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Structural basis of HIV-1 resistance to AZT by excisionPCR amplification of DNA containing non-standard base pairs by variants of reverse transcriptase from Human Immunodeficiency Virus-1Autosomal dominant and sporadic monocytopenia with susceptibility to mycobacteria, fungi, papillomaviruses, and myelodysplasiaWhy do HIV-1 and HIV-2 use different pathways to develop AZT resistance?Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA.HIV-1 Reverse Transcriptase Structure with RNase H Inhibitor Dihydroxy Benzoyl Naphthyl Hydrazone Bound at a Novel SiteHigh-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations.Crystal engineering of HIV-1 reverse transcriptase for structure-based drug designStructural Basis for the Role of the K65R Mutation in HIV-1 Reverse Transcriptase Polymerization, Excision Antagonism, and Tenofovir ResistanceStructure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active SiteStructural and Functional Analyses of the Second-Generation Integrase Strand Transfer Inhibitor Dolutegravir (S/GSK1349572)Activities, Crystal Structures, and Molecular Dynamics of Dihydro-1 H -isoindole Derivatives, Inhibitors of HIV-1 IntegraseA comparison of the ability of rilpivirine (TMC278) and selected analogues to inhibit clinically relevant HIV-1 reverse transcriptase mutantsThe Integrator complex controls the termination of transcription at diverse classes of gene targets.Enhancers are major targets for murine leukemia virus vector integrationDifferential effects of human immunodeficiency virus type 1 capsid and cellular factors nucleoporin 153 and LEDGF/p75 on the efficiency and specificity of viral DNA integrationHRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor.On the detection of multiple-binding modes of ligands to proteins, from biological, structural, and modeling data.Lens epithelium-derived growth factor fusion proteins redirect HIV-1 DNA integration.Flexible use of nuclear import pathways by HIV-1.Mutations in HIV-1 reverse transcriptase affect the errors made in a single cycle of viral replication.Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition.Mutations of a residue within the polyproline-rich region of Env alter the replication rate and level of cytopathic effects in chimeric avian retroviral vectorsMutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo.Alternate polypurine tracts (PPTs) affect the rous sarcoma virus RNase H cleavage specificity and reveal a preferential cleavage following a GA dinucleotide sequence at the PPT-U3 junction.Nature, position, and frequency of mutations made in a single cycle of HIV-1 replication.Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase.Mutations in the U5 sequences adjacent to the primer binding site do not affect tRNA cleavage by rous sarcoma virus RNase H but do cause aberrant integrations in vivoConstruction and characterization of a replication-competent retroviral shuttle vector plasmidThe M184V mutation reduces the selective excision of zidovudine 5'-monophosphate (AZTMP) by the reverse transcriptase of human immunodeficiency virus type 1Mutation of the catalytic domain of the foamy virus reverse transcriptase leads to loss of processivity and infectivity.Nucleoside analog resistance caused by insertions in the fingers of human immunodeficiency virus type 1 reverse transcriptase involves ATP-mediated excision.The level of reverse transcriptase (RT) in human immunodeficiency virus type 1 particles affects susceptibility to nonnucleoside RT inhibitors but not to lamivudine4-amino-1-hydroxy-2-oxo-1,8-naphthyridine-containing compounds having high potency against raltegravir-resistant integrase mutants of HIV-1Identification of a 3-aminoimidazo[1,2-a]pyridine inhibitor of HIV-1 reverse transcriptase.Foamy retrovirus integrase contains a Pol dimerization domain required for protease activation.Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097.Synthesis, biological activity, and crystal structure of potent nonnucleoside inhibitors of HIV-1 reverse transcriptase that retain activity against mutant forms of the enzyme.HIV-1 reverse transcriptase connection subdomain mutations reduce template RNA degradation and enhance AZT excisionDevelopment of tricyclic hydroxy-1H-pyrrolopyridine-trione containing HIV-1 integrase inhibitors.
P50
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P50
description
virologist
@en
name
Stephen H. Hughes
@en
Stephen H. Hughes
@nl
type
label
Stephen H. Hughes
@en
Stephen H. Hughes
@nl
prefLabel
Stephen H. Hughes
@en
Stephen H. Hughes
@nl