of the C9orf72 (C9ALS/FTD) gene [166].
Huntington’s disease is caused by CAG expansion repeats in the HTT gene [167];
Fragile X syndrome (FXS) arises when the FMR1 gene reach <230 CGG repeats.
Fragile X-associated tremor/ataxia syndrome (FXTAS) is associated with CGG/CCG repeat expansion in the fragile X gene, FMR1 [168].
Molecular pathogenesis of endogenous nucleotide repeat expansion diseases is complicated and pertained to the presence of
An interesting common aspect of these pathologies is that they are caused by mutated cis-elements and are often produced through bidirectional transcription. Resultant toxic RNA causes intracellular stress and sequestration of RNA-BPs toward expanded sequence repeats [171], which changes the biochemistry of posttranscriptional regulatory networks in affected tissues. The abovementioned diseases represent an incomplete list of a growing number of disorders that can potentially have similar therapeutic opportunities. The recently developed ‘base editor’ CRISPR-Cas9 methodology has demonstrated a high power of nucleotide-level precision editing, making this approach suitable for repeat excision as genetic therapies for the above listed conditions [172] and may also correct many other RNA pathologies, for example, those driven by nonsense-mediated mRNA decay [173].
\nmRNA molecules move through different cellular compartments within messenger ribonucleoprotein (mRNP) complexes in dynamic association with RNA-binding proteins that bind to conserved cis-elements shared by subsets of transcripts [174]. The association of specific trans-binding factors with conserved regulatory cis-elements shared by subsets of mRNAs coordinates the fate of these bound transcripts through posttranscriptional processes such as splicing, intracellular localization, translation, storage, or mRNA decay [175, 176]. Not surprisingly, very few transcripts have only one type of regulatory element. Focusing on individual scenarios, we built a concise predictive model of higher-order complexes that can be formed simultaneously within different cellular compartments, starting in from the nucleus and moving into the cytoplasm.
Regulation of splicing by cis-elements (\nFigure 1A\n):
The cis-elements within precursor RNA are catalyzed by different components of the spliceosome during constitutive splicing events [177]. Binding by RNA-BP to short intronic splicing regulatory elements (ISREs) regulates exon inclusion or exon skipping during stage-specific constitutive splicing transitions, in a position-dependent manner [67]. These processes are orchestrated by biochemical recognition and binding on a competitive basis by a family of U proteins that compose the spliceosome.
RNA-BPs also bind to multivalent intronic sequences in precursor mRNA and regulate the alternative splicing (e.g., exon skipping, alternative splice site retention, or intron retention). Alternatively-spliced transcripts may contain different 3′ or 5′ UTRs that can be subject to differential translational regulation of mature transcripts. An important regulators of alternative splicing efficiency are PTBP, SR, RBM, and HNRNP families of proteins and snRNAs. The use of alternative exons leads to the production of transcripts with different open reading frames (ORFs) and diversifies the repertoire of encoded proteins, giving rise to protein isoforms with alternative N- and C- termini.
Regulation of adenylation by cis-acting elements (\nFigure 1B\n):
Alternative polyadenylation (APA) occurs in a tandem manner with splicing. Many splicing factors are also 3′-end processing factors within the mRNA 3′-end cleavage and polyadenylation (CPA) complexes. The recognition of cis-elements upstream of canonical or alternative PAS serves as a docking site for specific RNA-binding proteins (e.g., CPSF, CF, CSTFs, HNRNPs, MBNL, and CPEB), which in turn recruit canonical poly(A) polymerases (PAPOL). The CPA complex requires stabilization by a downstream GU/GC-rich sequence element (DSE) and its interaction with the CPSF-processing factors. The upstream sequence element (USE) is U-rich and serves an auxiliary role, binding to CF and PAPOL, and also stabilizes the cleavage complex.
The cleavage and polyadenylation specific factor (CPSF) binds weaker noncanonical polyadenylation (AUUAAA) signals and cuts at the proximal polyadenylation site (PAS). The utilization of distal canonical PAS results in the processing of the full mature transcript. Cleavage at the proximal PAS leads to shortening of the 3′ untranslated region and loss of regulatory sequences within the 3′ UTR (e.g., ARE or GRE or miRNA-binding sites). MBNL can mask the region upstream of weak noncanonical PA signals, blocking the binding of cleavage factor I (CF).
The CPEB1 protein binds the cytoplasmic polyadenylation element (CPE, consensus sequence 5′-UUUUUAU -3′) located upstream of non-canonical PA signals within the mRNA and shuttles it into the cytoplasm. The cytoplasmic CPEB1-CPE complex recruits poly(A) polymerase (PAP), which promotes the lengthening of the poly(A) tail and increases translation efficiency. The greater the distance between CPE and poly(A) tails of transcripts, the weaker the rate of adenylation.
Regulation of
Most eukaryotic mRNAs are translated by the cap-dependent mechanism, which requires recognition of the cap structure (m7GpppN) at the 5′ end by early initiation factor complexes (eIFs). EIFs recruit ribosomal subunits and initiator Met-tRNA and scan along the 5′ UTR of the mRNA to reach the start codon (an AUG triplet). During the scanning, the secondary RNA structure unwinds in an ATP-dependent manner. The 5′ UTR is rich in GC-content and is prone to folding into secondary structures, which may hinder ribosomal assembly [178]. Hairpin loops as secondary structure regulatory elements were described only for a handful of mRNAs, and their role in genome-wide translation is not known. A combination of new ribo-sequencing with fluorescent visualization might shed light on the role of hairpin loops in translation in the near future [179, 180, 181, 182]. Other internal 5′ UTR cis-element structures are AREs and GREs. Their effects on translation are mediated by a combination of RNA-BPs. They are often found to be part of hairpin loops. Visualizing a folded hairpin structure
The translation initiation via internal ribosomal entry site (IRES) occurs in a cap-independent manner. Mammalian IRES facilitates bypassing of the eIF4E-m7GpppN cap interaction and recruitment of the small and large ribosomal subunits and tRNA to the transcript, initiating translation at the canonical AUG start codon.
G-quadruplexes within/near IRES may potentiate alternative translation. However, G4 structures in 3′ or 5′ UTRs and an open reading frame mainly repress cap-dependent translation (reviewed in Ref. [183]).
The poly(A) tail also plays a role in translation as an mRNA stabilizer and a facilitator of mRNA circularization, which promotes translation. De-adenylation processes tend to slowdown the translation rate and eventually lead to mRNA degradation.
Regulation of mRNA stabilization or decay by cis-acting elements (\nFigure 1D\n):
In mammalian cells, mRNA stabilization or decay is regulated by cis-elements in the 3′ UTR. Numerous known RNA-BPs serve as trans-binding factors for ARE/GRE and other elements to facilitate transcript deadenylation and subsequent decay by exonucleases. There are also a number of RNA-BPs with the opposite function, which stabilize and promote mRNA translation. Posttranslational alteration of RNA-BPs (particularly within RNA-binding domains) can lead them to dissociate from RNA-binding complexes, and be replaced by other competitors, thereby contributing to mRNA de/stabilization [76]. A fine-tuned balance must be reached in cells for proper function at the organismal level.
Interplay between mRNA, miRNA and RNA-BPs (\nFigure 1E\n):
The estimates on how different miRNA and mRNA are loaded into the RNA-BP-bound RISC (RNA-induced silencing complex) were derived from CLIP assays results [184, 185, 186]. Several scenarios are possible to extract from these: If both miRNA and RNA-BP are bound to the 3′ UTR of mRNA, they will be sufficiently close to each other and the complex can be identified by CLIP. They would work cooperatively to promote the assembly of decay machinery. Independent binding by a competitor RNA-BP might disrupt this complex. The strength of miRNA-mRNA canonical and noncanonical bond formation can be computed to project possible biochemical outcomes [187, 188, 189].
The mRNA 3′ UTR length and secondary structure formation can greatly influence both miRNA and RNA-BP-binding efficiency; it can also disrupt or assuage the assembly of RNA-BP complexes by providing high affinity or multioccupancy binding sites. The outcomes of this scenario could be anywhere from marginal translational repression to accelerated mRNA degradation.
Cis-acting sequences within miRNAs that resemble cis-elements (ARE or GRE) have perfect complementarity to RNA-BP’s RNA-recognition motifs (RRMs). They can, in theory, occlude RRM-binding sites, acting as alternative inhibitors of RNA-BP activity. This could potentiate (or hinder) translational repression and mRNA degradation of target mRNA, depending on which RNA-BP was affected.
Predictive scenarios of cis-element effects and trans-binding factors behavior on mRNA splicing, adenylation, translation, and decay. Blunt arrows indicate direct suppression; arrows represent activation. These figures are made by using the ingenuity pathway analysis software based upon the observations from previous studies or suggested regulatory mechanisms. A. Consensus multivalent sequences represent the intronic splice sites that are recognized by a family of small nuclear ribonucleoproteins (U snRNPs). These regulatory cis-elements can be divided into two types: (1) intronic regions which almost always begin with the dinucleotide GU and end with AG; and (2) intronic regions which have either AU and AC termini or GU and AG termini. Introns are also rich with pyrimidine nucleotides that cumulatively compose a pyrimidine binding tract, which also have a unique poly(A) branch point sequence upstream. Of the other four types of cis-acting elements: two are located within exons (exonic splicing enhancers, ESEs, and exonic splicing silencers, ESSs), and two are located within introns (intronic splicing enhancers, ISEs, and intronic splicing silencers, ISSs). The key trans-acting splicing factors are shown: SR, serine/arginine-rich (SR) proteins; U1 small nuclear ribonucleoproteins (U1 snRNPs); HNRNPs, heterogeneous nuclear ribonucleoproteins; PTB, polypyrimidine tract binding protein. B. Adenylation of pre-mRNA is triggered by cis-regulatory sequences named poly(A) signals: AAUAAA or/and AUUAAA; the U/GU-rich and UGUA elements. By direct analogy to splicing, canonical adenylation is regulated by RNA-BPs or snRNAs. CF, cleavage factor; CSTF, cleavage stimulation factor; CPSF, cleavage polyadenylation specificity factor; MBNL, muscle blind like protein; PAP, poly(A) polymerase; PABP, poly(A) binding protein; CPEB, cytoplasmic polyadenylation element binding protein; miRNA BS, miRNA binding sites; S RNA-BP, stabilizing RNA-binding protein; D RNA-BP, destabilizing RNA-binding protein; CPA, cleavage polyadenylation assembly; CPE, cytoplasmic polyadenylation element. C. Cis-mediated regulation of canonical and alternative translation includes sequences in all parts of mRNA. In canonical translation, the initiation factors (RNA-BPs) bind the 5′ m7GpppN cap, and then linearly scan through the 5′ UTR until reaching an AUG start codon. For simplicity, the components of the translation machinery are shown as eIF2 and eIFs (eukaryotic early translation initiation factors). PABP, poly(A) binding protein; IRES, internal ribosomal entry site; P, phosphorylation of RNA-BP. D. Schematic illustration of the cytoplasmic mRNA decay complex formation. The details for this scenario are provided in the text. S RNA-BP, stabilizing RNA-binding proteins; D RNA-BP, destabilizing RNA-binding proteins; PABP, poly(A)-binding protein; eIF2 and eIFs, eukaryotic early translation initiation factors. E. Scenarios for miRNA mediated mRNA translational repression or decay pathways. The details for this scenario are provided in the text. RISC, RNA-induced silencing complex; P, phosphorylation of RNA-BP.
Examples given in this chapter suggest that mRNA regulation is important in multiple aspects of mammalian biology; however, it is largely unknown how the combinatorial regulation is achieved at the biological complexity of the organisms. Transcriptome-wide mapping of cis-elements and trans-binding sites demonstrates huge regulatory potentials for non-coding parts of mRNA. The more details we learn about cross-talk, molecular assembly, and compartmentalization of RNA-protein complexes, the more unifying principles we may find. Understanding of the factors and elements involved in the regulation of a particular gene expression in a single cell [190] is of paramount importance when designing molecular therapies or when attempting to modulate the expression of a target gene. Thus, scientists and geneticists have exciting opportunities ahead in the field of therapeutic genome editing.
\nThis work is supported by University of Minnesota department of Medicine start-up fund to I. V-S. We acknowledge the University of Minnesota Supercomputing Institute for providing the access to Ingenuity Pathway Assistant.
\nNone declared.
3′ UTR | 3′ untranslated region |
ARE | AU-rich element adenylate(A)- and uridylate(U)-rich element |
DMPK | Dystrophia myotonica protein kinase |
GRE | GU-rich element, guanidine(G)- and uridylate(U)-rich element |
m7GpppN cap | 7-Methylguanosine cap |
Met-tRNA | Methionine loaded onto transfer RNA |
NFkB | Nuclear factor kappa-light chain enhancer of activated B cells |
PTBP | Polypyrimidine tract binding protein |
RRM | RNA-recognition motif |
SRSF1 | Serine/arginine-rich splicing factor |
UPF1 | Up-frameshift protein 1 |
Conformal antenna arrays are beneficial for applications that need an antenna to be placed on a non-flat surface, for example, on the fuselage of a UAV/airplane in the aerospace industry [1, 2, 3], implantable sensors in wearable networks [4, 5, 6, 7, 8], and satellite communications [9, 10, 11]. One of the main advantages of using conformal antenna is its structural integration ability on singly curved (e.g., a wedge/cylinder) [12, 13, 14, 15] and doubly curved (like a sphere) surfaces [16]. This can be very useful in applications where using definite flat surface may not be a practical design choice. Another exciting application of conformal antenna array is at the base station in a cellular mobile communication system. Today, mobile service providers are utilizing three separate antenna panels (dipole or monopole array) in a cell for a 120° sector coverage. What about, if one cylindrical array is used instead of three dipole arrays [17]? This can result in a much smaller transmitter requirement with 360° azimuthal coverage plus reduced base station size at a lower cost (specifically beneficial in crowded residential areas where cellular companies have to rent the space for base station installation).
On the other hand, these curved surfaces may be subjected to intentional (e.g., flexing wings of a UAV/aircraft) and/or unintentional (bending of aircraft wings due to severe weather conditions/vibrations) forces that change the shape of the surface [12]. As a result, the radiation pattern of the conformal antenna array is changed as shown in Figure 1. The results in [18] indicate that directivity of conformal antenna array can be reduced by 5–15 dB. In the literature, various methods have been proposed to compensate the reduction in directivity and to improve/correct the radiation pattern of a conformal antenna array. In [1, 2, 3, 11, 19, 20, 21], mechanical calibration techniques have been used to steer the main beam on a conformal surface in the desired direction. In [12, 13, 15, 16, 22, 23, 24, 25], projection method of [26] is used to correct the main beam direction of a deformed/flex surface. In [27, 28, 29, 30], various optimization algorithms have been used to control the radiation pattern of conformal antenna arrays. In summary, it has been shown that the radiation pattern of a conformal antenna array can be improved with different calibration techniques, signal processing algorithms, sensor circuitry, and phase and amplitude adjustments.
Array on a conformal surface.
This chapter will focus on phase compensation of four-element conformal cylindrical antenna array using (1) projection method and (2) convex optimization method. First, a brief introduction and working principle of phase compensation is presented using projection method. Then, array factor expression will be derived to compensate the radiation pattern of conformal cylindrical array. Then, the convex optimization algorithm will be discussed to compute the array weights for pattern recovery of conformal cylindrical array. Then, compensated gain using both the methods will be compared to linear flat array to explore the gain limitations of these compensated techniques for conformal antenna arrays. Finally, conclusion and future work are presented.
The projection method in [26] and its further exploration in [12, 15, 22] are adopted here to describe the behavior of the conformal antenna array shown in Figure 2. For discussion, consider the problem where the flat antenna array is placed on the singly curved surface shaped as a cylinder with radius r as shown in Figure 2. The position of each antenna element on the cylinder is represented as
Phase compensation of a conformal cylindrical antenna array.
To compute this compensated phase, the antenna elements are projected on the reference plane and then the distances from antenna elements on cylindrical surface (shown as black dots) to the projected elements on the reference plane (shown as dashed circles) are calculated. Suppose
The distance from the antenna elements on the cylinder to the projected elements on the reference plane can be computed using:
where
The required compensated phase to correct the broadside radiation pattern of a conformal cylindrical antenna array in Figure 2 is then given by:
where
To analytically compute the corrected (compensated) radiation pattern and validate with simulation results, the following compensated array factor
where
where
For this work, the phase difference
The broadside gain maximization problem of a conformal antenna array in Figure 2 can be formulated as a linear constrained quadratic programming problem [32], i.e.,
where
(a) 3D plot of the objective function plotted as a function of real
Iterative optimization algorithms are normally adopted to find this minimum. Although second-order Newton method is able to find the solution in fewer steps, it requires evaluation of complex quadratic norm defined as the Hessian matrix
where
To analytically compute the corrected (compensated) radiation pattern and validate with simulation results, the compensated array factor
The four-element microstrip patch antenna array on a cylindrical surface with radius
Parameter | Projection method | Convex optimization | |
---|---|---|---|
8 | [121.67,0,0,121.67] | [−89.49,146.95,146.95,-89.49] | |
6.17 | 6.17 | ||
0.8 | 0.8 | ||
10 | [101.84,0,0,101.84] | [−170.44,85.95,85.95,−170.44] | |
4 | |||
0.53 | |||
12 | [86.95,0,0,86.95] | [114.61,26.05,26.05,114.61] | |
2.74 | |||
0.4 | |||
15 | [70.95,0,0,70.95] | [9.66,−62.66,−62.66,9.66] | |
1.765 | |||
0.24 | |||
30 | [36.42,0,0,36.42] | [−102.2,−139.3,−139.3,−102.2] | |
0.5 | |||
0 |
Computed parameters of conformal cylindrical array for various radii of curvatures.
(a) Analytical results for phase compensation of a conformal cylindrical antenna array with
When radii of curvatures of cylindrical surface array increase (less deformation), both the projection and convex optimization (phase correction only) methods recover the broadside radiation pattern with decreasing gap between corrected and uncorrected gains as shown in Figures 5
(a) Analytical results for phase compensation of a conformal cylindrical antenna array with
(a) Analytical results for phase compensation of a conformal cylindrical antenna array with
(a) Analytical results for phase compensation of a conformal cylindrical antenna array with
In the limiting case, when the radius of curvature of conformal cylindrical array increases up to 30 cm and above (approaching flat array), the compensated gains achieved from both projection and convex optimization methods nearly reaches the linear flat array gain, which is demonstrated in Figure 8 and is shown in Table 1.
(a) Analytical results for phase compensation of a conformal cylindrical antenna array with
In this chapter, phase compensation techniques based on projection method and convex optimization (phase correction only) have been discussed for recovery of broadside radiation pattern on a conformal cylindrical-shaped antenna array. The compensated gains of both the methods have been compared with linear flat antenna array. It is shown that the maximum broadside gain recovered with both the methods is less than the linear antenna array for severe deformation cases and approaches the gain of linear antenna array for less conformal deformation surfaces. The analytical expressions and convex optimization algorithm used can be used by a designer to predict the maximum possible compensated gain of conformal antenna array.
The proposed techniques can be extended for broadside pattern correction of conformal antenna arrays on other deformed surfaces (spherical nose of plane, flexing wings of UAV, etc.). Another interesting research can be to extend these techniques for beamforming on conformal deformed surfaces (e.g., on base station/tower of cellular companies) to improve the signal-to-noise ratio (SNR) and its capacity. In this work, convex optimization is used to compute the compensated phases (with uniform amplitudes constraint) for recovery of broadside radiation pattern only. In practice, the technique is robust and can be used to calculate complex weights (amplitude tapering as well as phase correction), which can be further explored for beamforming applications and side lobe level control of conformal antenna arrays.
This work is supported by Ignite (NTF), Ministry of IT & Telecom, Government of Pakistan via project no. ICTRDF/TR&D/2015/04.
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Saxena",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRET3QAO/Profile_Picture_2022-05-10T10:10:26.jpeg",institutionString:"King George's Medical University",institution:{name:"King George's Medical University",institutionURL:null,country:{name:"India"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null}]},subseriesFiltersForPublishedBooks:[{group:"subseries",caption:"Bacterial Infectious Diseases",value:3,count:2},{group:"subseries",caption:"Parasitic Infectious Diseases",value:5,count:4},{group:"subseries",caption:"Viral Infectious Diseases",value:6,count:7}],publicationYearFilters:[{group:"publicationYear",caption:"2022",value:2022,count:2},{group:"publicationYear",caption:"2021",value:2021,count:4},{group:"publicationYear",caption:"2020",value:2020,count:3},{group:"publicationYear",caption:"2019",value:2019,count:3},{group:"publicationYear",caption:"2018",value:2018,count:1}],authors:{paginationCount:229,paginationItems:[{id:"318170",title:"Dr.",name:"Aneesa",middleName:null,surname:"Moolla",slug:"aneesa-moolla",fullName:"Aneesa Moolla",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/318170/images/system/318170.png",biography:"Dr. Aneesa Moolla has extensive experience in the diverse fields of health care having previously worked in dental private practice, at the Red Cross Flying Doctors association, and in healthcare corporate settings. She is now a lecturer at the University of Witwatersrand, South Africa, and a principal researcher at the Health Economics and Epidemiology Research Office (HE2RO), South Africa. Dr. Moolla holds a Ph.D. in Psychology with her research being focused on mental health and resilience. In her professional work capacity, her research has further expanded into the fields of early childhood development, mental health, the HIV and TB care cascades, as well as COVID. She is also a UNESCO-trained International Bioethics Facilitator.",institutionString:"University of the Witwatersrand",institution:{name:"University of the Witwatersrand",country:{name:"South Africa"}}},{id:"419588",title:"Ph.D.",name:"Sergio",middleName:"Alexandre",surname:"Gehrke",slug:"sergio-gehrke",fullName:"Sergio Gehrke",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000038WgMKQA0/Profile_Picture_2022-06-02T11:44:20.jpg",biography:"Dr. Sergio Alexandre Gehrke is a doctorate holder in two fields. The first is a Ph.D. in Cellular and Molecular Biology from the Pontificia Catholic University, Porto Alegre, Brazil, in 2010 and the other is an International Ph.D. in Bioengineering from the Universidad Miguel Hernandez, Elche/Alicante, Spain, obtained in 2020. In 2018, he completed a postdoctoral fellowship in Materials Engineering in the NUCLEMAT of the Pontificia Catholic University, Porto Alegre, Brazil. He is currently the Director of the Postgraduate Program in Implantology of the Bioface/UCAM/PgO (Montevideo, Uruguay), Director of the Cathedra of Biotechnology of the Catholic University of Murcia (Murcia, Spain), an Extraordinary Full Professor of the Catholic University of Murcia (Murcia, Spain) as well as the Director of the private center of research Biotecnos – Technology and Science (Montevideo, Uruguay). Applied biomaterials, cellular and molecular biology, and dental implants are among his research interests. He has published several original papers in renowned journals. In addition, he is also a Collaborating Professor in several Postgraduate programs at different universities all over the world.",institutionString:null,institution:{name:"Universidad Católica San Antonio de Murcia",country:{name:"Spain"}}},{id:"342152",title:"Dr.",name:"Santo",middleName:null,surname:"Grace Umesh",slug:"santo-grace-umesh",fullName:"Santo Grace Umesh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/342152/images/16311_n.jpg",biography:null,institutionString:null,institution:{name:"SRM Dental College",country:{name:"India"}}},{id:"333647",title:"Dr.",name:"Shreya",middleName:null,surname:"Kishore",slug:"shreya-kishore",fullName:"Shreya Kishore",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/333647/images/14701_n.jpg",biography:"Dr. Shreya Kishore completed her Bachelor in Dental Surgery in Chettinad Dental College and Research Institute, Chennai, and her Master of Dental Surgery (Orthodontics) in Saveetha Dental College, Chennai. She is also Invisalign certified. She’s working as a Senior Lecturer in the Department of Orthodontics, SRM Dental College since November 2019. She is actively involved in teaching orthodontics to the undergraduates and the postgraduates. Her clinical research topics include new orthodontic brackets, fixed appliances and TADs. She’s published 4 articles in well renowned indexed journals and has a published patency of her own. Her private practice is currently limited to orthodontics and works as a consultant in various clinics.",institutionString:null,institution:{name:"SRM Dental College",country:{name:"India"}}},{id:"323731",title:"Prof.",name:"Deepak M.",middleName:"Macchindra",surname:"Vikhe",slug:"deepak-m.-vikhe",fullName:"Deepak M. Vikhe",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/323731/images/13613_n.jpg",biography:"Dr Deepak M.Vikhe .\n\n\t\n\tDr Deepak M.Vikhe , completed his Masters & PhD in Prosthodontics from Rural Dental College, Loni securing third rank in the Pravara Institute of Medical Sciences Deemed University. He was awarded Dr.G.C.DAS Memorial Award for Research on Implants at 39th IPS conference Dubai (U A E).He has two patents under his name. He has received Dr.Saraswati medal award for best research for implant study in 2017.He has received Fully funded scholarship to Spain ,university of Santiago de Compostela. He has completed fellowship in Implantlogy from Noble Biocare. \nHe has attended various conferences and CDE programmes and has national publications to his credit. His field of interest is in Implant supported prosthesis. Presently he is working as a associate professor in the Dept of Prosthodontics, Rural Dental College, Loni and maintains a successful private practice specialising in Implantology at Rahata.\n\nEmail: drdeepak_mvikhe@yahoo.com..................",institutionString:null,institution:{name:"Pravara Institute of Medical Sciences",country:{name:"India"}}},{id:"204110",title:"Dr.",name:"Ahmed A.",middleName:null,surname:"Madfa",slug:"ahmed-a.-madfa",fullName:"Ahmed A. Madfa",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/204110/images/system/204110.jpg",biography:"Dr. Madfa is currently Associate Professor of Endodontics at Thamar University and a visiting lecturer at Sana'a University and University of Sciences and Technology. He has more than 6 years of experience in teaching. His research interests include root canal morphology, functionally graded concept, dental biomaterials, epidemiology and dental education, biomimetic restoration, finite element analysis and endodontic regeneration. Dr. Madfa has numerous international publications, full articles, two patents, a book and a book chapter. Furthermore, he won 14 international scientific awards. Furthermore, he is involved in many academic activities ranging from editorial board member, reviewer for many international journals and postgraduate students' supervisor. Besides, I deliver many courses and training workshops at various scientific events. Dr. Madfa also regularly attends international conferences and holds administrative positions (Deputy Dean of the Faculty for Students’ & Academic Affairs and Deputy Head of Research Unit).",institutionString:"Thamar University",institution:null},{id:"210472",title:"Dr.",name:"Nermin",middleName:"Mohammed Ahmed",surname:"Yussif",slug:"nermin-yussif",fullName:"Nermin Yussif",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/210472/images/system/210472.jpg",biography:"Dr. Nermin Mohammed Ahmed Yussif is working at the Faculty of dentistry, University for October university for modern sciences and arts (MSA). Her areas of expertise include: periodontology, dental laserology, oral implantology, periodontal plastic surgeries, oral mesotherapy, nutrition, dental pharmacology. She is an editor and reviewer in numerous international journals.",institutionString:"MSA University",institution:null},{id:"204606",title:"Dr.",name:"Serdar",middleName:null,surname:"Gözler",slug:"serdar-gozler",fullName:"Serdar Gözler",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/204606/images/system/204606.jpeg",biography:"Dr. Serdar Gözler has completed his undergraduate studies at the Marmara University Faculty of Dentistry in 1978, followed by an assistantship in the Prosthesis Department of Dicle University Faculty of Dentistry. Starting his PhD work on non-resilient overdentures with Assoc. Prof. Hüsnü Yavuzyılmaz, he continued his studies with Prof. Dr. Gürbüz Öztürk of Istanbul University Faculty of Dentistry Department of Prosthodontics, this time on Gnatology. He attended training programs on occlusion, neurology, neurophysiology, EMG, radiology and biostatistics. In 1982, he presented his PhD thesis \\Gerber and Lauritzen Occlusion Analysis Techniques: Diagnosis Values,\\ at Istanbul University School of Dentistry, Department of Prosthodontics. As he was also working with Prof. Senih Çalıkkocaoğlu on The Physiology of Chewing at the same time, Gözler has written a chapter in Çalıkkocaoğlu\\'s book \\Complete Prostheses\\ entitled \\The Place of Neuromuscular Mechanism in Prosthetic Dentistry.\\ The book was published five times since by the Istanbul University Publications. Having presented in various conferences about occlusion analysis until 1998, Dr. Gözler has also decided to use the T-Scan II occlusion analysis method. Having been personally trained by Dr. Robert Kerstein on this method, Dr. Gözler has been lecturing on the T-Scan Occlusion Analysis Method in conferences both in Turkey and abroad. Dr. Gözler has various articles and presentations on Digital Occlusion Analysis methods. He is now Head of the TMD Clinic at Prosthodontic Department of Faculty of Dentistry , Istanbul Aydın University , Turkey.",institutionString:"Istanbul Aydin University",institution:{name:"Istanbul Aydın University",country:{name:"Turkey"}}},{id:"256417",title:"Associate Prof.",name:"Sanaz",middleName:null,surname:"Sadry",slug:"sanaz-sadry",fullName:"Sanaz Sadry",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/256417/images/8106_n.jpg",biography:null,institutionString:null,institution:{name:"Istanbul Aydın University",country:{name:"Turkey"}}},{id:"240870",title:"Ph.D.",name:"Alaa Eddin Omar",middleName:null,surname:"Al Ostwani",slug:"alaa-eddin-omar-al-ostwani",fullName:"Alaa Eddin Omar Al Ostwani",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/240870/images/system/240870.jpeg",biography:"Dr. Al Ostwani Alaa Eddin Omar received his Master in dentistry from Damascus University in 2010, and his Ph.D. in Pediatric Dentistry from Damascus University in 2014. Dr. Al Ostwani is an assistant professor and faculty member at IUST University since 2014. \nDuring his academic experience, he has received several awards including the scientific research award from the Union of Arab Universities, the Syrian gold medal and the international gold medal for invention and creativity. Dr. Al Ostwani is a Member of the International Association of Dental Traumatology and the Syrian Society for Research and Preventive Dentistry since 2017. He is also a Member of the Reviewer Board of International Journal of Dental Medicine (IJDM), and the Indian Journal of Conservative and Endodontics since 2016.",institutionString:"International University for Science and Technology.",institution:{name:"Islamic University of Science and Technology",country:{name:"India"}}},{id:"42847",title:"Dr.",name:"Belma",middleName:null,surname:"Işik Aslan",slug:"belma-isik-aslan",fullName:"Belma Işik Aslan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/42847/images/system/42847.jpg",biography:"Dr. Belma IşIk Aslan was born in 1976 in Ankara-TURKEY. After graduating from TED Ankara College in 1994, she attended to Gazi University, Faculty of Dentistry in Ankara. She completed her PhD in orthodontic education at Gazi University between 1999-2005. Dr. Işık Aslan stayed at the Providence Hospital Craniofacial Institude and Reconstructive Surgery in Michigan, USA for three months as an observer. She worked as a specialist doctor at Gazi University, Dentistry Faculty, Department of Orthodontics between 2005-2014. She was appointed as associate professor in January, 2014 and as professor in 2021. Dr. Işık Aslan still works as an instructor at the same faculty. She has published a total of 35 articles, 10 book chapters, 39 conference proceedings both internationally and nationally. Also she was the academic editor of the international book 'Current Advances in Orthodontics'. She is a member of the Turkish Orthodontic Society and Turkish Cleft Lip and Palate Society. She is married and has 2 children. Her knowledge of English is at an advanced level.",institutionString:"Gazi University Dentistry Faculty Department of Orthodontics",institution:null},{id:"202198",title:"Dr.",name:"Buket",middleName:null,surname:"Aybar",slug:"buket-aybar",fullName:"Buket Aybar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/202198/images/6955_n.jpg",biography:"Buket Aybar, DDS, PhD, was born in 1971. She graduated from Istanbul University, Faculty of Dentistry, in 1992 and completed her PhD degree on Oral and Maxillofacial Surgery in Istanbul University in 1997.\r\nDr. Aybar is currently a full-time professor in Istanbul University, Faculty of Dentistry Department of Oral and Maxillofacial Surgery. She has teaching responsibilities in graduate and postgraduate programs. Her clinical practice includes mainly dentoalveolar surgery.\r\nHer topics of interest are biomaterials science and cell culture studies. She has many articles in international and national scientific journals and chapters in books; she also has participated in several scientific projects supported by Istanbul University Research fund.",institutionString:null,institution:{name:"Marmara University",country:{name:"Turkey"}}},{id:"178412",title:"Associate Prof.",name:"Guhan",middleName:null,surname:"Dergin",slug:"guhan-dergin",fullName:"Guhan Dergin",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/178412/images/6954_n.jpg",biography:"Assoc. Prof. Dr. Gühan Dergin was born in 1973 in Izmit. He graduated from Marmara University Faculty of Dentistry in 1999. He completed his specialty of OMFS surgery in Marmara University Faculty of Dentistry and obtained his PhD degree in 2006. In 2005, he was invited as a visiting doctor in the Oral and Maxillofacial Surgery Department of the University of North Carolina, USA, where he went on a scholarship. Dr. Dergin still continues his academic career as an associate professor in Marmara University Faculty of Dentistry. He has many articles in international and national scientific journals and chapters in books.",institutionString:null,institution:{name:"Marmara University",country:{name:"Turkey"}}},{id:"178414",title:"Prof.",name:"Yusuf",middleName:null,surname:"Emes",slug:"yusuf-emes",fullName:"Yusuf Emes",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/178414/images/6953_n.jpg",biography:"Born in Istanbul in 1974, Dr. Emes graduated from Istanbul University Faculty of Dentistry in 1997 and completed his PhD degree in Istanbul University faculty of Dentistry Department of Oral and Maxillofacial Surgery in 2005. He has papers published in international and national scientific journals, including research articles on implantology, oroantral fistulas, odontogenic cysts, and temporomandibular disorders. Dr. Emes is currently working as a full-time academic staff in Istanbul University faculty of Dentistry Department of Oral and Maxillofacial Surgery.",institutionString:null,institution:{name:"Istanbul University",country:{name:"Turkey"}}},{id:"192229",title:"Ph.D.",name:"Ana Luiza",middleName:null,surname:"De Carvalho Felippini",slug:"ana-luiza-de-carvalho-felippini",fullName:"Ana Luiza De Carvalho Felippini",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/192229/images/system/192229.jpg",biography:null,institutionString:"University of São Paulo",institution:{name:"University of Sao Paulo",country:{name:"Brazil"}}},{id:"256851",title:"Prof.",name:"Ayşe",middleName:null,surname:"Gülşen",slug:"ayse-gulsen",fullName:"Ayşe Gülşen",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/256851/images/9696_n.jpg",biography:"Dr. Ayşe Gülşen graduated in 1990 from Faculty of Dentistry, University of Ankara and did a postgraduate program at University of Gazi. \nShe worked as an observer and research assistant in Craniofacial Surgery Departments in New York, Providence Hospital in Michigan and Chang Gung Memorial Hospital in Taiwan. \nShe works as Craniofacial Orthodontist in Department of Aesthetic, Plastic and Reconstructive Surgery, Faculty of Medicine, University of Gazi, Ankara Turkey since 2004.",institutionString:"Orthodontist, Assoc Prof in the Department of Aesthetic, Plastic and Reconstructive Surgery, Faculty of Medicine, University of Gazi",institution:null},{id:"255366",title:"Prof.",name:"Tosun",middleName:null,surname:"Tosun",slug:"tosun-tosun",fullName:"Tosun Tosun",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/255366/images/7347_n.jpg",biography:"Graduated at the Faculty of Dentistry, University of Istanbul, Turkey in 1989;\nVisitor Assistant at the University of Padua, Italy and Branemark Osseointegration Center of Treviso, Italy between 1993-94;\nPhD thesis on oral implantology in University of Istanbul and was awarded the academic title “Dr.med.dent.”, 1997;\nHe was awarded the academic title “Doç.Dr.” (Associated Professor) in 2003;\nProficiency in Botulinum Toxin Applications, Reading-UK in 2009;\nMastership, RWTH Certificate in Laser Therapy in Dentistry, AALZ-Aachen University, Germany 2009-11;\nMaster of Science (MSc) in Laser Dentistry, University of Genoa, Italy 2013-14.\n\nDr.Tosun worked as Research Assistant in the Department of Oral Implantology, Faculty of Dentistry, University of Istanbul between 1990-2002. \nHe worked part-time as Consultant surgeon in Harvard Medical International Hospitals and John Hopkins Medicine, Istanbul between years 2007-09.\u2028He was contract Professor in the Department of Surgical and Diagnostic Sciences (DI.S.C.), Medical School, University of Genova, Italy between years 2011-16. \nSince 2015 he is visiting Professor at Medical School, University of Plovdiv, Bulgaria. \nCurrently he is Associated Prof.Dr. at the Dental School, Oral Surgery Dept., Istanbul Aydin University and since 2003 he works in his own private clinic in Istanbul, Turkey.\u2028\nDr.Tosun is reviewer in journal ‘Laser in Medical Sciences’, reviewer in journal ‘Folia Medica\\', a Fellow of the International Team for Implantology, Clinical Lecturer of DGZI German Association of Oral Implantology, Expert Lecturer of Laser&Health Academy, Country Representative of World Federation for Laser Dentistry, member of European Federation of Periodontology, member of Academy of Laser Dentistry. Dr.Tosun presents papers in international and national congresses and has scientific publications in international and national journals. He speaks english, spanish, italian and french.",institutionString:null,institution:{name:"Istanbul Aydın University",country:{name:"Turkey"}}},{id:"260116",title:"Dr.",name:"Mehmet",middleName:null,surname:"Yaltirik",slug:"mehmet-yaltirik",fullName:"Mehmet Yaltirik",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/260116/images/7413_n.jpg",biography:"Birth Date 25.09.1965\r\nBirth Place Adana- Turkey\r\nSex Male\r\nMarrial Status Bachelor\r\nDriving License Acquired\r\nMother Tongue Turkish\r\n\r\nAddress:\r\nWork:University of Istanbul,Faculty of Dentistry, Department of Oral Surgery and Oral Medicine 34093 Capa,Istanbul- TURKIYE",institutionString:null,institution:{name:"Istanbul University",country:{name:"Turkey"}}},{id:"171887",title:"Prof.",name:"Zühre",middleName:null,surname:"Akarslan",slug:"zuhre-akarslan",fullName:"Zühre Akarslan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/171887/images/system/171887.jpg",biography:"Zühre Akarslan was born in 1977 in Cyprus. She graduated from Gazi University Faculty of Dentistry, Ankara, Turkey in 2000. \r\nLater she received her Ph.D. degree from the Oral Diagnosis and Radiology Department; which was recently renamed as Oral and Dentomaxillofacial Radiology, from the same university. \r\nShe is working as a full-time Associate Professor and is a lecturer and an academic researcher. \r\nHer expertise areas are dental caries, cancer, dental fear and anxiety, gag reflex in dentistry, oral medicine, and dentomaxillofacial radiology.",institutionString:"Gazi University",institution:{name:"Gazi University",country:{name:"Turkey"}}},{id:"272237",title:"Dr.",name:"Pinar",middleName:"Kiymet",surname:"Karataban",slug:"pinar-karataban",fullName:"Pinar Karataban",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/272237/images/8911_n.png",biography:"Assist.Prof.Dr.Pınar Kıymet Karataban, DDS PhD \n\nDr.Pınar Kıymet Karataban was born in Istanbul in 1975. After her graduation from Marmara University Faculty of Dentistry in 1998 she started her PhD in Paediatric Dentistry focused on children with special needs; mainly children with Cerebral Palsy. She finished her pHD thesis entitled \\'Investigation of occlusion via cast analysis and evaluation of dental caries prevalance, periodontal status and muscle dysfunctions in children with cerebral palsy” in 2008. She got her Assist. Proffessor degree in Istanbul Aydın University Paediatric Dentistry Department in 2015-2018. ın 2019 she started her new career in Bahcesehir University, Istanbul as Head of Department of Pediatric Dentistry. In 2020 she was accepted to BAU International University, Batumi as Professor of Pediatric Dentistry. She’s a lecturer in the same university meanwhile working part-time in private practice in Ege Dental Studio (https://www.egedisklinigi.com/) a multidisciplinary dental clinic in Istanbul. Her main interests are paleodontology, ancient and contemporary dentistry, oral microbiology, cerebral palsy and special care dentistry. She has national and international publications, scientific reports and is a member of IAPO (International Association for Paleodontology), IADH (International Association of Disability and Oral Health) and EAPD (European Association of Pediatric Dentistry).",institutionString:null,institution:null},{id:"172009",title:"Dr.",name:"Fatma Deniz",middleName:null,surname:"Uzuner",slug:"fatma-deniz-uzuner",fullName:"Fatma Deniz Uzuner",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/172009/images/7122_n.jpg",biography:"Dr. Deniz Uzuner was born in 1969 in Kocaeli-TURKEY. After graduating from TED Ankara College in 1986, she attended the Hacettepe University, Faculty of Dentistry in Ankara. \nIn 1993 she attended the Gazi University, Faculty of Dentistry, Department of Orthodontics for her PhD education. After finishing the PhD education, she worked as orthodontist in Ankara Dental Hospital under the Turkish Government, Ministry of Health and in a special Orthodontic Clinic till 2011. Between 2011 and 2016, Dr. Deniz Uzuner worked as a specialist in the Department of Orthodontics, Faculty of Dentistry, Gazi University in Ankara/Turkey. In 2016, she was appointed associate professor. Dr. Deniz Uzuner has authored 23 Journal Papers, 3 Book Chapters and has had 39 oral/poster presentations. She is a member of the Turkish Orthodontic Society. Her knowledge of English is at an advanced level.",institutionString:null,institution:null},{id:"332914",title:"Dr.",name:"Muhammad Saad",middleName:null,surname:"Shaikh",slug:"muhammad-saad-shaikh",fullName:"Muhammad Saad Shaikh",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Jinnah Sindh Medical University",country:{name:"Pakistan"}}},{id:"315775",title:"Dr.",name:"Feng",middleName:null,surname:"Luo",slug:"feng-luo",fullName:"Feng Luo",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Sichuan University",country:{name:"China"}}},{id:"344229",title:"Dr.",name:"Sankeshan",middleName:null,surname:"Padayachee",slug:"sankeshan-padayachee",fullName:"Sankeshan Padayachee",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of the Witwatersrand",country:{name:"South Africa"}}},{id:"315727",title:"Ms.",name:"Kelebogile A.",middleName:null,surname:"Mothupi",slug:"kelebogile-a.-mothupi",fullName:"Kelebogile A. Mothupi",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of the Witwatersrand",country:{name:"South Africa"}}},{id:"423519",title:"Dr.",name:"Sizakele",middleName:null,surname:"Ngwenya",slug:"sizakele-ngwenya",fullName:"Sizakele Ngwenya",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of the Witwatersrand",country:{name:"South Africa"}}},{id:"337613",title:"Mrs.",name:"Tshakane",middleName:null,surname:"R.M.D. Ralephenya",slug:"tshakane-r.m.d.-ralephenya",fullName:"Tshakane R.M.D. Ralephenya",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of the Witwatersrand",country:{name:"South Africa"}}},{id:"419270",title:"Dr.",name:"Ann",middleName:null,surname:"Chianchitlert",slug:"ann-chianchitlert",fullName:"Ann Chianchitlert",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Walailak University",country:{name:"Thailand"}}},{id:"419271",title:"Dr.",name:"Diane",middleName:null,surname:"Selvido",slug:"diane-selvido",fullName:"Diane Selvido",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Walailak University",country:{name:"Thailand"}}},{id:"419272",title:"Dr.",name:"Irin",middleName:null,surname:"Sirisoontorn",slug:"irin-sirisoontorn",fullName:"Irin Sirisoontorn",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Walailak University",country:{name:"Thailand"}}}]}},subseries:{item:{id:"4",type:"subseries",title:"Fungal Infectious Diseases",keywords:"Emerging Fungal Pathogens, Invasive Infections, Epidemiology, Cell Membrane, Fungal Virulence, Diagnosis, Treatment",scope:"Fungi are ubiquitous and there are almost no non-pathogenic fungi. Fungal infectious illness prevalence and prognosis are determined by the exposure between fungi and host, host immunological state, fungal virulence, and early and accurate diagnosis and treatment. \r\nPatients with both congenital and acquired immunodeficiency are more likely to be infected with opportunistic mycosis. Fungal infectious disease outbreaks are common during the post- disaster rebuilding era, which is characterised by high population density, migration, and poor health and medical conditions.\r\nSystemic or local fungal infection is mainly associated with the fungi directly inhaled or inoculated in the environment during the disaster. The most common fungal infection pathways are human to human (anthropophilic), animal to human (zoophilic), and environment to human (soilophile). Diseases are common as a result of widespread exposure to pathogenic fungus dispersed into the environment. \r\nFungi that are both common and emerging are intertwined. In Southeast Asia, for example, Talaromyces marneffei is an important pathogenic thermally dimorphic fungus that causes systemic mycosis. Widespread fungal infections with complicated and variable clinical manifestations, such as Candida auris infection resistant to several antifungal medicines, Covid-19 associated with Trichoderma, and terbinafine resistant dermatophytosis in India, are among the most serious disorders. \r\nInappropriate local or systemic use of glucocorticoids, as well as their immunosuppressive effects, may lead to changes in fungal infection spectrum and clinical characteristics. Hematogenous candidiasis is a worrisome issue that affects people all over the world, particularly ICU patients. CARD9 deficiency and fungal infection have been major issues in recent years. Invasive aspergillosis is associated with a significant death rate. 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