2010
Structural insight into the mechanisms of enveloped virus tethering by tetherin
Yang H, Wang J, Jia X, McNatt MW, Zang T, Pan B, Meng W, Wang HW, Bieniasz PD, Xiong Y. Structural insight into the mechanisms of enveloped virus tethering by tetherin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 18428-18432. PMID: 20940320, PMCID: PMC2972963, DOI: 10.1073/pnas.1011485107.Peer-Reviewed Original ResearchAntigens, CDBase SequenceCell LineCrystallography, X-RayDimerizationDNA PrimersGPI-Linked ProteinsHIV-1HumansImmunity, InnateIn Vitro TechniquesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedMutant ProteinsProtein StabilityProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsStatic ElectricityVirus Release
2009
Impact of Novel Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutations P119S and T165A on 4′-Ethynylthymidine Analog Resistance Profile
Yang G, Paintsil E, Dutschman GE, Grill SP, Wang CJ, Wang J, Tanaka H, Hamasaki T, Baba M, Cheng YC. Impact of Novel Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutations P119S and T165A on 4′-Ethynylthymidine Analog Resistance Profile. Antimicrobial Agents And Chemotherapy 2009, 53: 4640-4646. PMID: 19704131, PMCID: PMC2772322, DOI: 10.1128/aac.00686-09.Peer-Reviewed Original ResearchStructural Basis for Functional Tetramerization of Lentiviral Integrase
Hare S, Di Nunzio F, Labeja A, Wang J, Engelman A, Cherepanov P. Structural Basis for Functional Tetramerization of Lentiviral Integrase. PLOS Pathogens 2009, 5: e1000515. PMID: 19609359, PMCID: PMC2705190, DOI: 10.1371/journal.ppat.1000515.Peer-Reviewed Original ResearchConceptsDimer-dimer interface
2008
Mechanism of Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase by a Stavudine Analogue, 4′-Ethynyl Stavudine Triphosphate
Yang G, Wang J, Cheng Y, Dutschman GE, Tanaka H, Baba M, Cheng YC. Mechanism of Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase by a Stavudine Analogue, 4′-Ethynyl Stavudine Triphosphate. Antimicrobial Agents And Chemotherapy 2008, 52: 2035-2042. PMID: 18391035, PMCID: PMC2415781, DOI: 10.1128/aac.00083-08.Peer-Reviewed Original ResearchConceptsM184V mutantNucleoside reverse transcriptase inhibitorHuman immunodeficiency virus type 1Immunodeficiency virus type 1Human immunodeficiency virus type 1 reverse transcriptaseReverse transcriptase inhibitorType 1 reverse transcriptaseVirus type 1Mechanism of inhibitionHIV-1 RTWild-type RTStavudine triphosphateTranscriptase inhibitorD4TD4TTPType 1WT RTMutant RTsReverse transcriptase
1994
Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion
Jäger J, Smerdon S, Wang J, Boisvert D, Steitz T. Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion. Structure 1994, 2: 869-876. PMID: 7529124, DOI: 10.1016/s0969-2126(94)00087-5.Peer-Reviewed Original ResearchStructural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer.
Wang J, Smerdon S, Jäger J, Kohlstaedt L, Rice P, Friedman J, Steitz T. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7242-7246. PMID: 7518928, PMCID: PMC44375, DOI: 10.1073/pnas.91.15.7242.Peer-Reviewed Original ResearchStructure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1.
Smerdon S, Jäger J, Wang J, Kohlstaedt L, Chirino A, Friedman J, Rice P, Steitz T. Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 3911-3915. PMID: 7513427, PMCID: PMC43692, DOI: 10.1073/pnas.91.9.3911.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntiviral AgentsBinding SitesCrystallography, X-RayDrug Resistance, MicrobialHIV Reverse TranscriptaseHIV-1Models, MolecularMolecular Sequence DataMolecular StructureNevirapineNucleosidesProtein Structure, TertiaryPyridinesReverse Transcriptase InhibitorsRNA-Directed DNA PolymeraseConceptsHuman immunodeficiency virus type 1Immunodeficiency virus type 1Drug resistance mutationsVirus type 1Type 1Reverse transcriptaseHIV-1 reverse transcriptaseNevirapineResistance mutationsNonnucleoside inhibitorsDrugsViable virusSpecific inhibitorInhibitorsClose contactMutationsTranscriptaseSame binding site
1993
Two DNA polymerases: HIV reverse transcriptase and the Klenow fragment of Escherichia coli DNA polymerase I.
Steitz T, Smerdon S, Jäger J, Wang J, Kohlstaedt L, Friedman J, Beese L, Rice P. Two DNA polymerases: HIV reverse transcriptase and the Klenow fragment of Escherichia coli DNA polymerase I. Cold Spring Harbor Symposia On Quantitative Biology 1993, 58: 495-504. PMID: 7525146, DOI: 10.1101/sqb.1993.058.01.056.Peer-Reviewed Original Research
1992
Crystal Structure at 3.5 Å Resolution of HIV-1 Reverse Transcriptase Complexed with an Inhibitor
Kohlstaedt L, Wang J, Friedman J, Rice P, Steitz T. Crystal Structure at 3.5 Å Resolution of HIV-1 Reverse Transcriptase Complexed with an Inhibitor. Science 1992, 256: 1783-1790. PMID: 1377403, DOI: 10.1126/science.1377403.Peer-Reviewed Original Research