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Volumn 10, Issue 4, 2012, Pages 279-290

The structural biology of HIV-1: Mechanistic and therapeutic insights

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CHEMOKINE RECEPTOR CCR5 ANTAGONIST; ENFUVIRTIDE; ETRAVIRINE; GAG PROTEIN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; INTEGRASE; INTEGRASE INHIBITOR; LAMIVUDINE; MARAVIROC; MESSENGER RNA; NONNUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITOR; PF 3450074; POL PROTEIN; RALTEGRAVIR; REV PROTEIN; RILPIVIRINE; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS GLYCOPROTEIN; VIRUS RNA; ZIDOVUDINE;

EID: 84858409977     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro2747     Document Type: Review
Times cited : (267)

References (165)
  • 1
    • 0033521911 scopus 로고    scopus 로고
    • Origin of HIV-1 in the chimpanzee Pan troglodytes troglodytes
    • Gao, F. et al. Origin of HIV-1 in the chimpanzee Pan troglodytes troglodytes. Nature 397, 436-441 (1999).
    • (1999) Nature , vol.397 , pp. 436-441
    • Gao, F.1
  • 5
    • 77956188831 scopus 로고    scopus 로고
    • BST-2/tetherin: A new component of the innate immune response to enveloped viruses
    • Evans, D. T., Serra-Moreno, R., Singh, R. K. & Guatelli, J. C. BST-2/tetherin: a new component of the innate immune response to enveloped viruses. Trends Microbiol. 18, 388-396 (2010).
    • (2010) Trends Microbiol. , vol.18 , pp. 388-396
    • Evans, D.T.1    Serra-Moreno, R.2    Singh, R.K.3    Guatelli, J.C.4
  • 6
    • 56949089824 scopus 로고    scopus 로고
    • Restriction of retroviral replication by APOBEC3G/F and TRIM5α
    • Huthoff, H. & Towers, G. J. Restriction of retroviral replication by APOBEC3G/F and TRIM5α. Trends Microbiol. 16, 612-619 (2008).
    • (2008) Trends Microbiol. , vol.16 , pp. 612-619
    • Huthoff, H.1    Towers, G.J.2
  • 7
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu, P. et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441, 847-852 (2006).
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 8
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • Zanetti, G., Briggs, J. A., Grunewald, K., Sattentau, Q. J. & Fuller, S. D. Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog. 2, e83 (2006).
    • (2006) PLoS Pathog. , vol.2
    • Zanetti, G.1    Briggs, J.A.2    Grunewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 10
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (1998). (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 12
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • DOI 10.1038/nature03327
    • Chen, B. et al. Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433, 834-841 (2005). (Pubitemid 40314887)
    • (2005) Nature , vol.433 , Issue.7028 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273 (1997). (Pubitemid 27199898)
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 14
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J. & Wiley, D. C. Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430 (1997). (Pubitemid 27227210)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4    Wiley, D.C.5
  • 15
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon, V. et al. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 6, e1000880 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Buzon, V.1
  • 16
    • 33748087473 scopus 로고    scopus 로고
    • The SIV surface spike imaged by electron tomography: One leg or three?
    • Subramaniam, S. The SIV surface spike imaged by electron tomography: one leg or three? PLoS Pathog. 2, e91 (2006).
    • (2006) PLoS Pathog. , vol.2
    • Subramaniam, S.1
  • 17
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: Further evidence for tripod-like legs
    • Zhu, P., Winkler, H., Chertova, E., Taylor, K. A. & Roux, K. H. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog. 4, e1000203 (2008).
    • (2008) PLoS Pathog. , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5
  • 18
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera, M. et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl Acad. Sci. USA 107, 1166-1171 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 19
    • 55249083812 scopus 로고    scopus 로고
    • Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120
    • Madani, N. et al. Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120. Structure 16, 1689-1701 (2008).
    • (2008) Structure , vol.16 , pp. 1689-1701
    • Madani, N.1
  • 20
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker, L. M. et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326, 285-289 (2009).
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 21
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu, X. et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329, 856-861 (2010).
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 22
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu, X. et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333, 1593-1602 (2011).
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 23
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker, L. M. et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477, 466-470 (2011).
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1
  • 24
    • 77649318846 scopus 로고    scopus 로고
    • Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals
    • Corti, D. et al. Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 5, e8805 (2010).
    • (2010) PLoS ONE , vol.5
    • Corti, D.1
  • 25
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou, T. et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329, 811-817 (2010).
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 28
    • 77957942154 scopus 로고    scopus 로고
    • Design of a potent D-peptide HIV-1 entry inhibitor with a strong barrier to resistance
    • Welch, B. D. et al. Design of a potent D-peptide HIV-1 entry inhibitor with a strong barrier to resistance. J. Virol. 84, 11235-11244 (2010).
    • (2010) J. Virol. , vol.84 , pp. 11235-11244
    • Welch, B.D.1
  • 29
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: Insights from three-dimensional reconstructions of authentic virions
    • DOI 10.1016/j.str.2005.09.010, PII S0969212605003898
    • Briggs, J. A. et al. The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14, 15-20 (2006). (Pubitemid 43350069)
    • (2006) Structure , vol.14 , Issue.1 , pp. 15-20
    • Briggs, J.A.G.1    Grunewald, K.2    Glass, B.3    Forster, F.4    Krausslich, H.-G.5    Fuller, S.D.6
  • 30
    • 70350771279 scopus 로고    scopus 로고
    • Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function
    • Byeon, I. J. et al. Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139, 780-790 (2009).
    • (2009) Cell , vol.139 , pp. 780-790
    • Byeon, I.J.1
  • 31
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos, O. et al. X-ray structures of the hexameric building block of the HIV capsid. Cell 137, 1282-1292 (2009).
    • (2009) Cell , vol.137 , pp. 1282-1292
    • Pornillos, O.1
  • 32
    • 78751670547 scopus 로고    scopus 로고
    • Atomic-level modelling of the HIV capsid
    • Pornillos, O., Ganser-Pornillos, B. K. & Yeager, M. Atomic-level modelling of the HIV capsid. Nature 469, 424-427 (2011).
    • (2011) Nature , vol.469 , pp. 424-427
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Yeager, M.3
  • 33
    • 0034653538 scopus 로고    scopus 로고
    • 2-terminal capsid domain: Structure determinants for proper core assembly and subsequent steps of early replication
    • DOI 10.1006/viro.1999.0178
    • Fitzon, T. et al. Proline residues in the HIV-1 NH2-terminal capsid domain: structure determinants for proper core assembly and subsequent steps of early replication. Virology 268, 294-307 (2000). (Pubitemid 30159979)
    • (2000) Virology , vol.268 , Issue.2 , pp. 294-307
    • Fitzon, T.1    Leschonsky, B.2    Bieler, K.3    Paulus, C.4    Schroder, J.5    Wolf, H.6    Wagner, R.7
  • 34
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • DOI 10.1128/JVI.76.11.5667-5677.2002
    • Forshey, B. M., von Schwedler, U., Sundquist, W. I. & Aiken, C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76, 5667-5677 (2002). (Pubitemid 34517917)
    • (2002) Journal of Virology , vol.76 , Issue.11 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 35
    • 78650042418 scopus 로고    scopus 로고
    • HIV capsid is a tractable target for small molecule therapeutic intervention
    • Blair, W. S. et al. HIV capsid is a tractable target for small molecule therapeutic intervention. PLoS Pathog. 6, e1001220 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Blair, W.S.1
  • 38
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • DOI 10.1126/science.283.5398.80
    • Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T. & Sundquist, W. I. Assembly and analysis of conical models for the HIV-1 core. Science 283, 80-83 (1999). (Pubitemid 29044851)
    • (1999) Science , vol.283 , Issue.5398 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 39
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys
    • DOI 10.1038/nature02343
    • Stremlau, M. et al. The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys. Nature 427, 848-853 (2004). (Pubitemid 38297747)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 40
    • 33645794537 scopus 로고    scopus 로고
    • Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5α restriction factor
    • Stremlau, M. et al. Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5α restriction factor. Proc. Natl Acad. Sci. USA 103, 5514-5519 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 5514-5519
    • Stremlau, M.1
  • 41
    • 79955377543 scopus 로고    scopus 로고
    • TRIM5 is an innate immune sensor for the retrovirus capsid lattice
    • Pertel, T. et al. TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 472, 361-365 (2011).
    • (2011) Nature , vol.472 , pp. 361-365
    • Pertel, T.1
  • 42
    • 56449102983 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of a chimeric TRIM21-TRIM5α protein
    • Kar, A. K., Diaz-Griffero, F., Li, Y., Li, X. & Sodroski, J. Biochemical and biophysical characterization of a chimeric TRIM21-TRIM5α protein. J. Virol. 82, 11669-11681 (2008).
    • (2008) J. Virol. , vol.82 , pp. 11669-11681
    • Kar, A.K.1    Diaz-Griffero, F.2    Li, Y.3    Li, X.4    Sodroski, J.5
  • 43
    • 84885879561 scopus 로고    scopus 로고
    • Hexagonal assembly of a restricting TRIM5α protein
    • Ganser-Pornillos, B. K. et al. Hexagonal assembly of a restricting TRIM5α protein. Proc. Natl Acad. Sci. USA 108, 534-539 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 534-539
    • Ganser-Pornillos, B.K.1
  • 44
    • 78650064115 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi, J., Zhou, J., Shah, V. B., Aiken, C. & Whitby, K. Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J. Virol. 85, 542-549 (2011).
    • (2011) J. Virol. , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 45
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A. & Steitz, T. A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256, 1783-1790 (1992).
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 47
    • 0028842293 scopus 로고
    • The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1
    • Rodgers, D. W. et al. The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. Proc. Natl Acad. Sci. USA 92, 1222-1226 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1222-1226
    • Rodgers, D.W.1
  • 48
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H., Chopra, R., Verdine, G. L. & Harrison, S. C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282, 1669-1675 (1998). (Pubitemid 28549275)
    • (1998) Science , vol.282 , Issue.5394 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 50
    • 0026755210 scopus 로고
    • Biochemical studies on the reverse transcriptase and RNase H activities from human immunodeficiency virus strains resistant to 3′-azido-3′- deoxythymidine
    • Lacey, S. F. et al. Biochemical studies on the reverse transcriptase and RNase H activities from human immunodeficiency virus strains resistant to 3′-azido-3′-deoxythymidine. J. Biol. Chem. 267, 15789-15794 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 15789-15794
    • Lacey, S.F.1
  • 51
    • 0032506055 scopus 로고    scopus 로고
    • Phenotypic mechanism of HIV-1 resistance to 3'-azido-3'-deoxythymidine (AZT): Increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase
    • DOI 10.1021/bi981200e
    • Arion, D., Kaushik, N., McCormick, S., Borkow, G. & Parniak, M. A. Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′- deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase. Biochemistry 37, 15908-15917 (1998). (Pubitemid 28524762)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15908-15917
    • Arion, D.1    Kaushik, N.2    McCormick, S.3    Borkow, G.4    Parniak, M.A.5
  • 52
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: An increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • DOI 10.1016/S1097-2765(00)80185-9
    • Meyer, P. R., Matsuura, S. E., Mian, A. M., So, A. G. & Scott, W. A. A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol. Cell 4, 35-43 (1999). (Pubitemid 29386129)
    • (1999) Molecular Cell , vol.4 , Issue.1 , pp. 35-43
    • Meyer, P.R.1    Matsuura, S.E.2    Mohsin Mian, A.3    So, A.G.4    Scott, W.A.5
  • 53
    • 77957797787 scopus 로고    scopus 로고
    • Structural basis of HIV-1 resistance to AZT by excision
    • Tu, X. et al. Structural basis of HIV-1 resistance to AZT by excision. Nature Struct. Mol. Biol. 17, 1202-1209 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1202-1209
    • Tu, X.1
  • 54
    • 0028172345 scopus 로고
    • Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance
    • Tantillo, C. et al. Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance. J. Mol. Biol. 243, 369-387 (1994).
    • (1994) J. Mol. Biol. , vol.243 , pp. 369-387
    • Tantillo, C.1
  • 55
    • 0028947588 scopus 로고
    • High resolution structures of HIV-1 RT from four RT-inhibitor complexes
    • Ren, J. et al. High resolution structures of HIV-1 RT from four RT-inhibitor complexes. Nature Struct. Biol. 2, 293-302 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 293-302
    • Ren, J.1
  • 56
    • 0030596068 scopus 로고    scopus 로고
    • Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant
    • Das, K. et al. Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant. J. Mol. Biol. 264, 1085-1100 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 1085-1100
    • Das, K.1
  • 57
    • 0028924567 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors
    • Esnouf, R. et al. Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. Nature Struct. Biol. 2, 303-308 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 303-308
    • Esnouf, R.1
  • 58
    • 0035965124 scopus 로고    scopus 로고
    • Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors
    • DOI 10.1006/jmbi.2001.4988
    • Ren, J. et al. Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors. J. Mol. Biol. 312, 795-805 (2001). (Pubitemid 33116741)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.4 , pp. 795-805
    • Ren, J.1    Nichols, C.2    Bird, L.3    Chamberlain, P.4    Weaver, K.5    Short, S.6    Stuart, D.I.7    Stammers, D.K.8
  • 60
    • 33751529192 scopus 로고    scopus 로고
    • Crystal Structures of Clinically Relevant Lys103Asn/Tyr181Cys Double Mutant HIV-1 Reverse Transcriptase in Complexes with ATP and Non-nucleoside Inhibitor HBY 097
    • DOI 10.1016/j.jmb.2006.08.097, PII S0022283606011090
    • Das, K. et al. Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097. J. Mol. Biol. 365, 77-89 (2007). (Pubitemid 44830031)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 77-89
    • Das, K.1    Sarafianos, S.G.2    Clark Jr., A.D.3    Boyer, P.L.4    Hughes, S.H.5    Arnold, E.6
  • 62
    • 33751206549 scopus 로고    scopus 로고
    • Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • DOI 10.1128/JVI.01038-06
    • Guo, F., Cen, S., Niu, M., Saadatmand, J. & Kleiman, L. Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J. Virol. 80, 11710-11722 (2006). (Pubitemid 44788884)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 65
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • DOI 10.1038/nature01709
    • Mangeat, B. et al. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424, 99-103 (2003). (Pubitemid 36834849)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 66
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • DOI 10.1038/nature01707
    • Zhang, H. et al. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424, 94-98 (2003). (Pubitemid 36834848)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 67
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • DOI 10.1038/nm945
    • Sheehy, A. M., Gaddis, N. C. & Malim, M. H. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nature Med. 9, 1404-1407 (2003). (Pubitemid 37466190)
    • (2003) Nature Medicine , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 68
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex
    • DOI 10.1126/science.1089591
    • Yu, X. et al. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302, 1056-1060 (2003). (Pubitemid 37386201)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.-F.7
  • 69
    • 53649086178 scopus 로고    scopus 로고
    • Small-molecule inhibition of HIV-1 Vif
    • Nathans, R. et al. Small-molecule inhibition of HIV-1 Vif. Nature Biotech. 26, 1187-1192 (2008).
    • (2008) Nature Biotech. , vol.26 , pp. 1187-1192
    • Nathans, R.1
  • 70
    • 77952781524 scopus 로고    scopus 로고
    • Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G
    • Cen, S. et al. Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G. J. Biol. Chem. 285, 16546-16552 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 16546-16552
    • Cen, S.1
  • 72
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman, E. N. et al. Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr. Biol. 15, 166-170 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 166-170
    • Newman, E.N.1
  • 73
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
    • DOI 10.1074/jbc.M500382200
    • Hache, G., Liddament, M. T. & Harris, R. S. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J. Biol. Chem. 280, 10920-10924 (2005). (Pubitemid 40418393)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 10920-10924
    • Hache, G.1    Liddament, M.T.2    Harris, R.S.3
  • 74
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • Chen, K. M. et al. Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452, 116-119 (2008).
    • (2008) Nature , vol.452 , pp. 116-119
    • Chen, K.M.1
  • 75
    • 60549109045 scopus 로고    scopus 로고
    • Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G
    • Furukawa, A. et al. Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. EMBO J. 28, 440-451 (2009).
    • (2009) EMBO J. , vol.28 , pp. 440-451
    • Furukawa, A.1
  • 76
    • 67349258491 scopus 로고    scopus 로고
    • An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model
    • Harjes, E. et al. An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. J. Mol. Biol. 389, 819-832 (2009).
    • (2009) J. Mol. Biol. , vol.389 , pp. 819-832
    • Harjes, E.1
  • 77
    • 55549098517 scopus 로고    scopus 로고
    • Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
    • Holden, L. G. et al. Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456, 121-124 (2008).
    • (2008) Nature , vol.456 , pp. 121-124
    • Holden, L.G.1
  • 78
    • 73449099592 scopus 로고    scopus 로고
    • Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces
    • Shandilya, S. M. et al. Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure 18, 28-38 (2010).
    • (2010) Structure , vol.18 , pp. 28-38
    • Shandilya, S.M.1
  • 79
    • 1242319532 scopus 로고    scopus 로고
    • Human endogenous retrovirus K solo-LTR formation and insertional polymorphisms: Implications for human and viral evolution
    • DOI 10.1073/pnas.0307885100
    • Hughes, J. F. & Coffin, J. M. Human endogenous retrovirus K solo-LTR formation and insertional polymorphisms: Implications for human and viral evolution. Proc. Natl Acad. Sci. USA 101, 1668-1672 (2004). (Pubitemid 38234212)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.6 , pp. 1668-1672
    • Hughes, J.F.1    Coffin, J.M.2
  • 80
    • 34347398120 scopus 로고    scopus 로고
    • HIV-1 proviral DNA excision using an evolved recombinase
    • DOI 10.1126/science.1141453
    • Sarkar, I., Hauber, I., Hauber, J. & Buchholz, F. HIV-1 proviral DNA excision using an evolved recombinase. Science 316, 1912-1915 (2007). (Pubitemid 47025793)
    • (2007) Science , vol.316 , Issue.5833 , pp. 1912-1915
    • Sarkar, I.1    Hauber, I.2    Hauber, J.3    Buchholz, F.4
  • 81
    • 65549105028 scopus 로고    scopus 로고
    • Piecing together the structure of retroviral integrase, an important target in AIDS therapy
    • Jaskolski, M., Alexandratos, J. N., Bujacz, G. & Wlodawer, A. Piecing together the structure of retroviral integrase, an important target in AIDS therapy. FEBS J. 276, 2926-2946 (2009).
    • (2009) FEBS J. , vol.276 , pp. 2926-2946
    • Jaskolski, M.1    Alexandratos, J.N.2    Bujacz, G.3    Wlodawer, A.4
  • 82
    • 12944270496 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase
    • Espeseth, A. S. et al. HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. Proc. Natl Acad. Sci. USA 97, 11244-11249 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11244-11249
    • Espeseth, A.S.1
  • 83
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S., Gupta, S. S., Valkov, E., Engelman, A. & Cherepanov, P. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464, 232-236 (2010).
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 84
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration from X-ray structures of its key intermediates
    • Maertens, G. N., Hare, S. & Cherepanov, P. The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468, 326-329 (2010).
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 85
    • 79952070221 scopus 로고    scopus 로고
    • Structural biology of retroviral DNA integration
    • Li, X., Krishnan, L., Cherepanov, P. & Engelman, A. Structural biology of retroviral DNA integration. Virology 411, 194-205 (2011).
    • (2011) Virology , vol.411 , pp. 194-205
    • Li, X.1    Krishnan, L.2    Cherepanov, P.3    Engelman, A.4
  • 86
    • 79953124784 scopus 로고    scopus 로고
    • Structural insights into the retroviral DNA integration apparatus
    • Cherepanov, P., Maertens, G. N. & Hare, S. Structural insights into the retroviral DNA integration apparatus. Curr. Opin. Struct. Biol. 21, 249-256 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 249-256
    • Cherepanov, P.1    Maertens, G.N.2    Hare, S.3
  • 87
    • 58549092798 scopus 로고    scopus 로고
    • Functional and structural characterization of the integrase from the prototype foamy virus
    • Valkov, E. et al. Functional and structural characterization of the integrase from the prototype foamy virus. Nucleic Acids Res. 37, 243-255 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 243-255
    • Valkov, E.1
  • 88
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance
    • Hare, S. et al. Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc. Natl Acad. Sci. USA 107, 20057-20062 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20057-20062
    • Hare, S.1
  • 89
    • 79952580956 scopus 로고    scopus 로고
    • Differential sensitivities of retroviruses to integrase strand transfer inhibitors
    • Koh, Y., Matreyek, K. A. & Engelman, A. Differential sensitivities of retroviruses to integrase strand transfer inhibitors. J. Virol. 85, 3677-3682 (2011).
    • (2011) J. Virol. , vol.85 , pp. 3677-3682
    • Koh, Y.1    Matreyek, K.A.2    Engelman, A.3
  • 91
    • 42949114952 scopus 로고    scopus 로고
    • The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication
    • Engelman, A. & Cherepanov, P. The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication. PLoS Pathog. 4, e1000046 (2008).
    • (2008) PLoS Pathog. , vol.4
    • Engelman, A.1    Cherepanov, P.2
  • 94
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • Christ, F. et al. Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nature Chem. Biol. 6, 442-448 (2010).
    • (2010) Nature Chem. Biol. , vol.6 , pp. 442-448
    • Christ, F.1
  • 95
    • 80052847538 scopus 로고    scopus 로고
    • Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572)
    • Hare, S. et al. Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572). Mol. Pharmacol. 80, 565-572 (2011).
    • (2011) Mol. Pharmacol. , vol.80 , pp. 565-572
    • Hare, S.1
  • 97
    • 77953431827 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 Tat complexed with human P-TEFb
    • Tahirov, T. H. et al. Crystal structure of HIV-1 Tat complexed with human P-TEFb. Nature 465, 747-751 (2010).
    • (2010) Nature , vol.465 , pp. 747-751
    • Tahirov, T.H.1
  • 98
    • 78549248443 scopus 로고    scopus 로고
    • Structural basis for cooperative RNA binding and export complex assembly by HIV Rev
    • Daugherty, M. D., Liu, B. & Frankel, A. D. Structural basis for cooperative RNA binding and export complex assembly by HIV Rev. Nature Struct. Mol. Biol. 17, 1337-1442 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1337-1442
    • Daugherty, M.D.1    Liu, B.2    Frankel, A.D.3
  • 99
    • 77950539375 scopus 로고    scopus 로고
    • Implications of the HIV-1 Rev dimer structure at 3.2 Å resolution for multimeric binding to the Rev response element
    • DiMattia, M. A. et al. Implications of the HIV-1 Rev dimer structure at 3.2 Å resolution for multimeric binding to the Rev response element. Proc. Natl Acad. Sci. USA 107, 5810-5814 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5810-5814
    • Dimattia, M.A.1
  • 100
    • 0032401752 scopus 로고    scopus 로고
    • Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat
    • Bieniasz, P. D., Grdina, T. A., Bogerd, H. P. & Cullen, B. R. Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat. EMBO J. 17, 7056-7065 (1998). (Pubitemid 28550299)
    • (1998) EMBO Journal , vol.17 , Issue.23 , pp. 7056-7065
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 101
    • 0031846856 scopus 로고    scopus 로고
    • The ability of positive transcription elongation factor b to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat
    • Fujinaga, K. et al. The ability of positive transcription elongation factor b to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat. J. Virol. 72, 7154-7159 (1998). (Pubitemid 28377844)
    • (1998) Journal of Virology , vol.72 , Issue.9 , pp. 7154-7159
    • Fujinaga, K.1    Cujec, T.P.2    Peng, J.3    Garriga, J.4    Price, D.H.5    Grana, X.6    Peterlin, B.M.7
  • 102
    • 0028902911 scopus 로고
    • Structural studies of HIV-1 Tat protein
    • Bayer, P. et al. Structural studies of HIV-1 Tat protein. J. Mol. Biol. 247, 529-535 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 529-535
    • Bayer, P.1
  • 103
    • 57149121459 scopus 로고    scopus 로고
    • Structural insights into the cyclin T1-Tat-TAR RNA transcription activation complex from EIAV
    • Anand, K., Schulte, A., Vogel-Bachmayr, K., Scheffzek, K. & Geyer, M. Structural insights into the cyclin T1-Tat-TAR RNA transcription activation complex from EIAV. Nature Struct. Mol. Biol. 15, 1287-1292 (2008).
    • (2008) Nature Struct. Mol. Biol. , vol.15 , pp. 1287-1292
    • Anand, K.1    Schulte, A.2    Vogel-Bachmayr, K.3    Scheffzek, K.4    Geyer, M.5
  • 104
    • 0033920260 scopus 로고    scopus 로고
    • Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription
    • DOI 10.1128/MCB.20.14.5077-5086.2000
    • Zhou, M. et al. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 20, 5077-5086 (2000). (Pubitemid 30431561)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.14 , pp. 5077-5086
    • Zhou, M.1    Halanski, M.A.2    Radonovich, M.F.3    Kashanchi, F.4    Peng, J.5    Price, D.H.6    Brady, J.N.7
  • 105
    • 0035265946 scopus 로고    scopus 로고
    • Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
    • DOI 10.1016/S1097-2765(01)00207-6
    • Jain, C. & Belasco, J. G. Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. Mol. Cell 7, 603-614 (2001). (Pubitemid 32706352)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 106
    • 77955446835 scopus 로고    scopus 로고
    • HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes
    • Daugherty, M. D., Booth, D. S., Jayaraman, B., Cheng, Y. & Frankel, A. D. HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes. Proc. Natl Acad. Sci. USA 107, 12481-12486 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 12481-12486
    • Daugherty, M.D.1    Booth, D.S.2    Jayaraman, B.3    Cheng, Y.4    Frankel, A.D.5
  • 107
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor pr55(gag) virus-like particles from recombinant baculovirus-infected insect cells
    • DOI 10.1016/0092-8674(89)90873-8
    • Gheysen, D. et al. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59, 103-112 (1989). (Pubitemid 19248562)
    • (1989) Cell , vol.59 , Issue.1 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 109
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant, M. & Ratner, L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl Acad. Sci. USA 87, 523-527 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 110
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., Parent, L. J., Wills, J. W. & Resh, M. D. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68, 2556-2569 (1994).
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 112
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • DOI 10.1038/378743a0
    • Rao, Z. et al. Crystal structure of SIV matrix antigen and implications for virus assembly. Nature 378, 743-747 (1995). (Pubitemid 26001950)
    • (1995) Nature , vol.378 , Issue.6558 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jonest, I.M.5    Stuart, D.I.6
  • 113
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou, W. & Resh, M. D. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70, 8540-8548 (1996). (Pubitemid 26378433)
    • (1996) Journal of Virology , vol.70 , Issue.12 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2
  • 116
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • DOI 10.1126/science.1143422
    • Carlton, J. G. & Martin-Serrano, J. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316, 1908-1912 (2007). (Pubitemid 47025792)
    • (2007) Science , vol.316 , Issue.5833 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 118
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery: It's all in the neck
    • Hurley, J. H. & Hanson, P. I. Membrane budding and scission by the ESCRT machinery: it's all in the neck. Nature Rev. Mol. Cell Biol. 11, 556-566 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 121
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • DOI 10.1016/S0092-8674(03)00653-6
    • Strack, B., Calistri, A., Craig, S., Popova, E. & Göttlinger, H. G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114, 689-699 (2003). (Pubitemid 37186765)
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 123
    • 33847355934 scopus 로고    scopus 로고
    • Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding
    • DOI 10.1016/j.cell.2007.01.035, PII S0092867407001808
    • Fisher, R. D. et al. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128, 841-852 (2007). (Pubitemid 46341413)
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.-Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 126
    • 37849024338 scopus 로고    scopus 로고
    • nL late domains of HIV-1 and EIAV
    • Zhai, Q. et al. Structural and functional studies of ALIX interactions with YPXnL late domains of HIV-1 and EIAV. Nature Struct. Mol. Biol. 15, 43-49 (2008).
    • (2008) Nature Struct. Mol. Biol. , vol.15 , pp. 43-49
    • Zhai, Q.1
  • 127
    • 27744432641 scopus 로고    scopus 로고
    • 2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B
    • DOI 10.1042/BJ20050398
    • Katoh, K. et al. The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B. Biochem. J. 391, 677-685 (2005). (Pubitemid 41634794)
    • (2005) Biochemical Journal , vol.391 , Issue.3 , pp. 677-685
    • Katoh, K.1    Suzuki, H.2    Terasawa, Y.3    Mizuno, T.4    Yasuda, J.5    Shibata, H.6    Maki, M.7
  • 129
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos, O., Alam, S. L., Davis, D. R. & Sundquist, W. I. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nature Struct. Biol. 9, 812-817 (2002). (Pubitemid 35257779)
    • (2002) Nature Structural Biology , vol.9 , Issue.11 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 130
    • 78149426750 scopus 로고    scopus 로고
    • Crystallographic and functional analysis of the ESCRT-I/HIV-1 Gag PTAP interaction
    • Im, Y. J. et al. Crystallographic and functional analysis of the ESCRT-I/HIV-1 Gag PTAP interaction. Structure 18, 1536-1547 (2010).
    • (2010) Structure , vol.18 , pp. 1536-1547
    • Im, Y.J.1
  • 131
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • DOI 10.1038/nature06553, PII NATURE06553
    • Neil, S. J., Zang, T. & Bieniasz, P. D. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451, 425-430 (2008). (Pubitemid 351158893)
    • (2008) Nature , vol.451 , Issue.7177 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Bieniasz, P.D.3
  • 133
    • 0141494290 scopus 로고    scopus 로고
    • Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology
    • DOI 10.1034/j.1600-0854.2003.00129.x
    • Kupzig, S. et al. Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 4, 694-709 (2003). (Pubitemid 37168591)
    • (2003) Traffic , vol.4 , Issue.10 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 134
    • 81155154291 scopus 로고    scopus 로고
    • C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif
    • Andrew, A. J., Kao, S. & Strebel, K. C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif. J. Biol. Chem. 286, 39967-39981 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 39967-39981
    • Andrew, A.J.1    Kao, S.2    Strebel, K.3
  • 135
    • 77952856849 scopus 로고    scopus 로고
    • Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain
    • Hinz, A. et al. Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain. Cell Host Microbe 7, 314-323 (2010).
    • (2010) Cell Host Microbe , vol.7 , pp. 314-323
    • Hinz, A.1
  • 136
    • 78649845815 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of enveloped virus tethering by tetherin
    • Yang, H. et al. Structural insight into the mechanisms of enveloped virus tethering by tetherin. Proc. Natl Acad. Sci. USA 107, 18428-18432 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18428-18432
    • Yang, H.1
  • 137
    • 78149243391 scopus 로고    scopus 로고
    • Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations
    • Schubert, H. L. et al. Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations. Proc. Natl Acad. Sci. USA 107, 17951-17956 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17951-17956
    • Schubert, H.L.1
  • 138
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat, B. et al. HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog. 5, e1000574 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1
  • 139
    • 77954055324 scopus 로고    scopus 로고
    • Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment
    • Dube, M. et al. Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment. PLoS Pathog. 6, e1000856 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Dube, M.1
  • 140
    • 84855272482 scopus 로고    scopus 로고
    • HIV-1 Vpu antagonizes the innate restriction factor BST-2 via lipid-embedded helix-helix interactions
    • Skasko, M. et al. HIV-1 Vpu antagonizes the innate restriction factor BST-2 via lipid-embedded helix-helix interactions. J. Biol. Chem. 287, 58-67 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 58-67
    • Skasko, M.1
  • 141
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit, S. C. et al. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J. Virol. 68, 8017-8027 (1994). (Pubitemid 24362690)
    • (1994) Journal of Virology , vol.68 , Issue.12 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6    Swanstrom, R.7
  • 142
    • 67650482702 scopus 로고    scopus 로고
    • Structure and assembly of immature HIV
    • Briggs, J. A. et al. Structure and assembly of immature HIV. Proc. Natl Acad. Sci. USA 106, 11090-11095 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11090-11095
    • Briggs, J.A.1
  • 143
    • 79251521481 scopus 로고    scopus 로고
    • Structural analysis of HIV-1 maturation using cryo-electron tomography
    • de Marco, A. et al. Structural analysis of HIV-1 maturation using cryo-electron tomography. PLoS Pathog. 6, e1001215 (2010).
    • (2010) PLoS Pathog. , vol.6
    • De Marco, A.1
  • 144
    • 79251517063 scopus 로고    scopus 로고
    • Cryo electron tomography of native HIV-1 budding sites
    • Carlson, L. A. et al. Cryo electron tomography of native HIV-1 budding sites. PLoS Pathog. 6, e1001173 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Carlson, L.A.1
  • 148
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • Keller, P. W., Adamson, C. S., Heymann, J. B., Freed, E. O. & Steven, A. C. HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J. Virol. 85, 1420-1428 (2011).
    • (2011) J. Virol. , vol.85 , pp. 1420-1428
    • Keller, P.W.1    Adamson, C.S.2    Heymann, J.B.3    Freed, E.O.4    Steven, A.C.5
  • 154
    • 0029644513 scopus 로고
    • Safety and activity of saquinavir in HIV infection
    • Kitchen, V. S. et al. Safety and activity of saquinavir in HIV infection. Lancet 345, 952-955 (1995).
    • (1995) Lancet , vol.345 , pp. 952-955
    • Kitchen, V.S.1
  • 155
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • Wlodawer, A. & Erickson, J. W. Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62, 543-585 (1993). (Pubitemid 23237881)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 156
    • 73549092917 scopus 로고    scopus 로고
    • Fifteen years of HIV protease inhibitors: Raising the barrier to resistance
    • Wensing, A. M., van Maarseveen, N. M. & Nijhuis, M. Fifteen years of HIV protease inhibitors: raising the barrier to resistance. Antiviral Res. 85, 59-74 (2010).
    • (2010) Antiviral Res. , vol.85 , pp. 59-74
    • Wensing, A.M.1    Van Maarseveen, N.M.2    Nijhuis, M.3
  • 157
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: Analysis of crystal structures of six substrate complexes
    • DOI 10.1016/S0969-2126(02)00720-7, PII S0969212602007207
    • Prabu-Jeyabalan, M., Nalivaika, E. & Schiffer, C. A. Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 10, 369-381 (2002). (Pubitemid 34230624)
    • (2002) Structure , vol.10 , Issue.3 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 158
    • 5444247213 scopus 로고    scopus 로고
    • Combating susceptibility to drug resistance: Lessons from HIV-1 protease
    • DOI 10.1016/j.chembiol.2004.08.010, PII S1074552104002431
    • King, N. M., Prabu-Jeyabalan, M., Nalivaika, E. A. & Schiffer, C. A. Combating susceptibility to drug resistance: lessons from HIV-1 protease. Chem. Biol. 11, 1333-1338 (2004). (Pubitemid 39351371)
    • (2004) Chemistry and Biology , vol.11 , Issue.10 , pp. 1333-1338
    • King, N.M.1    Prabu-Jeyabalan, M.2    Nalivaika, E.A.3    Schiffer, C.A.4
  • 159
    • 77951484077 scopus 로고    scopus 로고
    • Evaluating the substrate-envelope hypo thesis: Structural analysis of novel HIV-1 protease inhibitors designed to be robust against drug resistance
    • Nalam, M. N. L. et al. Evaluating the substrate-envelope hypothesis: structural analysis of novel HIV-1 protease inhibitors designed to be robust against drug resistance. J. Virol. 84, 5368-5378 (2010).
    • (2010) J. Virol. , vol.84 , pp. 5368-5378
    • Nalam, M.N.L.1
  • 160
    • 79959843617 scopus 로고    scopus 로고
    • SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx
    • Laguette, N. et al. SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx. Nature 474, 654-657 (2011).
    • (2011) Nature , vol.474 , pp. 654-657
    • Laguette, N.1
  • 161
    • 79959858243 scopus 로고    scopus 로고
    • Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein
    • Hrecka, K. et al. Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein. Nature 474, 658-661 (2011).
    • (2011) Nature , vol.474 , pp. 658-661
    • Hrecka, K.1
  • 162
    • 0038606190 scopus 로고    scopus 로고
    • Structure-based design of AIDS drugs and the development of resistance
    • Wlodawer, A. Structure-based design of AIDS drugs and the development of resistance. Vox Sang. 83, 23-26 (2002).
    • (2002) Vox Sang. , vol.83 , pp. 23-26
    • Wlodawer, A.1
  • 163
    • 77955630528 scopus 로고    scopus 로고
    • AIDS/HIV. A boost for HIV vaccine design
    • Burton, D. R. & Weiss, R. A. AIDS/HIV. A boost for HIV vaccine design. Science 329, 770-773 (2010).
    • (2010) Science , vol.329 , pp. 770-773
    • Burton, D.R.1    Weiss, R.A.2
  • 164
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff, N. & Harrison, S. C. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy. Curr. Opin. Struct. Biol. 21, 265-273 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.2
  • 165
    • 36749088862 scopus 로고    scopus 로고
    • HIV drug development: The next 25 years
    • DOI 10.1038/nrd2336, PII NRD2336
    • Flexner, C. HIV drug development: the next 25 years. Nature Rev. Drug Discov. 6, 959-966 (2007). (Pubitemid 350201786)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.12 , pp. 959-966
    • Flexner, C.1


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