Ligand information, CID number, and reference of 47 drugs with potential activity against the SARS-CoV-2 viral cycle.
\\n\\n
IntechOpen Book Series will also publish a program of research-driven Thematic Edited Volumes that focus on specific areas and allow for a more in-depth overview of a particular subject.
\\n\\nIntechOpen Book Series will be launching regularly to offer our authors and editors exciting opportunities to publish their research Open Access. We will begin by relaunching some of our existing Book Series in this innovative book format, and will expand in 2022 into rapidly growing research fields that are driving and advancing society.
\\n\\nLaunching 2021
\\n\\nArtificial Intelligence, ISSN 2633-1403
\\n\\nVeterinary Medicine and Science, ISSN 2632-0517
\\n\\nBiochemistry, ISSN 2632-0983
\\n\\nBiomedical Engineering, ISSN 2631-5343
\\n\\nInfectious Diseases, ISSN 2631-6188
\\n\\nPhysiology (Coming Soon)
\\n\\nDentistry (Coming Soon)
\\n\\nWe invite you to explore our IntechOpen Book Series, find the right publishing program for you and reach your desired audience in record time.
\\n\\nNote: Edited in October 2021
\\n"}]',published:!0,mainMedia:{caption:"",originalUrl:"/media/original/132"}},components:[{type:"htmlEditorComponent",content:'With the desire to make book publishing more relevant for the digital age and offer innovative Open Access publishing options, we are thrilled to announce the launch of our new publishing format: IntechOpen Book Series.
\n\nDesigned to cover fast-moving research fields in rapidly expanding areas, our Book Series feature a Topic structure allowing us to present the most relevant sub-disciplines. Book Series are headed by Series Editors, and a team of Topic Editors supported by international Editorial Board members. Topics are always open for submissions, with an Annual Volume published each calendar year.
\n\nAfter a robust peer-review process, accepted works are published quickly, thanks to Online First, ensuring research is made available to the scientific community without delay.
\n\nOur innovative Book Series format brings you:
\n\nIntechOpen Book Series will also publish a program of research-driven Thematic Edited Volumes that focus on specific areas and allow for a more in-depth overview of a particular subject.
\n\nIntechOpen Book Series will be launching regularly to offer our authors and editors exciting opportunities to publish their research Open Access. We will begin by relaunching some of our existing Book Series in this innovative book format, and will expand in 2022 into rapidly growing research fields that are driving and advancing society.
\n\nLaunching 2021
\n\nArtificial Intelligence, ISSN 2633-1403
\n\nVeterinary Medicine and Science, ISSN 2632-0517
\n\nBiochemistry, ISSN 2632-0983
\n\nBiomedical Engineering, ISSN 2631-5343
\n\nInfectious Diseases, ISSN 2631-6188
\n\nPhysiology (Coming Soon)
\n\nDentistry (Coming Soon)
\n\nWe invite you to explore our IntechOpen Book Series, find the right publishing program for you and reach your desired audience in record time.
\n\nNote: Edited in October 2021
\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:"5427",leadTitle:null,fullTitle:"Modern Antenna Systems",title:"Modern Antenna Systems",subtitle:null,reviewType:"peer-reviewed",abstract:"The field of antenna engineering has been advancing at a remarkable pace to support modern communication systems. Recently, significant progress has been made in the development of new antennas and techniques targeted for applications in medical, defense, health care, communication, etc. The motivation of this project is to present cutting-edge research materials in the field of antennas for modern wireless communication.",isbn:"978-953-51-2926-4",printIsbn:"978-953-51-2925-7",pdfIsbn:"978-953-51-4111-2",doi:"10.5772/62853",price:119,priceEur:129,priceUsd:155,slug:"modern-antenna-systems",numberOfPages:220,isOpenForSubmission:!1,isInWos:1,isInBkci:!0,hash:"b38d742cc1390bb9b98d357536c523fe",bookSignature:"Mohammad A. Matin",publishedDate:"February 22nd 2017",coverURL:"https://cdn.intechopen.com/books/images_new/5427.jpg",numberOfDownloads:21184,numberOfWosCitations:8,numberOfCrossrefCitations:17,numberOfCrossrefCitationsByBook:1,numberOfDimensionsCitations:18,numberOfDimensionsCitationsByBook:0,hasAltmetrics:0,numberOfTotalCitations:43,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"April 5th 2016",dateEndSecondStepPublish:"April 26th 2016",dateEndThirdStepPublish:"July 31st 2016",dateEndFourthStepPublish:"October 29th 2016",dateEndFifthStepPublish:"November 28th 2016",currentStepOfPublishingProcess:5,indexedIn:"1,2,3,4,5,6,7,8",editedByType:"Edited by",kuFlag:!1,featuredMarkup:null,editors:[{id:"12623",title:"Prof.",name:"Mohammad Abdul",middleName:"A",surname:"Matin",slug:"mohammad-abdul-matin",fullName:"Mohammad Abdul Matin",profilePictureURL:"https://mts.intechopen.com/storage/users/12623/images/1967_n.jpg",biography:"Dr. Mohammad A Matin is a Professor of the Department of Electrical and Computer Engineering at North South University (NSU), where he has been since 2008. He was first appointed as Assistant Professor and then promoted to Associate Professor at North South University in 2011 and later on Professor. While in that post he was also the coordinator of EEE program. During 2012-2017, he was an Associate Professor at Universiti Teknologi Brunei (UTB), Brunei Darussalam (QS World University ranking 379). He received his B.Sc. degree in Electrical and Electronic Engineering from BUET (Bangladesh), his M.Sc. degree in Digital Communication from Loughborough University, UK and PhD in Wireless Communication from Newcastle University, UK. He has taught several courses in communications, electronics and signal processing at KUET, Khulna University, BRAC University, and UKM (Malaysia) during his career. He has published over 90 peer-reviewed journals and conference papers, and is the author/editor of 16 (sixteen) academic books such as Towards Cognitive IoT Networks (Springer, 2020), Communication Systems for Electrical Engineers (Springer, 2018), Spectrum Access and Management for Cognitive Radio Networks (Springer, 2016), Coding for MIMO-OFDM in Future Wireless Systems (Springer, 2015), Advances in Sensor Networks Research (Nova publisher, USA, 2014) and 10 (ten) book chapters. He has presented invited talks in Bangladesh and Malaysia and has served as a member of the program committee for more than 50 international conferences. He is on the editorial board of several international journals such as IEEE Communications Magazine, IEEE, USA, IET Wireless Sensor Systems (IET-WSS), and so on. Dr. Matin is a member of the IEEE, IEEE Communications Society (IEEE ComSoc), and several other international organizations. He served as a counselor of IEEE North South University (2008–2011), and secretary of the IEEE Communication Society, Bangladesh Chapter (2010–2011). He has received a number of prizes and scholarships including the Best student prize (Loughborough University), Commonwealth Scholarship, and Overseas Research Scholarship (ORS) conferred by the Committee of Vice Chancellors and Principals (CVCP) in the UK. He has been fortunate enough to work in WFS Project with Wireless Fibre Sytems Ltd, UK as an expert. His current research interests include UWB communication, wireless sensor networks, cognitive radio, EM modeling, and antenna engineering.",institutionString:null,position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"4",totalChapterViews:"0",totalEditedBooks:"7",institution:{name:"North South University",institutionURL:null,country:{name:"Bangladesh"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"762",title:"Wireless Communication System",slug:"electrical-and-electronic-engineering-wireless-communication-system"}],chapters:[{id:"53569",title:"Introduction and Outline",doi:"10.5772/66983",slug:"introduction-and-outline",totalDownloads:2401,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:null,signatures:"Mohammad Abdul Matin",downloadPdfUrl:"/chapter/pdf-download/53569",previewPdfUrl:"/chapter/pdf-preview/53569",authors:[{id:"12623",title:"Prof.",name:"Mohammad Abdul",surname:"Matin",slug:"mohammad-abdul-matin",fullName:"Mohammad Abdul Matin"}],corrections:null},{id:"53876",title:"Recent Computer-Aided Design Techniques for Rectangular Microstrip Antenna",doi:"10.5772/66355",slug:"recent-computer-aided-design-techniques-for-rectangular-microstrip-antenna",totalDownloads:1788,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"In modern microwave systems, rectangular microstrip patch antennas (RMPAs) are probably the most investigated topics among the planar antennas. There are several methods available in literature, for designing and analyzing such antennas, but most of them are very complex and give only approximate results. In this chapter, we have discussed the most accurate and updated computer-aided design (CAD) formulations related to probe-fed RMPA for computing its fundamental input characteristics (resonant frequency and input impedance) and improving radiation characteristics, i.e. gain and polarization purity (the parameter that signifies how much an RMPA is free from spurious modes). These formulations have evolved in the last decades and have been validated against numerous simulations and measurements. The present CAD formulas for resonant frequency and input impedance can accurately address a wide range of RMPA with patch width to patch length ratio (W/L) from 0.5 to 2.0, a substrate having thickness up to 0.23 λg where λg is the guide wavelength and relative permittivity (εr) ranging over 2.2–10.8. The role of a finite air gap on resonant frequency and gain of an RMPA have also been presented. The chapter will be surely useful to antenna designers to achieve a concrete understanding of the RMPA theory.",signatures:"Sudipta Chattopadhyay and Subhradeep Chakraborty",downloadPdfUrl:"/chapter/pdf-download/53876",previewPdfUrl:"/chapter/pdf-preview/53876",authors:[{id:"188270",title:"Dr.",name:"Sudipta",surname:"Chattopadhyay",slug:"sudipta-chattopadhyay",fullName:"Sudipta Chattopadhyay"},{id:"189392",title:"Mr.",name:"Subhradeep",surname:"Chakraborty",slug:"subhradeep-chakraborty",fullName:"Subhradeep Chakraborty"}],corrections:null},{id:"52528",title:"Application of Composite Right/Left-Handed Metamaterials in Leaky-Wave Antennas",doi:"10.5772/65643",slug:"application-of-composite-right-left-handed-metamaterials-in-leaky-wave-antennas",totalDownloads:2664,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"This chapter reviews the most significant advancements in the context of metamaterial (MTM) leaky wave antennas (LWAs). A brief review of the mechanism of leaky wave radiation along with an important class of MTMs known as composite right/left-handed (CRLH) structures is presented. Then, recent outstanding works in the area of CRLH LWAs are reported in detail. These works include the application of electronic control, substrate integrated waveguides, dual band and wideband performance, ferrite loaded waveguides, and split-ring-resonator (SRR)-based MTMs in LWAs. Also, the benefits of LWAs to design high gain active structures, reflecto-directive systems, wideband dual-layer substrate integrated waveguide antennas and conformal antennas are discussed.",signatures:"Keyhan Hosseini and Zahra Atlasbaf",downloadPdfUrl:"/chapter/pdf-download/52528",previewPdfUrl:"/chapter/pdf-preview/52528",authors:[{id:"18749",title:"Dr.",name:"zahra",surname:"atlasbaf",slug:"zahra-atlasbaf",fullName:"zahra atlasbaf"},{id:"188222",title:"Ph.D.",name:"Keyhan",surname:"Hosseini",slug:"keyhan-hosseini",fullName:"Keyhan Hosseini"}],corrections:null},{id:"53785",title:"Metamaterial Antennas for Wireless Communications Transceivers",doi:"10.5772/66379",slug:"metamaterial-antennas-for-wireless-communications-transceivers",totalDownloads:1854,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Limited space is given to antennas in modern portable wireless systems, which means that antennas need to be small in size and compact structures. However, shrinkage of conventional antennas leads to performance degradation and complex mechanical assembly. Therefore, the design of miniature antennas for application in wireless communication systems is highly challenging using traditional means. In this chapter, it is shown that metamaterial (MTM) technology offers a solution to synthesize antennas with a small footprint with the added advantage of low cost and excellent radiation characteristics.",signatures:"Mohammad Alibakhshikenari, Mohammad Naser-Moghadasi,\nRamazan Ali Sadeghzadeh, Bal Singh Virdee and Ernesto Limiti",downloadPdfUrl:"/chapter/pdf-download/53785",previewPdfUrl:"/chapter/pdf-preview/53785",authors:[{id:"146608",title:"Prof.",name:"Mohammad",surname:"Naser-Moghadasi",slug:"mohammad-naser-moghadasi",fullName:"Mohammad Naser-Moghadasi"},{id:"188537",title:"Mr.",name:"Mohammad",surname:"Alibakhshikenari",slug:"mohammad-alibakhshikenari",fullName:"Mohammad Alibakhshikenari"},{id:"189212",title:"Prof.",name:"Bal Singh",surname:"Virdee",slug:"bal-singh-virdee",fullName:"Bal Singh Virdee"},{id:"189213",title:"Prof.",name:"Ernesto",surname:"Limiti",slug:"ernesto-limiti",fullName:"Ernesto Limiti"},{id:"194529",title:"Prof.",name:"Ramazan Ali",surname:"Sadeghzadeh",slug:"ramazan-ali-sadeghzadeh",fullName:"Ramazan Ali Sadeghzadeh"}],corrections:null},{id:"53871",title:"Planar Antennas with Enhanced Bandwidth and Radiation Characteristics",doi:"10.5772/66381",slug:"planar-antennas-with-enhanced-bandwidth-and-radiation-characteristics",totalDownloads:1892,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Wireless companies want next-generation gadgets to download at rates of gigabits per second. This is because there is an exponential growth in mobile traffic, however, existing digital networks and devices will not be efficient enough to handle this much growth. In order to realize this requirement, the next generation of wireless communication devices will need to operate over a much larger frequency bandwidth. In this chapter, novel wideband and ultra-wideband (UWB) antennas that are based on loading the background plane of a monopole radiator with concentric split-ring resonators are presented. It is shown that this modification improves the fractional bandwidth of the antenna from 41 to 87%; in particular, the operational bandwidth of the proposed antennas is double that of a conventional monopole antenna of the same size.",signatures:"Mohammad Alibakhshikenari, Mohammad Naser-Moghadasi,\nRamazan Ali Sadeghzadeh, Bal Singh Virdee and Ernesto Limiti",downloadPdfUrl:"/chapter/pdf-download/53871",previewPdfUrl:"/chapter/pdf-preview/53871",authors:[{id:"146608",title:"Prof.",name:"Mohammad",surname:"Naser-Moghadasi",slug:"mohammad-naser-moghadasi",fullName:"Mohammad Naser-Moghadasi"},{id:"188537",title:"Mr.",name:"Mohammad",surname:"Alibakhshikenari",slug:"mohammad-alibakhshikenari",fullName:"Mohammad Alibakhshikenari"},{id:"189212",title:"Prof.",name:"Bal Singh",surname:"Virdee",slug:"bal-singh-virdee",fullName:"Bal Singh Virdee"},{id:"189213",title:"Prof.",name:"Ernesto",surname:"Limiti",slug:"ernesto-limiti",fullName:"Ernesto Limiti"},{id:"194529",title:"Prof.",name:"Ramazan Ali",surname:"Sadeghzadeh",slug:"ramazan-ali-sadeghzadeh",fullName:"Ramazan Ali Sadeghzadeh"}],corrections:null},{id:"53259",title:"Compact Antenna with Enhanced Performances Using Artificial Meta-Surfaces",doi:"10.5772/66354",slug:"compact-antenna-with-enhanced-performances-using-artificial-meta-surfaces",totalDownloads:1988,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"In recent years, artificial meta‐surfaces, with the advantages of smaller physical space and less losses compared with three‐dimensional (3D) metamaterials (MTM), have intrigued a great impetus and been applied widely to cloaks, subwavelength planar lenses, holograms, etc. Typically, one most important part for meta‐surfaces’ applications is to improve the performance of antennas. In this chapter, we discuss our effort in exploring novel mechanisms of enhancing the antenna bandwidth using the magneto‐electro‐dielectric waveguided meta‐surface (MED‐WG‐MS), achieving circular polarization radiation through fractal meta‐surface, and also realizing beam manipulation using cascaded resonator layers, which is demonstrated from aspects of theoretical analysis, numerical calculation, and experimental measurement. The numerical and measured results coincide well with each other. Note that all designed antenna and microwave devices based on compact meta‐surfaces show advantages compared with the conventional cases.",signatures:"Tong Cai, He-Xiu Xu, Guang-Ming Wang and Jian-Gang Liang",downloadPdfUrl:"/chapter/pdf-download/53259",previewPdfUrl:"/chapter/pdf-preview/53259",authors:[{id:"187799",title:"Dr.",name:"He-Xiu",surname:"Xu",slug:"he-xiu-xu",fullName:"He-Xiu Xu"},{id:"189763",title:"Ph.D.",name:"Tong",surname:"Cai",slug:"tong-cai",fullName:"Tong Cai"},{id:"189832",title:"Prof.",name:"Guang-Ming",surname:"Wang",slug:"guang-ming-wang",fullName:"Guang-Ming Wang"},{id:"189833",title:"Prof.",name:"Jian-Gang",surname:"Liang",slug:"jian-gang-liang",fullName:"Jian-Gang Liang"}],corrections:null},{id:"52564",title:"A Circularly Polarized Spiral/Loop Antenna and Its Simple Feeding Mechanism",doi:"10.5772/65651",slug:"a-circularly-polarized-spiral-loop-antenna-and-its-simple-feeding-mechanism",totalDownloads:2112,totalCrossrefCites:2,totalDimensionsCites:2,hasAltmetrics:0,abstract:"In this chapter, a simple spiral/loop antenna radiating circular polarization is introduced. Circularly polarized antennas are complex structures in general because they are constituted by two or more antennas in multilayer structures or employ phase-shifting circuits. For this reason, the circularly polarized antennas are too complex to be applied to mobile communication devices such as radiofrequency identifier (RFID) and global positioning system (GPS) handy terminals. Simpler and easier circularly polarized antennas are necessary for these devices. The presented circularly polarized antenna is so simple that it is printable, and it has only one port that can be fed through a coaxial cable directly. In the first section, the necessity of the circularly polarized antennas for modern antenna systems is explained. Then, the historical conventional antennas are introduced by referring to important publications. In the second section, the novel simple circularly polarized antenna invented by the author will be presented. The basic structure of the presented antenna and its principle will be explained. In the third section, a feeding mechanism to feed the presented antenna through a coaxial cable will be presented. In conclusion, detailed characteristics of the presented antennas will be summarized.",signatures:"Mayumi Matsunaga",downloadPdfUrl:"/chapter/pdf-download/52564",previewPdfUrl:"/chapter/pdf-preview/52564",authors:[{id:"15254",title:"Prof.",name:"Mayumi",surname:"Matsunaga",slug:"mayumi-matsunaga",fullName:"Mayumi Matsunaga"}],corrections:null},{id:"53208",title:"Omnidirectional Circularly Polarized Antenna with High Gain in Wide Bandwidth",doi:"10.5772/66011",slug:"omnidirectional-circularly-polarized-antenna-with-high-gain-in-wide-bandwidth",totalDownloads:2461,totalCrossrefCites:4,totalDimensionsCites:4,hasAltmetrics:0,abstract:"A novel omnidirectional circularly polarized (CP) slot array antenna with high gain is proposed, which is based on the coaxial cylinder structure, and the orthogonal slots radiated the circular polarization wave around the cylinder. Further, the improved dual circularly polarized (CP) omnidirectional antenna based on slot array in coaxial cylinder structure is presented too, and two ports are assigned in its two side as left hand circularly polarized (LHCP) port and right hand circularly polarized (RHCP) port, respectively. The simulation and experiment results show their novelty and good performance of omnidirectional circular polarization with about 5 dBi gain in 5.2–5.9 GHz.",signatures:"Bin Zhou, Junping Geng, Xianling Liang, Ronghong Jin and\nGuanshen Chenhu",downloadPdfUrl:"/chapter/pdf-download/53208",previewPdfUrl:"/chapter/pdf-preview/53208",authors:[{id:"147056",title:"Prof.",name:"Xian-Ling",surname:"Liang",slug:"xian-ling-liang",fullName:"Xian-Ling Liang"},{id:"189327",title:"Prof.",name:"Junping",surname:"Geng",slug:"junping-geng",fullName:"Junping Geng"},{id:"189923",title:"Prof.",name:"Ronghong",surname:"Jin",slug:"ronghong-jin",fullName:"Ronghong Jin"},{id:"189925",title:"MSc.",name:"Bin",surname:"Zhou",slug:"bin-zhou",fullName:"Bin Zhou"},{id:"189927",title:"MSc.",name:"Guanshen",surname:"Chenhu",slug:"guanshen-chenhu",fullName:"Guanshen Chenhu"}],corrections:null},{id:"53498",title:"Investigating EM Dipole Radiating Element for Dual Polarized Phased Array Weather Radars",doi:"10.5772/66502",slug:"investigating-em-dipole-radiating-element-for-dual-polarized-phased-array-weather-radars",totalDownloads:2140,totalCrossrefCites:0,totalDimensionsCites:0,hasAltmetrics:0,abstract:"Dual‐polarized antenna radiating element is a critical component in the Multi‐function Phased Array Radar (MPAR). This paper studies the dual‐polarized radiating element based on the EM dipole concept. Two different geometries, i.e., loop approximated as magnetic dipole and a printed electric dipole, are used to form a single dual‐polarized radiating element. Radiation patterns based on Ansoft HFSS (High Frequency Structural Simulator) simulation software and measurements carried out in anechoic chambers are presented. Initial array design based on these elements will also be discussed.",signatures:"Ridhwan Khalid Mirza, Yan (Rockee) Zhang, Dusan Zrnic and\nRichard Doviak",downloadPdfUrl:"/chapter/pdf-download/53498",previewPdfUrl:"/chapter/pdf-preview/53498",authors:[{id:"189642",title:"M.Sc.",name:"Ridhwan Khalid",surname:"Mirza",slug:"ridhwan-khalid-mirza",fullName:"Ridhwan Khalid Mirza"},{id:"189644",title:"Prof.",name:"Yan",surname:"Zhang",slug:"yan-zhang",fullName:"Yan Zhang"}],corrections:null},{id:"53458",title:"Micro-Switch Design and Its Optimization Using Pattern Search Algorithm for Application in Reconfigurable Antenna",doi:"10.5772/66127",slug:"micro-switch-design-and-its-optimization-using-pattern-search-algorithm-for-application-in-reconfigu",totalDownloads:1885,totalCrossrefCites:11,totalDimensionsCites:12,hasAltmetrics:0,abstract:"This chapter reports the design and optimization algorithm of metal-contact RF microswitch. Various important evolutionary optimization techniques that can be used to optimize non-linear and even non-differentiable types of radio frequency (RF) circuit’s problems are also reviewed. The transient response of the proposed switch shows displacement time (i.e., squeezed-film damping effect) of 5.0 μs and pull-in voltage varying from 9.0 to 9.25 V. Primarily, the switch exhibits insertion loss of 0.15 to 0.51 dB in on-position and isolation of 75.96 to 35.83 dB in off-position at 0.1–10 GHz. Also, the proposed RF switch equivalent circuit and layout are validated in ADS software which was earlier simulated in HFSS. A pattern search (PS) algorithm is used to optimize RF characteristics of the proposed switch after a brief review of the different optimization techniques. After optimization, the switch shows decrement in insertion loss and increment in isolation at 0.1–10 GHz. Further, two such optimized switches are introduced on the defected ground structure (DGS) antenna to make it reconfigurable in terms of frequency. Reconfigurable antenna (RA) is simulated using HFSS software and simulation results are verified by showing the mark of agreement with the fabrication results. The novelty in the proposed design is due to dual-band behavior and better resonance performance than antennas available in the literature. 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The initial stage of the infection cycle starts with the recognition and anchoring of the SARS-CoV-2 spike protein complex into the host angiotensin-converting enzyme 2 (ACE2) through the receptor-binding domain (RBD) located at each one of the 3S proteins [13]. Then, the activation of the spike occurs at the surface or endosome level by transmembrane serine protease 2 (TMPRSS2) or cathepsin B/L proteases, respectively, to allow viral entry [14]. Once the virus membrane merges with the cell membrane, the genomic material enters the cell. The cell’s ribosomes then translate the viral RNA into pp1a/ab polyproteins, which will be later processed by cleavage through the enzymatic activity of the main protease (Mpro) and the papain-like protease (PLpro) [15]. This process will release 16 non-structural proteins (NSPs), including the RNA-dependent RNA polymerase (NSP12) and co-factors NSP7, and NSP8 of the RNA-replication machinery (Rdrp). After replication, expression of the structural proteins occurs, the genomic material is packaged, and the virion is assembled on a lipid membrane and matured for subsequent exocytosis. In addition, evidence suggests that the SARS-CoV-2 proteases and some of their cleavage products, besides their critical function for the proper infection process, interplay with the host’s innate immune response through different mechanisms [16]. In particular, PLpro-ISG15 interaction allows the virus to evade the innate immune response through deubiquitination and deISGylation activities of the protease [17, 18]. Interestingly, the process occurs at the same binding cavity as the PLpro known inhibitor, GRL0617 [19].
The code for the cavity-detection guided blind docking (CB-Dock) [20] stand-alone version is freely available at Yang Cao’s Lab webpage [http://clab.labshare.cn/cb-dock/php/manual.php#download].
The customized high-throughput virtual screening pipeline we developed can be accessed at GitHub [https://github.com/tripplab/HTVS].
We conducted an extensive scientific literature search for drugs reported as potentially able to prevent SARS-CoV-2 infection. The search included
We performed the molecular
ID | Drug | CIDa | References |
---|---|---|---|
RPA01 | Losartan | 3961 | [30, 31] |
RPA02 | Telmisartan | 65,999 | [30, 32] |
RPA03 | Arbidol | 131,411 | [33, 34] |
RPA04 | Camostat mesylate | 5,284,360 | [33, 35] |
RPA05 | Rimantadine | 5071 | [36] |
RPA06 | Chloroquine | 2719 | [33, 37] |
RPA07 | Hydroxychloroquine | 3652 | [33, 37] |
RPA08 | Baricitinib | 44,205,240 | [38, 39] |
RPA09 | Colchicine | 6167 | [40, 41] |
RPA10 | Disulfiram | 3117 | [42, 43] |
RPA11 | Ebselen | 3194 | [42, 43, 44] |
RPA12 | Hesperidin | 10,621 | [45, 46] |
RPA13 | Qingdainone | 3,035,728 | [47] |
RPA14 | Nafamostat | 4413 | [48, 49] |
RPA15 | Dipeptidyl nitrile-derivative | Compound 10 | [50] |
RPB01 | Lopinavir | 92,727 | [33, 51] |
RPB02 | Ritonavir | 392,622 | [33, 51] |
RPB03 | Darunavir | 213,039 | [36, 52] |
RPB04 | Cobicistat | 25,151,504 | [52] |
RPB05 | Isatin-derivative | Compound 26 | [53] |
RPB06 | Rupinatrivir | 6,440,352 | [54, 55] |
RPB07 | E-64 | 123,985 | [56] |
RPB08 | N3 inhibitor | 405,067,310 | [57] |
RPC01 | Ribavirin | 37,542 | [58, 59] |
RPC02 | Sofosbuvir | 45,375,808 | [58, 59] |
RPC03 | Molnupiravir | 145,996,610 | [58, 59] |
RPC04 | Nilotinib | 644,241 | [60, 61, 62] |
RPC05 | Saquinavir | 441,243 | [36, 58, 59, 62] |
RPC06 | Tipranavir | 54,682,461 | [58, 59, 62] |
RPC07 | Lonafarnib | 148,195 | [62] |
RPC08 | Tegobuvir | 23,649,154 | [58, 59, 62] |
RPC09 | Simeprevir | 24,873,435 | [58, 59] |
RPC10 | Filibuvir | 54,708,673 | [58, 59, 62] |
RPC11 | Cepharanthine | 10,206 | [62] |
RPC12 | Redemsivir | 121,304,016 | [33, 58, 59] |
RPC13 | Favipiravir | 492,405 | [33, 58, 59] |
RPD01 | rac5c | 76,853,649 | [18] |
EXT01 | Ascorbic Acid | 54,670,067 | [63] |
EXT02 | Ergocalciferol | 5,280,793 | [64, 65] |
EXT03 | Cholecalciferol | 5,280,795 | [64, 65] |
EXT04 | Ivermectin | 6,321,424 | [66] |
EXT05 | Azithromycin | 447,043 | [67] |
EXT06 | Heparin | 772 | [68] |
EXT07 | Methylprednisolone | 6741 | [69] |
EXT08 | Carvacrol | 10,364 | [70] |
EXT09 | Ursolic acid | 45,358,157 | [71] |
EXT10 | Oleanolic acid | 485,707 | [71] |
Ligand information, CID number, and reference of 47 drugs with potential activity against the SARS-CoV-2 viral cycle.
In the absence of the CID, the reference to the original investigation and the compound number are provided.
We included viral and cellular targets involved in the SARS-CoV-2 infection cycle, covering the entry, polyprotein processing, and replication. The targets’ three-dimensional structures were obtained from the Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB) in PDB format [23]. The complete structure of the spike homotrimer complex (PDB: 6VXX-1-1-1) was retrieved from the CHARMM-GUI Archive-COVID-19 proteins library [24]. We took special consideration to the spike complex given its large size and quaternary structure. We focused on four independent spike-based structures to extend the cavity sampling: the full-length spike’s homotrimer complex, the homotrimer head (S1), 1 S protein monomer, and one isolated receptor-binding domain (RBD).
Water, ions, glycosylations, and co-crystallized ligands were removed from all targets. Charges and hydrogens were fixed at neutral pH using chimera 1.15, their structure optimized, and the final configuration saved in PDB format [21]. In total, 16 structures of 10 targets were curated, as summarized in Table 2.
ID | Target | PDB IDa | SARS-CoV-2 infection step | References |
---|---|---|---|---|
H00 | ACE2 | 1R4L_A | Viral recognition | [72] |
H01 | ACE2 (B0AT1 closed complex) | 6M18_B | Viral recognition | [73] |
H02 | ACE2 (B0AT1 open complex) | 6M1D_B | Viral recognition | [73] |
H03 | TMPRSS2 | 7MEQ_A | Viral priming | [74] |
H04 | Cathepsin B | 3AI8_B | Viral priming | [75] |
H05 | Cathepsin L | 2NQD_B | Viral priming | [76] |
V01 | Spike homotrimer | 6VXX1-1-1 | Viral recognition | [77, 78] |
V01H | Spike homotrimer head | 6VXX1-1-1 | Viral recognition | [77, 78] |
V02 | S protein | 6VXX1-1-1 | Viral recognition | [77, 78] |
V02R | S protein’s RBD | 6VXX1-1-1 | Viral recognition | [77, 78] |
V03 | Mpro | 6LU7_A | Polyprotein processing | [79] |
V08 | PLpro | 7JRN_A | Polyprotein processing | [19] |
V04 | NSP12 | 7AAP_A | RNA replication | [80] |
V05 | NSP7 | 6M71_C | RNA replication | [81] |
V06 | NSP8 | 6NUR_B | RNA replication | [82] |
V07 | Rdrp-complex (NSP12-NSP7-NSP8) | 6M71_ABC | RNA replication | [81] |
Structural information and PDB entries of viral (V) and host (H) targets included.
Underscore denotes the chain selected from PDB coordinates files.
Molecular docking is a computational method that allows to sample the conformational space and rank the ligand poses through an energy scoring function. It attempts to generate an optimized target-ligand complex conformation with the lowest binding free-energy change estimate, predicting the interaction of the two molecules in the energy minimum. This task is a cyclic process performed by systematic or stochastic search methods. However, the latter is the choice of preference since it increases the probability of finding an energetic global minimum conformation because the search initiates from different random points [27]. For this reason, the results of two or more molecular docking cycles are not necessarily the same due to the random nature of the conformational search method. Therefore, performing as many cycles as necessary to get as close as possible to the energetic global minimum conformation is essential.
Easy customization of this parameter in the developed high-throughput virtual screening code offers the user the possibility of an exhaustive sampling of the conformational space that maximizes the accuracy of target-ligand complex prediction.
We have developed in-house bash scripts that integrate the CB-Dock’s cavity-guided blind molecular docking method, which automatically identifies binding sites by calculating putative cavities through a curvature-based detection approach. Molecular docking analysis is conducted in these putative cavities to sample and rank ligand poses and estimate the best target-ligand complex binding energy scores per cycle.
The pipeline has three phases comprised of nested loops, schematized in Figure 1 as a flowchart. First, each target
Flowchart of the customized high-throughput virtual screening pipeline implemented in this work. Four phases are involved, i) target and ligand molecular modeling (blue), ii) target cavity detection (green), iii) docking box optimization (orange), and iv) target-ligand docking (red).
In our study, we found that the optimal number of independent rounds is
The method we used for automatizing the virtual high-throughput screening process is blind; that is, it does not require any information on the binding site. Hence, we validated its predictions by reproducing the enzymatic targets’ experimental binding complexes. We gathered a set of ligands with available complex co-crystallized data. Eight known enzymatic inhibitors were modeled, optimized, and evaluated under the same methodology conditions as the rest of the ligands included in this study. The ligands in the control set are listed in Table 3.
Target ID | Target name | Ligand | PDB ID | Reference |
---|---|---|---|---|
1. Co-crystallized reproducibility | ||||
INH01 | ACE2 | MLN-4760 | 1R4L | [72] |
INH02 | TMPRSS2 | 4-Guanidinobenzoic acid | 7MEQ | [74] |
INH03 | Cathepsin B | Nitroxoline | 3AI8 | [75] |
INH04 | Cathepsin L | 4-Bipheylacetyl-cys-(D)-ARG-TYR -N-(2-Phenylethyl) Amide | 2NQD | [76] |
INV01 | Mpro | Narlaprevir | 7JYC | [19] |
INV02 | NSP12 | Remdesivir | 7BV2 | [84] |
INV03 | NSP12 | Favipiravir | 7AAP | [80] |
INV04 | PLpro | GRL0617 | 7JRN | [19] |
2. Negative controla | ||||
INV05 | Spike | Amantadine | NA | [83] |
Modeled ligands to validate that the method is capable of reproducing the co-crystallized complex conformations and previous
Does not prevent ACE2-Spike interaction despite inhibiting
Furthermore, at this time, a small drug-like co-crystallized molecule in complex with the spike homotrimer does not yet exist. We included amantadine (INV05) in our set as a negative control since it inhibits the SARS-CoV-2 infection but does not prevent spike-ACE2 interaction [83].
We inspected the top 10 size-ranked putative cavity sites screened for each target. We selected those that either had the active site (targets ACE2, TMPRSS2, cathepsin B/L, Mpro, and NSP12), or were inside a quaternary interface (targets spike, PLpro, and Rdrp). We selected the
We found that the
Target-ligand complex superimposition of native co-crystallized inhibitors (yellow) and the best-predicted ligand conformation after
After doing all the blind docking calculations with an extended conformation sampling, we analyzed the most negative energy scores. We performed a Z-score transformation of the data for each independent column in the matrix (targets
Target (columns) and ligand (rows) complex docking results. Heatmap of binding free-energy change estimates, using a color-based code according to the Z-score value through column analysis. Targets are grouped as host proteins (blue) and virus proteins (pink). Ligands are grouped by control set (green), potential repurposing drugs (orange), and others (brown). IDs correspond to those defined in
Since each column gathers the results for a different target, it is thus possible to identify which ligands had the best scores for each target (in green). It is worth noting that cathepsin L (H05) and PLpro (V08) co-crystallized inhibitors give a good binding free-energy estimate. Most of the co-crystallized inhibitors remained near the mean (in black, with respect to the experimental drug set), except for amantadine (INV05), which presents a positive Z-score value for the spike’s RBD (in red). The latter is concomitant to previous works, where amantadine fails to prevent the spike-ACE2 quaternary interaction [83].
Out of the 47 drugs screened, nine showed potential inhibition against viral or host targets of the SARS-CoV-2 infection cycle. Saquinavir, simeprevir, nilotinib, an isatin-derivative, telmisartan, tegobuvir, qingdainone, rac5c, and nafamostat achieved the selection criteria. Interestingly, all but rac5c and nafamostat showed the best scores against more than one target. The schematic representation of these results is summarized in Table 4.
ID | Drug | Target | VINA score | Z-scorea |
---|---|---|---|---|
RPC05 | Saquinavir | ACE2 (H00) | −12.9 | −1.70 |
RPB05 | Isatin-derivative | ACE2 (H01) | −10.7 | −2.06 |
RPC04 | Nilotinib | −10.2 | −1.72 | |
RPD01 | rac5c | −9.9 | −1.51 | |
RPC04 | Nilotinib | ACE2 (H02) | −10.7 | −1.85 |
RPC09 | Simeprevir | −10.4 | −1.62 | |
RPC04 | Nilotinib | TMPRSS2 (H03) | −8.9 | −1.58 |
RPC05 | Saquinavir | −8.8 | −1.49 | |
RPC04 | Nilotinib | Cathepsin B (H04) | −9.6 | −1.64 |
RPC09 | Simeprevir | −10.3 | −2.20 | |
RPA02 | Telmisartan | Spike (V02) | −9.4 | −1.63 |
RPB05 | Isatin-derivative | Spike (V01H) | −10.9 | −1.67 |
RPA13 | Qingdainone | Mpro (V03) | −9.4 | −1.56 |
RPC04 | Nilotinib | −9.7 | −1.80 | |
RPC09 | Simeprevir | NSP12 (V04) | −9.1 | −1.60 |
RPA13 | Qingdainone | NSP7 (V05) | −7.4 | −1.69 |
RPC08 | Tegobuvir | −7.3 | −1.59 | |
RPC09 | Simeprevir | −7.6 | −1.89 | |
RPA02 | Telmisartan | NSP8 (V06) | −8.8 | −1.65 |
RPC04 | Nilotinib | −8.9 | −1.73 | |
RPC05 | Saquinavir | −9 | −1.80 | |
RPC09 | Simeprevir | Rdrp (V07) | −10 | −1.96 |
RPA13 | Qingdainone | PLpro (V08) | −9.9 | −1.72 |
RPA14 | Nafamostat | −10.1 | −1.88 | |
RPC04 | Nilotinib | −9.8 | −1.65 | |
RPC08 | Tegobuvir | −9.8 | −1.65 |
Potential drugs for repurposing with the most negative free-energy change score found and their corresponding Z-score value grouped by the target.
Z-scores were calculated by the target.
Also, we inspected the results by ligand, performing a Z-score analysis by row (ligands). Since the rows gather data from the
Target (columns) and ligand (rows) complex docking results. Heatmap of binding free-energy change estimates, using a color-based code according to the Z-score value through row analysis. Targets are grouped as host proteins (blue) and virus proteins (pink). Ligands are grouped by control set (green), potential repurposing drugs (orange), and others (brown). IDs correspond to those defined in
The ligands such as arbidol, colchicine, qingdainone, nafamostat, and carvacrol exhibit a binding preference to PLpro (V08). It is important to highlight the essential function of the protease PLpro for processing the viral proteome and evading the host’s innate immune system. In the latter case, PLpro cleaves off post-translational modifications, such as ubiquitin and ubiquitin-like proteins from cell proteins, disrupting the inflammatory signaling pathway necessary for an appropriate immune response [17, 100]. Noteworthy, the potential PLpro inhibitors we have identified in the present work as repurposed drugs form a
Saquinavir is a peptide-mimetic HIV inhibitor. However, some reports suggest potential inhibitory activity against SARS-CoV-2 proteases [85, 86, 87] and other targets involved in the viral infection, such as the Rdrp replication complex [62, 88] and the spike-ACE2 PPI [89]. In our study, saquinavir showed the best energy scores against TMPRSS2, ACE2, and the NSP8-NSP12 interface of the Rdrp complex, as shown in Figure 5. The transmembrane serine protease 2 (TMPRRS2) is essential in several viral infections. Previous reports have shown that the inhibition of this target significantly reduces SARS-CoV-2 entry in lung cells at nM concentrations and therefore the viral infection [90]. Saquinavir also presented the best energy scores against the ACE2 active site, a critical host target needed to initiate entry through the formation of the spike-ACE2 quaternary complex. In this scenario, conformational changes upon ligand binding into the catalytic cavity may shift the relative positions of the receptor’s interface residues that bind to the spike protein and prevent the anchoring of the spike on host cells [91]. However, because saquinavir targets the catalytic site of ACE2, the main activity of this enzyme in the renin-angiotensin system requires further investigation of its biological effect as a competitive inhibitor [92]. In addition, our results show that this drug targets the Rdrp replication complex, which is consistent with the previous results reported in the literature [62, 93]. Interestingly, saquinavir appears to target two essential steps, compromising the entry and viral replication of the SARS-CoV-2.
Target-ligand complex conformations of potential drugs for repurposing. Molecular docking against viral and host targets relevant in the SARS-CoV-2 infection cycle. A. Superposition of ACE2 target (H00, H01, and H02) docked with saquinavir (cyan), isatin-derivative (red), nilotinib (pink), rac5c (brown), and simeprevir (yellow). B. TMPRSS2 docked with saquinavir (cyan) and nilotinib (pink). C. Spike docked with telmisartan (purple) and isatin-derivative (red). D. Cathepsin B docked with nilotinib and simeprevir (yellow). E. Mpro docked with nilotinib (pink) and qingdainone (orange). F. PLpro docked with nafamostat (green), nilotinib (pink), qingdainone (orange), and tegobuvir (dark orange). G. Superposition of NSP12 and NSP7 and NSP8 cofactors docked with simeprevir (yellow), tegobuvir (dark orange), nilotinib (pink), telmisartan (purple), qingdainone (orange), and saquinavir (cyan), created with the visual molecular dynamics (VMD) [
On the other hand, simeprevir also showed the best energy scores on targets relevant to viral entry and replication, including the active cavities of ACE2, cathepsin B, NSP12, and the Rdrp complex interface. We show a molecular visualization of these results in panels A, C, and G of Figure 5. This drug is a protease inhibitor that has presented potent
Nilotinib is used to treat chronic myelogenous leukemia as a Bcr-Abl tyrosine kinase antagonist. Our results suggest the potential inhibition of six targets involved in the SARS-CoV-2 infection process, including the catalytic cavities of enzyme targets ACE2, TMPRSS2, cathepsin B, Mpro, and the PLpro-ISG15 and Rdrp’s NSP8-NSP12 interfaces. We show a molecular visualization of these results in Figure 5. Reports suggest that nilotinib can inhibit the SARS-CoV and SARS-CoV-2 infection processes, but not MERS-CoV. Interestingly, the latter does not use ACE2 as a cell receptor [97, 98]. This observation is particularly interesting since other reports suggest that nilotinib can destabilize the SARS-CoV-2 spike-ACE2 complex [63]. According to our results, nilotinib might prevent the spike priming and activation since it showed the best energy scores against TMPRSS2 and cathepsin B at the active site cavities. These findings represent a potential inhibition of two independent priming pathways. Moreover, nilotinib potentially inhibits the Mpro and Rdrp complex and is consistent with previous
Interestingly, nilotinib also had the best energy scores against PLpro. In addition to PLpro’s essential protease activity in the processing of pp1a polyprotein, it is also implicated in host immune innate response evasion mechanisms as described in Section 4.4. The inhibition of PLpro decreases the exacerbated immune response, as described by other members of the Bcr-Abl inhibitors family, for example, ponatinib, which protects against cytokine storm in mouse models [101, 102].
Isatin-derivatives have shown potential antiviral properties, some of them with promising results against HCV, SARS-CoV [103, 104], and SARS-CoV-2 [53]. In particular, the compound 1-(naphthalen-2-ylmethyl)-2,3-dioxoindoline-5-carboxamide inhibits Mpro from SARS-CoV-2. Therefore, we decided to evaluate it against our whole set of targets. It presented the best score against the ACE2 active site, which might disrupt the spike-ACE2 interaction as discussed previously (see Section 5.1). Moreover, it also showed the best energy scores against the spike protein, precisely in the quaternary interface region of the homotrimer complex, and thus a plausible termination of the viral cycle at an early stage in the replication process.
Telmisartan is an anti-antihypertensive. There is evidence of a morbidity and mortality reduction in hospitalized patients infected with SARS-CoV-2 treated with this drug [105]. Telmisartan showed the best energy scores against a spike’s cavity in the homotrimer quaternary interface. Therefore, the isatin-derivative could inhibit two targets involved in the viral entry (spike and ACE2), while telmisartan might prevent the spike homotrimer formation and the Rdrp complex. We show the molecular visualization of these results in panels A, C, and G of Figure 5.
Tegobuvir is a non-nucleoside inhibitor of the NS5B polymerase of HCV. Our results suggest that this drug may prevent the formation of the Rdrp quaternary complex. Previously,
In addition, qingdainone also showed the potential inhibitory activity on Mpro active site, suggesting that this drug might completely disrupt the polyprotein processing stage by targeting both proteases, Mpro and PLpro. We show a molecular visualization of these results in Figure 5.
We included nafamostat and rac5c in our ligand sets due to evidence suggesting their inhibitory capacity against TMPRSS2 [108] and PLpro [18], respectively. Neither ligand achieved the selection criteria for their expected targets despite being on the borderline with scores of −8.3 and − 9.3 kcal/mol, which indicates the selection criteria’s exhaustiveness. However, nafamostat does achieve the best scores against PLpro’s USP domain, while rac5c presented the best score on the ACE2 active site. We show these results in panels A and F of Figure 5.
We have theoretically identified nine drugs or compounds for potential drug repurposing against SARS-CoV-2 through a cavity-based blind molecular docking protocol (Figure 6). Interestingly, seven of them present potential inhibitory activity on multiple targets at different stages of the viral infection cycle, including innate immune evasion. We have implemented an in-house high-throughput virtual screening pipeline that successfully reproduces experimental data and findings from previous works. After the target’s cavity detection and ranking by surface area, we used the pipeline to perform the numerous independent blind molecular docking rounds to achieve a sufficiently extensive conformational target-ligand complex search.
Repurposing drugs (left) with corresponding potential inhibitory activity on multiple viral or host targets (right).
Experimental design is a critical step in every scientific study, for example, method validation by including a control group. Nonetheless, one has to be wary of the limitations of the methodology employed. In this case, molecular docking can be a good estimator for the most energetically favorable
We analyzed the molecular binding predictions through rigorous visualization and Z-score-based statistical algorithms to identify the potential drugs for repurposing. In this context, our findings suggest that:
Saquinavir and simeprevir could target viral entry and Rdrp complex quaternary formation,
Nilotinib could target viral entry, polyprotein processing, and Rdrp quaternary complex formation,
An isatin-derivative and telmisartan could target SARS-CoV-2 entry into the host,
Tegobuvir, qingdainone, and nafamostat could target quaternary interface Rdrp regions, and
Nafamostat and rac5c could be potential inhibitors of PLpro and ACE2.
These results are relevant in understanding the SARS-CoV-2 drug’s molecular mechanisms and further clinical treatment development, either at a single or multi-target activity.
The authors acknowledge funding from the Consejo Nacional de Ciencia y Tecnología México [grant number 132376] and Fondo Sectorial de Investigación para la Educación [grant number A1-S-17041] to MCT. All computations and analyses reported here were performed at the bmdhpc computing resources of the Biomolecular Diversity Lab (tripplab.com) at CINVESTAV Unidad Monterrey, México.
The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.
Li-Ta | H00 | H01 | H02 | H03 | H04 | H05 | V01 | V01H | V02 | V02R | V03 | V04 | V05 | V06 | V07 | V08 |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
INH01 | −9.5 | −7.3 | −7.7 | |||||||||||||
INH02 | −6 | |||||||||||||||
INH03 | −6.2 | |||||||||||||||
INH04 | −9 | |||||||||||||||
INV01 | −7.2 | |||||||||||||||
INV02 | −7.5 | −5.5 | −6.7 | −7.8 | ||||||||||||
INV03 | −7.6 | −5.7 | −6.6 | −8.6 | ||||||||||||
INV04 | −9.8 | |||||||||||||||
INV05 | −6 | −6 | −4.1 | −3.4 |
VINA scores of the conformation with the lowest scores after 30 independent cycles of each target–ligand pair for the enzymatic known inhibitors included.
Li-Ta | H00 | H01 | H02 | H03 | H04 | H05 | V01 | V01H | V02 | V02R | V03 | V04 | V05 | V06 | V07 | V08 |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
RPA01 | −9.8 | −8.5 | −7.9 | −6.8 | −8 | −6.6 | −9.7 | −9.6 | −8.9 | −6.8 | −7.7 | −7.5 | −5.6 | −6.5 | −7.1 | −8.8 |
RPA02 | −11.4 | −8.8 | −10.3 | −8.2 | −8.1 | −7.5 | −9.3 | −10 | −9.4 | −7.7 | −8.7 | −8.2 | −6.9 | −8.8 | −9.2 | −9.2 |
RPA03 | −8.6 | −6.5 | −6.9 | −5.9 | −6.3 | −5.9 | −7.6 | −7.3 | −5.9 | −5.7 | −6.6 | −5.9 | −4.7 | −5.9 | −5.9 | −7.5 |
RPA04 | −9.8 | −8.7 | −8.7 | −7.6 | −7.6 | −7.8 | −9.5 | −9.4 | −7.8 | −6.6 | −7.4 | −7.3 | −6 | −7 | −7.6 | −8.4 |
RPA05 | −6.1 | −5 | −6.6 | −4.8 | −5.3 | −4.9 | −6.8 | −6.7 | −4.6 | −4.2 | −4.6 | −4.2 | −4.3 | −4.5 | −4.3 | −6 |
RPA06 | −7.3 | −7 | −7.6 | −5.7 | −5.8 | −5.9 | −7.8 | −7.8 | −6.4 | −5.2 | −6.1 | −5 | −4.5 | −5.8 | −5.3 | −7.3 |
RPA07 | −7.3 | −6.4 | −7.7 | −5.9 | −6 | −5.9 | −7.9 | −7.9 | −6.4 | −5.3 | −6.3 | −5.6 | −4.7 | −5.9 | −5.7 | −7.2 |
RPA08 | −9.5 | −8 | −7.9 | −7.3 | −7.9 | −6.7 | −8.9 | −8.9 | −8.3 | −5.9 | −8.2 | −6.9 | −5.3 | −6.2 | −6.9 | −8.1 |
RPA09 | −8.9 | −6.3 | −7.1 | −5.9 | −7 | −6.8 | −7.4 | −7.2 | −6.3 | −5.7 | −7 | −6.2 | −5.7 | −5.9 | −6.9 | −7.7 |
RPA10 | −4.7 | −5 | −5.1 | −3.9 | −4.3 | −4 | −5.2 | −5.2 | −4.1 | −3.4 | −4.5 | −3.6 | −3 | −3.6 | −3.7 | −4.7 |
RPA11 | −7.8 | −6.6 | −7.5 | −5.6 | −6.7 | −6 | −7.8 | −7.8 | −6.2 | −5.3 | −6.6 | −5.1 | −5.1 | −5.4 | −5.6 | −7.3 |
RPA12 | −11.6 | −9.1 | −8.9 | −8.7 | −8.8 | −8 | −9.2 | −9 | −7.8 | −7.5 | −8.9 | −8.9 | −6.5 | −7.1 | −8.8 | −8.3 |
RPA13 | −12 | −7.7 | −9.5 | −8 | −8.5 | −7.7 | −8.8 | −9.1 | −7.9 | −7 | −9.4 | −8 | −7.4 | −7.3 | −8.6 | −9.9 |
RPA14 | −10.5 | −9.2 | −9.5 | −8.3 | −8.3 | −7.8 | −9.8 | −9.9 | −8.2 | −7 | −8.5 | −8.4 | −6.8 | −7.7 | −8.9 | −10.1 |
RPA15 | −10.9 | −9.4 | −9.3 | −7.8 | −7.8 | −8.2 | −10.1 | −9.9 | −8.7 | −7.2 | −8.7 | −8 | −6 | −8 | −7.9 | −9 |
RPB01 | −11.1 | −8.7 | −9.3 | −7.6 | −8.3 | −7.7 | −9.1 | −9.8 | −8.8 | −7.5 | −8.9 | −7.3 | −5.8 | −7.8 | −8.3 | −8 |
RPB02 | −11.3 | −7.8 | −8.8 | −7.5 | −7.7 | −7.1 | −8.4 | −9.3 | −8.2 | −6.8 | −7.7 | −7.4 | −5.7 | −7.4 | −7.9 | −7.5 |
RPB03 | −10.6 | −7.8 | −8.5 | −7.5 | −8.6 | −7.6 | −9.7 | −9.6 | −8.6 | −6.9 | −8 | −7.3 | −5.9 | −6.8 | −7.6 | −7.8 |
RPB04 | −11.8 | −8 | −9 | −7.6 | −8.1 | −7.6 | −8 | −8.6 | −8.2 | −7.5 | −7.9 | −7.2 | −6.2 | −7.4 | −8.2 | −8 |
RPB05 | −10.4 | −10.7 | −9 | −8.2 | −8.9 | −8.4 | −11 | −10.9 | −8 | −6.9 | −8.3 | −7.6 | −6.2 | −8.1 | −7.6 | −9.7 |
RPB06 | −10.7 | −7.7 | −9.4 | −7.5 | −8.8 | −7.4 | −9.1 | −9.7 | −7.9 | −6.7 | −7.8 | −7.3 | −6.1 | −7.6 | −8.2 | −8 |
RPB07 | −8 | −6.3 | −7.3 | −6.3 | −7.6 | −6.4 | −8.3 | −8.1 | −6.8 | −5.8 | −7 | −6.6 | −5 | −5.5 | −6.8 | −7.6 |
RPB08 | −11.6 | −8.6 | −9 | −7.6 | −8.2 | −7.6 | −8.6 | −8.5 | −8.4 | −7.4 | −7.6 | −7.2 | −6.1 | −7.1 | −7.9 | −8.2 |
RPC01 | −7.6 | −6.1 | −7.2 | −7 | −6.7 | −5.9 | −7.7 | −7.7 | −6.5 | −5.4 | −6.6 | −5.9 | −4.5 | −5.1 | −6.4 | −6.4 |
RPC02 | −10.3 | −7.7 | −8.3 | −7.7 | −8.2 | −7.3 | −9.9 | −9.8 | −7.4 | −7.2 | −8.1 | −7.2 | −6.1 | −7 | −7.3 | −8 |
RPC03 | −8.1 | −6.7 | −7.8 | −7 | −7.2 | −5.9 | −8.6 | −8.6 | −7.1 | −5.8 | −7.4 | −6.8 | −5.1 | −5.8 | −6.6 | −6.9 |
RPC04 | −12.3 | −10.2 | −10.7 | −8.9 | −9.6 | −8.3 | −10 | −10.7 | −8.8 | −7.9 | −9.7 | −8.6 | −7.2 | −8.9 | −9.1 | −9.8 |
RPC05 | −12.9 | −8.7 | −9.3 | −8.8 | −8.2 | −8.4 | −10 | −10.4 | −8.6 | −7.7 | −9.1 | −8 | −6.5 | −9 | −8.6 | −8.4 |
RPC06 | −11 | −9.8 | −9.8 | −7.7 | −8.6 | −7.6 | −9.9 | −9.6 | −7.6 | −7.7 | −8.1 | −7.6 | −6.2 | −8 | −8.1 | −8.1 |
RPC07 | −12.5 | −8.9 | −9.8 | −8.6 | −9 | −7.8 | −8.9 | −9.5 | −8.4 | −7.2 | −9.1 | −8.7 | −6.9 | −8.1 | −8.8 | −8.9 |
RPC08 | −11.5 | −9.5 | −10.2 | −7.9 | −9 | −8.1 | −9.7 | −9.7 | −8.6 | −8.1 | −8.6 | −8.8 | −7.3 | −8.1 | −8.7 | −9.8 |
RPC09 | −10.9 | −9.3 | −10.4 | −8.6 | −10.3 | −8.6 | −4.9 | −8.7 | −9.1 | −8.1 | −8.4 | −9.1 | −7.6 | −8.3 | −10 | −9.3 |
RPC10 | −11.2 | −8.7 | −9 | −7.7 | −8.4 | −7.9 | −9.2 | −9.2 | −8.6 | −7.7 | −8.6 | −7.8 | −6.4 | −7.9 | −8.1 | −8.7 |
RPC11 | −8.5 | −7.4 | −9.1 | −7.7 | −8.8 | −7.4 | −8 | −7.9 | −8.7 | −6.5 | −7.7 | −8.8 | −6.8 | −6.6 | −8.9 | −7.2 |
RPC12 | −10.3 | −8.3 | −8.9 | −7.7 | −8.1 | −7.3 | −8.9 | −8.7 | −8.1 | −6.7 | −8.2 | −7.4 | −5.8 | −7.6 | −7.5 | −7.6 |
RPC13 | −6.3 | −5.5 | −5.9 | −6.2 | −5.7 | −5.4 | −6.2 | −6.2 | −6.5 | −4.4 | −5.3 | −4.7 | −4.1 | −4.5 | −5.5 | −5.5 |
RPC14 | −6.4 | −5.5 | −6 | −6.3 | −5.8 | −5.4 | −6.2 | −6.1 | −6.6 | −4.3 | −5.1 | −4.6 | −3.9 | −4.4 | −5.4 | −5.7 |
RPD01 | −11 | −9.9 | −9 | −8.1 | −7.9 | −8.3 | −8.8 | −8.6 | −8.1 | −7 | −7.7 | −7.4 | −6.4 | −7.8 | −7.7 | −9.1 |
EXT01 | −6.3 | −5.1 | −5.5 | −5.9 | −5.8 | −5.3 | −6.2 | −6.2 | −6.2 | −4.4 | −5.1 | −4.9 | −3.9 | −4.3 | −5.3 | −5.6 |
EXT02 | −10 | −8.4 | −8.5 | −6.5 | −7.1 | −7.2 | −9.8 | −9.6 | −7.6 | −6.3 | −7.3 | −6.6 | −6 | −7 | −7.1 | −7.2 |
EXT03 | −9 | −7.8 | −8.3 | −6.5 | −6.9 | −6.8 | −10.1 | −10 | −7.1 | −5.7 | −6.8 | −6.1 | −5.7 | −6.4 | −6.8 | −6.9 |
EXT04 | −8 | −9 | −9.6 | −8.4 | −8.2 | −7.9 | 0.9 | −3.1 | −8.2 | −7.5 | −8.2 | −8.7 | −7.2 | −7.2 | −9.3 | −8.2 |
EXT05 | −6.2 | −6.1 | −7.2 | −6.5 | −6.9 | −5.6 | −6.9 | −6.7 | −6.1 | −5.4 | −7.4 | −7 | −5.3 | −5.7 | −7.4 | −5.2 |
EXT06 | −9.6 | −6.9 | −7.4 | −6.9 | −7.6 | −7.5 | −5.1 | −5.5 | −6.5 | −6 | −7.7 | −7.6 | −5.4 | −6 | −8 | −6.9 |
EXT07 | −9.9 | −7.3 | −8.1 | −6.7 | −7.5 | −6.3 | −7.2 | −7.8 | −6.7 | −6.3 | −7.2 | −6.6 | −5.9 | −6.5 | −6.5 | −7.1 |
EXT08 | −6 | −6.8 | −6.1 | −4.9 | −5 | −5 | −6 | −6 | −5.3 | −4.4 | −4.8 | −4 | −4.4 | −5 | −4.5 | −6.5 |
EXT09 | −11.2 | −7 | −9.2 | −6.7 | −8.6 | −6.6 | −7.8 | −7.8 | −7.6 | −6.4 | −7 | −7.4 | −6.4 | −7.2 | −7 | −6.1 |
EXT10 | −9.7 | −7.7 | −9 | −7.3 | −8.3 | −6.1 | −7.1 | −7.8 | −6.8 | −6.7 | −7.7 | −7.4 | −6.3 | −6.9 | −7.6 | −6 |
VINA scores of the conformation with the lowest scores after 30 independent cycles of each target–ligand pair for the set of ligands evaluated.
ACE2 | |
COVID-19 | Coronavirus disease 19 |
HCV | |
HTVS | |
ISG15 | |
MERS-CoV | Middle East respiratory syndrome coronavirus |
Mpro | |
PLpro | |
PPI | |
RBD | |
Rdrp complex | RNA-dependent RNA polymerase complex |
SARS-CoV | Severe acute respiratory syndrome coronavirus |
SARS-CoV-2 | Severe acute respiratory syndrome coronavirus 2 |
ssRNA | |
TMPRSS2 | Transmembrane serine protease 2 |
We believe financial barriers should not prevent researchers from publishing their findings. With the need to make scientific research more publicly available and support the benefits of Open Access, more and more institutions and funders are dedicating resources to assist faculty members and researchers cover Open Access Publishing Fees (OAPFs). In addition, IntechOpen provides several further options presented below, all of which are available to researchers, and could secure the financing of your Open Access publication.
",metaTitle:"Waiver Policy",metaDescription:"We feel that financial barriers should never prevent researchers from publishing their research. With the need to make scientific research more publically available and support the benefits of Open Access, more institutions and funders have dedicated funds to assist their faculty members and researchers cover the APCs associated with publishing in Open Access. Below we have outlined several options available to secure financing for your Open Access publication.",metaKeywords:null,canonicalURL:"/page/waiver-policy",contentRaw:'[{"type":"htmlEditorComponent","content":"At IntechOpen, the majority of OAPFs are paid by an Author’s institution or funding agency - Institutions (73%) vs. Authors (23%).
\\n\\nThe first step in obtaining funds for your Open Access publication begins with your institution or library. IntechOpen’s publishing standards align with most institutional funding programs. Our advice is to petition your institution for help in financing your Open Access publication.
\\n\\nHowever, as Open Access becomes a more commonly used publishing option for the dissemination of scientific and scholarly content, in addition to institutions, there are a growing number of funders who allow the use of grants for covering OA publication costs, or have established separate funds for the same purpose.
\\n\\nPlease consult our Open Access Funding page to explore some of these funding opportunities and learn more about how you could finance your IntechOpen publication. Keep in mind that this list is not definitive, and while we are constantly updating and informing our Authors of new funding opportunities, we recommend that you always check with your institution first.
\\n\\nFor Authors who are unable to obtain funding from their institution or research funding bodies and still need help in covering publication costs, IntechOpen offers the possibility of applying for a Waiver.
\\n\\nOur mission is to support Authors in publishing their research and making an impact within the scientific community. Currently, 14% of Authors receive full waivers and 6% receive partial waivers.
\\n\\nWhile providing support and advice to all our international Authors, waiver priority will be given to those Authors who reside in countries that are classified by the World Bank as low-income economies. In this way, we can help ensure that the scientific work being carried out can make an impact within the worldwide scientific community, no matter where an Author might live.
\\n\\nThe application process is open after your submitted manuscript has been accepted for publication. To apply, please fill out a Waiver Request Form and send it to your Author Service Manager. If you have an official letter from your university or institution showing that funds for your OA publication are unavailable, please attach that as well. The Waiver Request will normally be addressed within one week from the application date. All chapters that receive waivers or partial waivers will be designated as such online.
\\n\\nDownload Waiver Request Form
\\n\\nFeel free to contact us at funders@intechopen.com if you have any questions about Funding options or our Waiver program. If you have already begun the process and require further assistance, please contact your Author Service Manager, who is there to assist you!
\\n\\nNote: All data represented above was collected by IntechOpen from 2013 to 2017.
\\n"}]'},components:[{type:"htmlEditorComponent",content:'At IntechOpen, the majority of OAPFs are paid by an Author’s institution or funding agency - Institutions (73%) vs. Authors (23%).
\n\nThe first step in obtaining funds for your Open Access publication begins with your institution or library. IntechOpen’s publishing standards align with most institutional funding programs. Our advice is to petition your institution for help in financing your Open Access publication.
\n\nHowever, as Open Access becomes a more commonly used publishing option for the dissemination of scientific and scholarly content, in addition to institutions, there are a growing number of funders who allow the use of grants for covering OA publication costs, or have established separate funds for the same purpose.
\n\nPlease consult our Open Access Funding page to explore some of these funding opportunities and learn more about how you could finance your IntechOpen publication. Keep in mind that this list is not definitive, and while we are constantly updating and informing our Authors of new funding opportunities, we recommend that you always check with your institution first.
\n\nFor Authors who are unable to obtain funding from their institution or research funding bodies and still need help in covering publication costs, IntechOpen offers the possibility of applying for a Waiver.
\n\nOur mission is to support Authors in publishing their research and making an impact within the scientific community. Currently, 14% of Authors receive full waivers and 6% receive partial waivers.
\n\nWhile providing support and advice to all our international Authors, waiver priority will be given to those Authors who reside in countries that are classified by the World Bank as low-income economies. In this way, we can help ensure that the scientific work being carried out can make an impact within the worldwide scientific community, no matter where an Author might live.
\n\nThe application process is open after your submitted manuscript has been accepted for publication. To apply, please fill out a Waiver Request Form and send it to your Author Service Manager. If you have an official letter from your university or institution showing that funds for your OA publication are unavailable, please attach that as well. The Waiver Request will normally be addressed within one week from the application date. All chapters that receive waivers or partial waivers will be designated as such online.
\n\nDownload Waiver Request Form
\n\nFeel free to contact us at funders@intechopen.com if you have any questions about Funding options or our Waiver program. If you have already begun the process and require further assistance, please contact your Author Service Manager, who is there to assist you!
\n\nNote: All data represented above was collected by IntechOpen from 2013 to 2017.
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In 2021 he has been awarded the “Raul Isturiz Award” Medal of the API. Also, in 2021, he was awarded with the “Jose Felix Patiño” Asclepius Staff Medal of the Colombian Medical College, due to his scientific contributions to COVID-19 during the pandemic. He is currently the Editor in Chief of the journal Travel Medicine and Infectious Diseases. His Scopus H index is 47 (Google Scholar H index, 68).",institutionString:"Institución Universitaria Visión de las Américas, Colombia",institution:null},{id:"332819",title:"Dr.",name:"Chukwudi Michael",middleName:"Michael",surname:"Egbuche",slug:"chukwudi-michael-egbuche",fullName:"Chukwudi Michael Egbuche",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/332819/images/14624_n.jpg",biography:"I an Dr. Chukwudi Michael Egbuche. 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The preliminary objectives of the study are to understand and develop the evidence-based tools and interventions for the control and prevention of malaria in different sites of the INDIA. Alongside, with the help of next-generation genomics study, the team has studied the antimalarial drug resistance in India. Further, he has extended his research in the development of Humanized mice for the study of liver-stage malaria and identification of molecular marker(s) for the Artemisinin resistance. At present, his research focuses on understanding the role of B cells in the activation of CD8+ T cells in malaria. 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She is currently an Adjunct Professor at Feevale University in Medicine and Biomedicine courses and a permanent professor of the Academic Master\\'s Degree in Virology. She has experience in the field of Microbiology, with an emphasis on Bacteriology, working mainly on the following topics: bacteriophages, bacterial resistance, clinical microbiology and food microbiology.",institutionString:null,institution:{name:"Universidade Feevale",country:{name:"Brazil"}}},{id:"229220",title:"Dr.",name:"Amjad",middleName:"Islam",surname:"Aqib",slug:"amjad-aqib",fullName:"Amjad Aqib",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/229220/images/system/229220.png",biography:"Dr. Amjad Islam Aqib obtained a DVM and MSc (Hons) from University of Agriculture Faisalabad (UAF), Pakistan, and a PhD from the University of Veterinary and Animal Sciences Lahore, Pakistan. Dr. Aqib joined the Department of Clinical Medicine and Surgery at UAF for one year as an assistant professor where he developed a research laboratory designated for pathogenic bacteria. Since 2018, he has been Assistant Professor/Officer in-charge, Department of Medicine, Manager Research Operations and Development-ORIC, and President One Health Club at Cholistan University of Veterinary and Animal Sciences, Bahawalpur, Pakistan. He has nearly 100 publications to his credit. His research interests include epidemiological patterns and molecular analysis of antimicrobial resistance and modulation and vaccine development against animal pathogens of public health concern.",institutionString:"Cholistan University of Veterinary and Animal Sciences",institution:{name:"University of Agriculture Faisalabad",country:{name:"Pakistan"}}},{id:"333753",title:"Dr.",name:"Rais",middleName:null,surname:"Ahmed",slug:"rais-ahmed",fullName:"Rais Ahmed",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/333753/images/20168_n.jpg",biography:null,institutionString:null,institution:{name:"University of Agriculture Faisalabad",country:{name:"Pakistan"}}},{id:"62900",title:"Prof.",name:"Fethi",middleName:null,surname:"Derbel",slug:"fethi-derbel",fullName:"Fethi Derbel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/62900/images/system/62900.jpeg",biography:"Professor Fethi Derbel was born in 1960 in Tunisia. He received his medical degree from the Sousse Faculty of Medicine at Sousse, University of Sousse, Tunisia. He completed his surgical residency in General Surgery at the University Hospital Farhat Hached of Sousse and was a member of the Unit of Liver Transplantation in the University of Rennes, France. He then worked in the Department of Surgery at the Sahloul University Hospital in Sousse. Professor Derbel is presently working at the Clinique les Oliviers, Sousse, Tunisia. His hospital activities are mostly concerned with laparoscopic, colorectal, pancreatic, hepatobiliary, and gastric surgery. He is also very interested in hernia surgery and performs ventral hernia repairs and inguinal hernia repairs. He has been a member of the GREPA and Tunisian Hernia Society (THS). During his residency, he managed patients suffering from diabetic foot, and he was very interested in this pathology. For this reason, he decided to coordinate a book project dealing with the diabetic foot. Professor Derbel has published many articles in journals and collaborates intensively with IntechOpen Access Publisher as an editor.",institutionString:"Clinique les Oliviers",institution:null},{id:"300144",title:"Dr.",name:"Meriem",middleName:null,surname:"Braiki",slug:"meriem-braiki",fullName:"Meriem Braiki",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/300144/images/system/300144.jpg",biography:"Dr. Meriem Braiki is a specialist in pediatric surgeon from Tunisia. She was born in 1985. She received her medical degree from the University of Medicine at Sousse, Tunisia. She achieved her surgical residency training periods in Pediatric Surgery departments at University Hospitals in Monastir, Tunis and France.\r\nShe is currently working at the Pediatric surgery department, Sidi Bouzid Hospital, Tunisia. Her hospital activities are mostly concerned with laparoscopic, parietal, urological and digestive surgery. She has published several articles in diffrent journals.",institutionString:"Sidi Bouzid Regional Hospital",institution:null},{id:"229481",title:"Dr.",name:"Erika M.",middleName:"Martins",surname:"de Carvalho",slug:"erika-m.-de-carvalho",fullName:"Erika M. de Carvalho",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/229481/images/6397_n.jpg",biography:null,institutionString:null,institution:{name:"Oswaldo Cruz Foundation",country:{name:"Brazil"}}},{id:"186537",title:"Prof.",name:"Tonay",middleName:null,surname:"Inceboz",slug:"tonay-inceboz",fullName:"Tonay Inceboz",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/186537/images/system/186537.jfif",biography:"I was graduated from Ege University of Medical Faculty (Turkey) in 1988 and completed his Med. PhD degree in Medical Parasitology at the same university. I became an Associate Professor in 2008 and Professor in 2014. I am currently working as a Professor at the Department of Medical Parasitology at Dokuz Eylul University, Izmir, Turkey.\n\nI have given many lectures, presentations in different academic meetings. I have more than 60 articles in peer-reviewed journals, 18 book chapters, 1 book editorship.\n\nMy research interests are Echinococcus granulosus, Echinococcus multilocularis (diagnosis, life cycle, in vitro and in vivo cultivation), and Trichomonas vaginalis (diagnosis, PCR, and in vitro cultivation).",institutionString:"Dokuz Eylül University",institution:{name:"Dokuz Eylül University",country:{name:"Turkey"}}},{id:"71812",title:"Prof.",name:"Hanem Fathy",middleName:"Fathy",surname:"Khater",slug:"hanem-fathy-khater",fullName:"Hanem Fathy Khater",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/71812/images/1167_n.jpg",biography:"Prof. Khater is a Professor of Parasitology at Benha University, Egypt. She studied for her doctoral degree, at the Department of Entomology, College of Agriculture, Food and Natural Resources, University of Missouri, Columbia, USA. She has completed her Ph.D. degrees in Parasitology in Egypt, from where she got the award for “the best scientific Ph.D. dissertation”. She worked at the School of Biological Sciences, Bristol, England, the UK in controlling insects of medical and veterinary importance as a grant from Newton Mosharafa, the British Council. Her research is focused on searching of pesticides against mosquitoes, house flies, lice, green bottle fly, camel nasal botfly, soft and hard ticks, mites, and the diamondback moth as well as control of several parasites using safe and natural materials to avoid drug resistances and environmental contamination.",institutionString:null,institution:{name:"Banha University",country:{name:"Egypt"}}},{id:"99780",title:"Prof.",name:"Omolade",middleName:"Olayinka",surname:"Okwa",slug:"omolade-okwa",fullName:"Omolade Okwa",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/99780/images/system/99780.jpg",biography:"Omolade Olayinka Okwa is presently a Professor of Parasitology at Lagos State University, Nigeria. She has a PhD in Parasitology (1997), an MSc in Cellular Parasitology (1992), and a BSc (Hons) Zoology (1990) all from the University of Ibadan, Nigeria. She teaches parasitology at the undergraduate and postgraduate levels. She was a recipient of a Commonwealth fellowship supported by British Council tenable at the Centre for Entomology and Parasitology (CAEP), Keele University, United Kingdom between 2004 and 2005. She was awarded an Honorary Visiting Research Fellow at the same university from 2005 to 2007. \nShe has been an external examiner to the Department of Veterinary Microbiology and Parasitology, University of Ibadan, MSc programme between 2010 and 2012. She is a member of the Nigerian Society of Experimental Biology (NISEB), Parasitology and Public Health Society of Nigeria (PPSN), Science Association of Nigeria (SAN), Zoological Society of Nigeria (ZSN), and is Vice Chairperson of the Organisation of Women in Science (OWSG), LASU chapter. She served as Head of Department of Zoology and Environmental Biology, Lagos State University from 2007 to 2010 and 2014 to 2016. She is a reviewer for several local and international journals such as Unilag Journal of Science, Libyan Journal of Medicine, Journal of Medicine and Medical Sciences, and Annual Research and Review in Science. \nShe has authored 45 scientific research publications in local and international journals, 8 scientific reviews, 4 books, and 3 book chapters, which includes the books “Malaria Parasites” and “Malaria” which are IntechOpen access publications.",institutionString:"Lagos State University",institution:{name:"Lagos State University",country:{name:"Nigeria"}}},{id:"273100",title:"Dr.",name:"Vijay",middleName:null,surname:"Gayam",slug:"vijay-gayam",fullName:"Vijay Gayam",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/273100/images/system/273100.jpeg",biography:"Dr. Vijay Bhaskar Reddy Gayam is currently practicing as an internist at Interfaith Medical Center in Brooklyn, New York, USA. He is also a Clinical Assistant Professor at the SUNY Downstate University Hospital and Adjunct Professor of Medicine at the American University of Antigua. He is a holder of an M.B.B.S. degree bestowed to him by Osmania Medical College and received his M.D. at Interfaith Medical Center. His career goals thus far have heavily focused on direct patient care, medical education, and clinical research. He currently serves in two leadership capacities; Assistant Program Director of Medicine at Interfaith Medical Center and as a Councilor for the American\r\nFederation for Medical Research. As a true academician and researcher, he has more than 50 papers indexed in international peer-reviewed journals. He has also presented numerous papers in multiple national and international scientific conferences. His areas of research interest include general internal medicine, gastroenterology and hepatology. He serves as an editor, editorial board member and reviewer for multiple international journals. His research on Hepatitis C has been very successful and has led to multiple research awards, including the 'Equity in Prevention and Treatment Award” from the New York Department of Health Viral Hepatitis Symposium (2018) and the 'Presidential Poster Award” awarded to him by the American College of Gastroenterology (2018). He was also awarded 'Outstanding Clinician in General Medicine” by Venus International Foundation for his extensive research expertise and services, perform over and above the standard expected in the advancement of healthcare, patient safety and quality of care.",institutionString:"Interfaith Medical Center",institution:{name:"Interfaith Medical Center",country:{name:"United States of America"}}},{id:"93517",title:"Dr.",name:"Clement",middleName:"Adebajo",surname:"Meseko",slug:"clement-meseko",fullName:"Clement Meseko",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/93517/images/system/93517.jpg",biography:"Dr. Clement Meseko obtained DVM and PhD degree in Veterinary Medicine and Virology respectively. He has worked for over 20 years in both private and public sectors including the academia, contributing to knowledge and control of infectious disease. Through the application of epidemiological skill, classical and molecular virological skills, he investigates viruses of economic and public health importance for the mitigation of the negative impact on people, animal and the environment in the context of Onehealth. \r\nDr. Meseko’s field experience on animal and zoonotic diseases and pathogen dynamics at the human-animal interface over the years shaped his carrier in research and scientific inquiries. He has been part of the investigation of Highly Pathogenic Avian Influenza incursions in sub Saharan Africa and monitors swine Influenza (Pandemic influenza Virus) agro-ecology and potential for interspecies transmission. He has authored and reviewed a number of journal articles and book chapters.",institutionString:"National Veterinary Research Institute",institution:{name:"National Veterinary Research Institute",country:{name:"Nigeria"}}},{id:"158026",title:"Prof.",name:"Shailendra K.",middleName:null,surname:"Saxena",slug:"shailendra-k.-saxena",fullName:"Shailendra K. Saxena",position:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRET3QAO/Profile_Picture_2022-05-10T10:10:26.jpeg",biography:"Professor Dr. Shailendra K. Saxena is a vice dean and professor at King George's Medical University, Lucknow, India. His research interests involve understanding the molecular mechanisms of host defense during human viral infections and developing new predictive, preventive, and therapeutic strategies for them using Japanese encephalitis virus (JEV), HIV, and emerging viruses as a model via stem cell and cell culture technologies. His research work has been published in various high-impact factor journals (Science, PNAS, Nature Medicine) with a high number of citations. He has received many awards and honors in India and abroad including various Young Scientist Awards, BBSRC India Partnering Award, and Dr. JC Bose National Award of Department of Biotechnology, Min. of Science and Technology, Govt. of India. Dr. Saxena is a fellow of various international societies/academies including the Royal College of Pathologists, United Kingdom; Royal Society of Medicine, London; Royal Society of Biology, United Kingdom; Royal Society of Chemistry, London; and Academy of Translational Medicine Professionals, Austria. He was named a Global Leader in Science by The Scientist. He is also an international opinion leader/expert in vaccination for Japanese encephalitis by IPIC (UK).",institutionString:"King George's Medical University",institution:{name:"King George's Medical University",country:{name:"India"}}},{id:"94928",title:"Dr.",name:"Takuo",middleName:null,surname:"Mizukami",slug:"takuo-mizukami",fullName:"Takuo Mizukami",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94928/images/6402_n.jpg",biography:null,institutionString:null,institution:{name:"National Institute of Infectious Diseases",country:{name:"Japan"}}},{id:"233433",title:"Dr.",name:"Yulia",middleName:null,surname:"Desheva",slug:"yulia-desheva",fullName:"Yulia Desheva",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/233433/images/system/233433.png",biography:"Dr. Yulia Desheva is a leading researcher at the Institute of Experimental Medicine, St. Petersburg, Russia. She is a professor in the Stomatology Faculty, St. Petersburg State University. She has expertise in the development and evaluation of a wide range of live mucosal vaccines against influenza and bacterial complications. Her research interests include immunity against influenza and COVID-19 and the development of immunization schemes for high-risk individuals.",institutionString:'Federal State Budgetary Scientific Institution "Institute of Experimental Medicine"',institution:null},{id:"238958",title:"Mr.",name:"Atamjit",middleName:null,surname:"Singh",slug:"atamjit-singh",fullName:"Atamjit Singh",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/238958/images/6575_n.jpg",biography:null,institutionString:null,institution:null},{id:"252058",title:"M.Sc.",name:"Juan",middleName:null,surname:"Sulca",slug:"juan-sulca",fullName:"Juan Sulca",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/252058/images/12834_n.jpg",biography:null,institutionString:null,institution:null},{id:"191392",title:"Dr.",name:"Marimuthu",middleName:null,surname:"Govindarajan",slug:"marimuthu-govindarajan",fullName:"Marimuthu Govindarajan",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/191392/images/5828_n.jpg",biography:"Dr. M. 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He serves as an editorial board member in various national and international scientific journals.",institutionString:null,institution:null},{id:"274660",title:"Dr.",name:"Damodar",middleName:null,surname:"Paudel",slug:"damodar-paudel",fullName:"Damodar Paudel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/274660/images/8176_n.jpg",biography:"I am DrDamodar Paudel,currently working as consultant Physician in Nepal police Hospital.",institutionString:null,institution:null},{id:"241562",title:"Dr.",name:"Melvin",middleName:null,surname:"Sanicas",slug:"melvin-sanicas",fullName:"Melvin Sanicas",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/241562/images/6699_n.jpg",biography:null,institutionString:null,institution:null},{id:"117248",title:"Dr.",name:"Andrew",middleName:null,surname:"Macnab",slug:"andrew-macnab",fullName:"Andrew Macnab",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of British Columbia",country:{name:"Canada"}}},{id:"322007",title:"Dr.",name:"Maria Elizbeth",middleName:null,surname:"Alvarez-Sánchez",slug:"maria-elizbeth-alvarez-sanchez",fullName:"Maria Elizbeth Alvarez-Sánchez",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Universidad Autónoma de la Ciudad de México",country:{name:"Mexico"}}},{id:"337443",title:"Dr.",name:"Juan",middleName:null,surname:"A. 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