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Implications of HIV-1 M group polymorphisms on integrase inhibitor efficacy and resistance: Genetic and structural in silico analyses

dc.contributor.authorLoizidou, Eriketi Z.en
dc.contributor.authorKousiappa, Ioannaen
dc.contributor.authorZeinalipour-Yazdi, Constantinos D.en
dc.contributor.authorVan De Vijver, D. A. M. C.en
dc.contributor.authorKostrikis, Leontios G.en
dc.creatorLoizidou, Eriketi Z.en
dc.creatorKousiappa, Ioannaen
dc.creatorZeinalipour-Yazdi, Constantinos D.en
dc.creatorVan De Vijver, D. A. M. C.en
dc.creatorKostrikis, Leontios G.en
dc.date.accessioned2019-11-21T06:21:13Z
dc.date.available2019-11-21T06:21:13Z
dc.date.issued2009
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/55799
dc.description.abstractThe extensive polymorphisms among HIV-1 subtypes have been implicated in drug resistance development. Integrase inhibitors represent the latest addition to the treatment of HIV-1, and their efficacy and resistance patterns among M group strains are currently under investigation. This study analyzed the intersubtype variation within 108 integrase sequences from seven subtypes. The residues associated with catalytic activity and primary resistance to raltegravir were highly conserved among all strains. Variations were observed in residues associated with secondary resistance. Molecular modeling studies indicated a two-way binding mode of raltegravir that explains the resistance pathways and the implication of nonconservative mutations in integrase-raltegravir interactions. © 2009 American Chemical Society.en
dc.sourceBiochemistryen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-58549116531&doi=10.1021%2fbi8019349&partnerID=40&md5=c4f5861cad0735331036968eedd8497e
dc.subjectarticleen
dc.subjectmathematical modelen
dc.subjectpriority journalen
dc.subjectdrug efficacyen
dc.subjectDNA polymorphismen
dc.subjectPolymorphismen
dc.subjectvirus strainen
dc.subjectgene sequenceen
dc.subjectMutationen
dc.subjectgenetic analysisen
dc.subjectantibiotic resistanceen
dc.subjectenzyme activityen
dc.subjectHuman immunodeficiency virus 1en
dc.subjectHIV-1en
dc.subjectraltegraviren
dc.subjectgenetic variabilityen
dc.subjectprotein motifen
dc.subjectcrystal structureen
dc.subjectcomputer modelen
dc.subjectBinding energyen
dc.subjectDrug resistanceen
dc.subjectPolymorphism, Geneticen
dc.subjectmolecular dockingen
dc.subjectProtein Bindingen
dc.subjectDrug Resistance, Viralen
dc.subjectmolecular modelen
dc.subjectProtein Conformationen
dc.subjectHIV Integraseen
dc.subjectHIV Integrase Inhibitorsen
dc.subjectintegraseen
dc.subjectintegrase inhibitoren
dc.subjectprotein structureen
dc.subjectBinding Sitesen
dc.subjectenzyme active siteen
dc.subjectBinding modesen
dc.subjectCatalytic activitiesen
dc.subjectdrug protein bindingen
dc.subjectgenetic resistanceen
dc.subjectIn-silicoen
dc.subjectIntegrase (IN)en
dc.subjectModels, Molecularen
dc.subjectMolecular modeling studiesen
dc.subjectPyrrolidinonesen
dc.subjectviral geneticsen
dc.titleImplications of HIV-1 M group polymorphisms on integrase inhibitor efficacy and resistance: Genetic and structural in silico analysesen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1021/bi8019349
dc.description.volume48
dc.description.issue1
dc.description.startingpage4
dc.description.endingpage6
dc.author.faculty002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Χημείας / Department of Chemistry
dc.type.uhtypeArticleen
dc.description.notes<p>Manufacturers: Mercken
dc.description.notesCited By :23</p>en
dc.source.abbreviationBiochemistryen
dc.contributor.orcidZeinalipour-Yazdi, Constantinos D. [0000-0002-8388-1549]
dc.gnosis.orcid0000-0002-8388-1549


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