메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)

Author keywords

[No Author keywords available]

Indexed keywords

GUANIDINE; UREA; VIRUS ENVELOPE PROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; REVERSE TRANSCRIPTASE, HUMAN IMMUNODEFICIENCY VIRUS 1; RNA DIRECTED DNA POLYMERASE;

EID: 79959595814     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021339     Document Type: Article
Times cited : (30)

References (112)
  • 1
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L, Morris L, Burton DR, Mascola JR, (2009) Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine? Nat Med 15: 866-870.
    • (2009) Nat Med , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 2
    • 53349160053 scopus 로고    scopus 로고
    • Challenges in the development of an HIV-1 vaccine
    • Barouch DH, (2008) Challenges in the development of an HIV-1 vaccine. Nature 455: 613-619.
    • (2008) Nature , vol.455 , pp. 613-619
    • Barouch, D.H.1
  • 4
    • 38949204965 scopus 로고    scopus 로고
    • HIV-1 neutralization: mechanisms and relevance to vaccine design
    • Zwick MB, Burton DR, (2007) HIV-1 neutralization: mechanisms and relevance to vaccine design. Curr HIV Res 5: 608-624.
    • (2007) Curr HIV Res , vol.5 , pp. 608-624
    • Zwick, M.B.1    Burton, D.R.2
  • 5
    • 0030897825 scopus 로고    scopus 로고
    • Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex
    • Fouts TR, Binley JM, Trkola A, Robinson JE, Moore JP, (1997) Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex. J Virol 71: 2779-2785.
    • (1997) J Virol , vol.71 , pp. 2779-2785
    • Fouts, T.R.1    Binley, J.M.2    Trkola, A.3    Robinson, J.E.4    Moore, J.P.5
  • 6
    • 0035155850 scopus 로고    scopus 로고
    • Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers
    • Yang X, Wyatt R, Sodroski J, (2001) Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers. J Virol 75: 1165-1171.
    • (2001) J Virol , vol.75 , pp. 1165-1171
    • Yang, X.1    Wyatt, R.2    Sodroski, J.3
  • 7
    • 0028999803 scopus 로고
    • Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Sattentau QJ, Moore JP, (1995) Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J Exp Med 182: 185-196.
    • (1995) J Exp Med , vol.182 , pp. 185-196
    • Sattentau, Q.J.1    Moore, J.P.2
  • 8
    • 0037213278 scopus 로고    scopus 로고
    • Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies
    • Poignard P, Moulard M, Golez E, Vivona V, Franti M, et al. (2003) Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies. J Virol 77: 353-365.
    • (2003) J Virol , vol.77 , pp. 353-365
    • Poignard, P.1    Moulard, M.2    Golez, E.3    Vivona, V.4    Franti, M.5
  • 9
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore PL, Crooks ET, Porter L, Zhu P, Cayanan CS, et al. (2006) Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 80: 2515-2528.
    • (2006) J Virol , vol.80 , pp. 2515-2528
    • Moore, P.L.1    Crooks, E.T.2    Porter, L.3    Zhu, P.4    Cayanan, C.S.5
  • 10
    • 77949378988 scopus 로고    scopus 로고
    • In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type-1
    • Leaman DP, Kinkead H, Zwick MB, (2010) In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type-1. J Virol 84: 3382-3395.
    • (2010) J Virol , vol.84 , pp. 3382-3395
    • Leaman, D.P.1    Kinkead, H.2    Zwick, M.B.3
  • 11
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune JM, Rabin LB, Feinberg MB, Lieberman M, Kosek JC, et al. (1988) Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 53: 55-67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5
  • 12
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, et al. (1990) Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 265: 10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5
  • 13
    • 72849117137 scopus 로고    scopus 로고
    • Roles of the interactions between Env and Gag proteins in the HIV-1 replication cycle
    • Murakami T, (2008) Roles of the interactions between Env and Gag proteins in the HIV-1 replication cycle. Microbiol Immunol 52: 287-295.
    • (2008) Microbiol Immunol , vol.52 , pp. 287-295
    • Murakami, T.1
  • 14
    • 0021720872 scopus 로고
    • T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
    • Klatzmann D, Champagne E, Chamaret S, Gruest J, Guetard D, et al. (1984) T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature 312: 767-768.
    • (1984) Nature , vol.312 , pp. 767-768
    • Klatzmann, D.1    Champagne, E.2    Chamaret, S.3    Gruest, J.4    Guetard, D.5
  • 15
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish AG, Beverley PC, Clapham PR, Crawford DH, Greaves MF, et al. (1984) The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312: 763-767.
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3    Crawford, D.H.4    Greaves, M.F.5
  • 16
    • 32544446940 scopus 로고    scopus 로고
    • HIV and the chemokine system: 10 years later
    • Lusso P, (2006) HIV and the chemokine system: 10 years later. EMBO J 25: 447-456.
    • (2006) EMBO J , vol.25 , pp. 447-456
    • Lusso, P.1
  • 18
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore JP, McKeating JA, Weiss RA, Sattentau QJ, (1990) Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250: 1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 19
    • 0027399209 scopus 로고
    • Two mechanisms of soluble CD4 (sCD4)-mediated inhibition of human immunodeficiency virus type 1 (HIV-1) infectivity and their relation to primary HIV-1 isolates with reduced sensitivity to sCD4
    • Orloff SL, Kennedy MS, Belperron AA, Maddon PJ, McDougal JS, (1993) Two mechanisms of soluble CD4 (sCD4)-mediated inhibition of human immunodeficiency virus type 1 (HIV-1) infectivity and their relation to primary HIV-1 isolates with reduced sensitivity to sCD4. J Virol 67: 1461-1471.
    • (1993) J Virol , vol.67 , pp. 1461-1471
    • Orloff, S.L.1    Kennedy, M.S.2    Belperron, A.A.3    Maddon, P.J.4    McDougal, J.S.5
  • 20
    • 0027173841 scopus 로고
    • Physicochemical dissociation of CD4-mediated syncytium formation and shedding of human immunodeficiency virus type 1 gp120
    • Fu YK, Hart TK, Jonak ZL, Bugelski PJ, (1993) Physicochemical dissociation of CD4-mediated syncytium formation and shedding of human immunodeficiency virus type 1 gp120. J Virol 67: 3818-3825.
    • (1993) J Virol , vol.67 , pp. 3818-3825
    • Fu, Y.K.1    Hart, T.K.2    Jonak, Z.L.3    Bugelski, P.J.4
  • 21
    • 0026601827 scopus 로고
    • Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates
    • Moore JP, McKeating JA, Huang YX, Ashkenazi A, Ho DD, (1992) Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates. J Virol 66: 235-243.
    • (1992) J Virol , vol.66 , pp. 235-243
    • Moore, J.P.1    McKeating, J.A.2    Huang, Y.X.3    Ashkenazi, A.4    Ho, D.D.5
  • 22
    • 66349110542 scopus 로고    scopus 로고
    • Soluble CD4 and CD4-mimetic compounds inhibit HIV-1 infection by induction of a short-lived activated state
    • Haim H, Si Z, Madani N, Wang L, Courter JR, et al. (2009) Soluble CD4 and CD4-mimetic compounds inhibit HIV-1 infection by induction of a short-lived activated state. PLoS Pathog 5: e1000360.
    • (2009) PLoS Pathog , vol.5
    • Haim, H.1    Si, Z.2    Madani, N.3    Wang, L.4    Courter, J.R.5
  • 23
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus
    • Chertova E, Bess JW Jr, Crise BJ, Sowder IR, Schaden TM, et al. (2002) Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus. J Virol 76: 5315-5325.
    • (2002) J Virol , vol.76 , pp. 5315-5325
    • Chertova, E.1    Bess Jr., J.W.2    Crise, B.J.3    Sowder, I.R.4    Schaden, T.M.5
  • 24
    • 0037223708 scopus 로고    scopus 로고
    • Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site
    • Herrera C, Spenlehauer C, Fung MS, Burton DR, Beddows S, et al. (2003) Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site. J Virol 77: 1084-1091.
    • (2003) J Virol , vol.77 , pp. 1084-1091
    • Herrera, C.1    Spenlehauer, C.2    Fung, M.S.3    Burton, D.R.4    Beddows, S.5
  • 25
    • 13544252604 scopus 로고    scopus 로고
    • Neutralizing as well as non-neutralizing polyclonal immunoglobulin (Ig)G from infected patients capture HIV-1 via antibodies directed against the principal immunodominant domain of gp41
    • Burrer R, Haessig-Einius S, Aubertin AM, Moog C, (2005) Neutralizing as well as non-neutralizing polyclonal immunoglobulin (Ig)G from infected patients capture HIV-1 via antibodies directed against the principal immunodominant domain of gp41. Virology 333: 102-113.
    • (2005) Virology , vol.333 , pp. 102-113
    • Burrer, R.1    Haessig-Einius, S.2    Aubertin, A.M.3    Moog, C.4
  • 26
    • 12344251568 scopus 로고    scopus 로고
    • Inter-subunit disulfide bonds in soluble HIV-1 envelope glycoprotein trimers
    • Yuan W, Craig S, Yang X, Sodroski J, (2005) Inter-subunit disulfide bonds in soluble HIV-1 envelope glycoprotein trimers. Virology 332: 369-383.
    • (2005) Virology , vol.332 , pp. 369-383
    • Yuan, W.1    Craig, S.2    Yang, X.3    Sodroski, J.4
  • 27
    • 12344264596 scopus 로고    scopus 로고
    • Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage
    • Pancera M, Wyatt R, (2005) Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage. Virology 332: 145-156.
    • (2005) Virology , vol.332 , pp. 145-156
    • Pancera, M.1    Wyatt, R.2
  • 28
    • 38949090023 scopus 로고    scopus 로고
    • N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus
    • Dey AK, David KB, Ray N, Ketas TJ, Klasse PJ, et al. (2008) N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus. Virology 372: 187-200.
    • (2008) Virology , vol.372 , pp. 187-200
    • Dey, A.K.1    David, K.B.2    Ray, N.3    Ketas, T.J.4    Klasse, P.J.5
  • 29
    • 20644433322 scopus 로고    scopus 로고
    • The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles
    • Herrera C, Klasse PJ, Michael E, Kake S, Barnes K, et al. (2005) The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles. Virology 338: 154-172.
    • (2005) Virology , vol.338 , pp. 154-172
    • Herrera, C.1    Klasse, P.J.2    Michael, E.3    Kake, S.4    Barnes, K.5
  • 30
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton DR, Pyati J, Koduri R, Sharp SJ, Thornton GB, et al. (1994) Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266: 1024-1027.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1    Pyati, J.2    Koduri, R.3    Sharp, S.J.4    Thornton, G.B.5
  • 31
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola A, Purtscher M, Muster T, Ballaun C, Buchacher A, et al. (1996) Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J Virol 70: 1100-1108.
    • (1996) J Virol , vol.70 , pp. 1100-1108
    • Trkola, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4    Buchacher, A.5
  • 32
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, Wagner D, Phung P, et al. (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326: 285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3    Wagner, D.4    Phung, P.5
  • 33
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T, Steindl F, Purtscher M, Trkola A, Klima A, et al. (1993) A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J Virol 67: 6642-6647.
    • (1993) J Virol , vol.67 , pp. 6642-6647
    • Muster, T.1    Steindl, F.2    Purtscher, M.3    Trkola, A.4    Klima, A.5
  • 34
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick MB, Labrijn AF, Wang M, Spenlehauer C, Saphire EO, et al. (2001) Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J Virol 75: 10892-10905.
    • (2001) J Virol , vol.75 , pp. 10892-10905
    • Zwick, M.B.1    Labrijn, A.F.2    Wang, M.3    Spenlehauer, C.4    Saphire, E.O.5
  • 35
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope surface identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, Yang ZY, Li Y, Hogerkorp CM, Schief WR, et al. (2010) Rational design of envelope surface identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329: 856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1    Yang, Z.Y.2    Li, Y.3    Hogerkorp, C.M.4    Schief, W.R.5
  • 36
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-Electron Tomographic Structure of an Immunodeficiency Virus Envelope Complex In Situ
    • Zanetti G, Briggs JA, Grunewald K, Sattentau QJ, Fuller SD, (2006) Cryo-Electron Tomographic Structure of an Immunodeficiency Virus Envelope Complex In Situ. PLoS Pathog 2: e83.
    • (2006) PLoS Pathog , vol.2
    • Zanetti, G.1    Briggs, J.A.2    Grunewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 37
    • 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 KA, Roux KH, (2008) Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog 4: e1000203.
    • (2008) PLoS Pathog , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5
  • 39
    • 78650426126 scopus 로고    scopus 로고
    • Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure
    • Wu SR, Loving R, Lindqvist B, Hebert H, Koeck PJ, et al. (2010) Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure. Proc Natl Acad Sci U S A 107: 18844-18849.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18844-18849
    • Wu, S.R.1    Loving, R.2    Lindqvist, B.3    Hebert, H.4    Koeck, P.J.5
  • 40
    • 65249185539 scopus 로고    scopus 로고
    • Structure of the HIV-1 gp41 membrane-proximal ectodomain region in a putative prefusion conformation
    • Liu J, Deng Y, Dey AK, Moore JP, Lu M, (2009) Structure of the HIV-1 gp41 membrane-proximal ectodomain region in a putative prefusion conformation. Biochemistry 48: 2915-2923.
    • (2009) Biochemistry , vol.48 , pp. 2915-2923
    • Liu, J.1    Deng, Y.2    Dey, A.K.3    Moore, J.P.4    Lu, M.5
  • 41
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun ZY, Oh KJ, Kim M, Yu J, Brusic V, et al. (2008) HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 28: 52-63.
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1    Oh, K.J.2    Kim, M.3    Yu, J.4    Brusic, V.5
  • 42
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt R, Kwong PD, Desjardins E, Sweet RW, Robinson J, et al. (1998) The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393: 705-711.
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1    Kwong, P.D.2    Desjardins, E.3    Sweet, R.W.4    Robinson, J.5
  • 43
    • 0033919404 scopus 로고    scopus 로고
    • Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    • Kwong PD, Wyatt R, Sattentau QJ, Sodroski J, Hendrickson WA, (2000) Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J Virol 74: 1961-1972.
    • (2000) J Virol , vol.74 , pp. 1961-1972
    • Kwong, P.D.1    Wyatt, R.2    Sattentau, Q.J.3    Sodroski, J.4    Hendrickson, W.A.5
  • 44
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth E, Olshevsky U, Furman C, Sodroski J, (1991) Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J Virol 65: 2119-2123.
    • (1991) J Virol , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 45
    • 0037213299 scopus 로고    scopus 로고
    • Concordant modulation of neutralization resistance and high infectivity of the primary human immunodeficiency virus type 1 MN strain and definition of a potential gp41 binding site in gp120
    • Leavitt M, Park EJ, Sidorov IA, Dimitrov DS, Quinnan GV Jr, (2003) Concordant modulation of neutralization resistance and high infectivity of the primary human immunodeficiency virus type 1 MN strain and definition of a potential gp41 binding site in gp120. J Virol 77: 560-570.
    • (2003) J Virol , vol.77 , pp. 560-570
    • Leavitt, M.1    Park, E.J.2    Sidorov, I.A.3    Dimitrov, D.S.4    Quinnan Jr., G.V.5
  • 46
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley JM, Sanders RW, Clas B, Schuelke N, Master A, et al. (2000) A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J Virol 74: 627-643.
    • (2000) J Virol , vol.74 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5
  • 47
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • Chen B, Vogan EM, Gong H, Skehel JJ, Wiley DC, et al. (2005) Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433: 834-841.
    • (2005) Nature , vol.433 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5
  • 48
    • 0030730243 scopus 로고    scopus 로고
    • Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein
    • Wyatt R, Desjardin E, Olshevsky U, Nixon C, Binley J, et al. (1997) Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J Virol 71: 9722-9731.
    • (1997) J Virol , vol.71 , pp. 9722-9731
    • Wyatt, R.1    Desjardin, E.2    Olshevsky, U.3    Nixon, C.4    Binley, J.5
  • 49
    • 0142211253 scopus 로고    scopus 로고
    • Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41
    • Poumbourios P, Maerz AL, Drummer HE, (2003) Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41. J Biol Chem 278: 42149-42160.
    • (2003) J Biol Chem , vol.278 , pp. 42149-42160
    • Poumbourios, P.1    Maerz, A.L.2    Drummer, H.E.3
  • 50
    • 22844441184 scopus 로고    scopus 로고
    • Alanine scanning mutants of the HIV gp41 loop
    • Jacobs A, Sen J, Rong L, Caffrey M, (2005) Alanine scanning mutants of the HIV gp41 loop. J Biol Chem 280: 27284-27288.
    • (2005) J Biol Chem , vol.280 , pp. 27284-27288
    • Jacobs, A.1    Sen, J.2    Rong, L.3    Caffrey, M.4
  • 51
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • Wei X, Decker JM, Liu H, Zhang Z, Arani RB, et al. (2002) Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob Agents Chemother 46: 1896-1905.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3    Zhang, Z.4    Arani, R.B.5
  • 52
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor RI, Chen BK, Choe S, Landau NR, (1995) Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206: 935-944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 53
    • 33947600590 scopus 로고    scopus 로고
    • Cloning and characterization of functional subtype A HIV-1 envelope variants transmitted through breastfeeding
    • Rainwater SM, Wu X, Nduati R, Nedellec R, Mosier D, et al. (2007) Cloning and characterization of functional subtype A HIV-1 envelope variants transmitted through breastfeeding. Curr HIV Res 5: 189-197.
    • (2007) Curr HIV Res , vol.5 , pp. 189-197
    • Rainwater, S.M.1    Wu, X.2    Nduati, R.3    Nedellec, R.4    Mosier, D.5
  • 54
    • 0025268873 scopus 로고
    • Rapid complementation assays measuring replicative potential of human immunodeficiency virus type 1 envelope glycoprotein mutants
    • Helseth E, Kowalski M, Gabuzda D, Olshevsky U, Haseltine W, et al. (1990) Rapid complementation assays measuring replicative potential of human immunodeficiency virus type 1 envelope glycoprotein mutants. J Virol 64: 2416-2420.
    • (1990) J Virol , vol.64 , pp. 2416-2420
    • Helseth, E.1    Kowalski, M.2    Gabuzda, D.3    Olshevsky, U.4    Haseltine, W.5
  • 55
    • 0035202616 scopus 로고    scopus 로고
    • Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies
    • Zwick MB, Wang M, Poignard P, Stiegler G, Katinger H, et al. (2001) Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J Virol 75: 12198-12208.
    • (2001) J Virol , vol.75 , pp. 12198-12208
    • Zwick, M.B.1    Wang, M.2    Poignard, P.3    Stiegler, G.4    Katinger, H.5
  • 56
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • Zwick MB, Jensen R, Church S, Wang M, Stiegler G, et al. (2005) Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J Virol 79: 1252-1261.
    • (2005) J Virol , vol.79 , pp. 1252-1261
    • Zwick, M.B.1    Jensen, R.2    Church, S.3    Wang, M.4    Stiegler, G.5
  • 57
    • 23244434512 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies
    • Li M, Gao F, Mascola JR, Stamatatos L, Polonis VR, et al. (2005) Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J Virol 79: 10108-10125.
    • (2005) J Virol , vol.79 , pp. 10108-10125
    • Li, M.1    Gao, F.2    Mascola, J.R.3    Stamatatos, L.4    Polonis, V.R.5
  • 58
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, Hui H, Kappes JC, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422: 307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3    Hui, H.4    Kappes, J.C.5
  • 59
    • 0036260635 scopus 로고    scopus 로고
    • HIV type 1 variants transmitted to women in Kenya require the CCR5 coreceptor for entry, regardless of the genetic complexity of the infecting virus
    • Long EM, Rainwater SM, Lavreys L, Mandaliya K, Overbaugh J, (2002) HIV type 1 variants transmitted to women in Kenya require the CCR5 coreceptor for entry, regardless of the genetic complexity of the infecting virus. AIDS Res Hum Retroviruses 18: 567-576.
    • (2002) AIDS Res Hum Retroviruses , vol.18 , pp. 567-576
    • Long, E.M.1    Rainwater, S.M.2    Lavreys, L.3    Mandaliya, K.4    Overbaugh, J.5
  • 60
    • 45049083040 scopus 로고    scopus 로고
    • Relationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralization
    • Crooks ET, Jiang P, Franti M, Wong S, Zwick MB, et al. (2008) Relationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralization. Virology 377: 364-378.
    • (2008) Virology , vol.377 , pp. 364-378
    • Crooks, E.T.1    Jiang, P.2    Franti, M.3    Wong, S.4    Zwick, M.B.5
  • 61
    • 0029957230 scopus 로고    scopus 로고
    • Efficient infection of a human T-cell line and of human primary peripheral blood leukocytes with a pseudotyped retrovirus vector
    • Sharma S, Cantwell M, Kipps TJ, Friedmann T, (1996) Efficient infection of a human T-cell line and of human primary peripheral blood leukocytes with a pseudotyped retrovirus vector. Proc Natl Acad Sci U S A 93: 11842-11847.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11842-11847
    • Sharma, S.1    Cantwell, M.2    Kipps, T.J.3    Friedmann, T.4
  • 62
    • 0028155283 scopus 로고
    • Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization
    • Buchacher A, Predl R, Strutzenberger K, Steinfellner W, Trkola A, et al. (1994) Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res Hum Retroviruses 10: 359-369.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 359-369
    • Buchacher, A.1    Predl, R.2    Strutzenberger, K.3    Steinfellner, W.4    Trkola, A.5
  • 63
    • 34247106331 scopus 로고    scopus 로고
    • An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10
    • Nelson JD, Brunel FM, Jensen R, Crooks ET, Cardoso RM, et al. (2007) An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10. J Virol 81: 4033-4043.
    • (2007) J Virol , vol.81 , pp. 4033-4043
    • Nelson, J.D.1    Brunel, F.M.2    Jensen, R.3    Crooks, E.T.4    Cardoso, R.M.5
  • 64
    • 0037471318 scopus 로고    scopus 로고
    • Conformational changes in env oligomer induced by an antibody dependent on the V3 loop base
    • Cavacini L, Duval M, Song L, Sangster R, Xiang SH, et al. (2003) Conformational changes in env oligomer induced by an antibody dependent on the V3 loop base. Aids 17: 685-689.
    • (2003) Aids , vol.17 , pp. 685-689
    • Cavacini, L.1    Duval, M.2    Song, L.3    Sangster, R.4    Xiang, S.H.5
  • 65
    • 0026318224 scopus 로고
    • Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI
    • Peden K, Emerman M, Montagnier L, (1991) Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI. Virology 185: 661-672.
    • (1991) Virology , vol.185 , pp. 661-672
    • Peden, K.1    Emerman, M.2    Montagnier, L.3
  • 66
    • 0037311452 scopus 로고    scopus 로고
    • Two mechanisms for human immunodeficiency virus type 1 inhibition by N-terminal modifications of RANTES
    • Pastore C, Picchio GR, Galimi F, Fish R, Hartley O, et al. (2003) Two mechanisms for human immunodeficiency virus type 1 inhibition by N-terminal modifications of RANTES. Antimicrob Agents Chemother 47: 509-517.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 509-517
    • Pastore, C.1    Picchio, G.R.2    Galimi, F.3    Fish, R.4    Hartley, O.5
  • 67
    • 33646867165 scopus 로고    scopus 로고
    • The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent
    • Kirschner M, Monrose V, Paluch M, Techodamrongsin N, Rethwilm A, et al. (2006) The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent. Protein Expr Purif 48: 61-68.
    • (2006) Protein Expr Purif , vol.48 , pp. 61-68
    • Kirschner, M.1    Monrose, V.2    Paluch, M.3    Techodamrongsin, N.4    Rethwilm, A.5
  • 68
    • 0032992212 scopus 로고    scopus 로고
    • Variants from the diverse virus population identified at seroconversion of a clade A human immunodeficiency virus type 1-infected woman have distinct biological properties
    • Poss M, Overbaugh J, (1999) Variants from the diverse virus population identified at seroconversion of a clade A human immunodeficiency virus type 1-infected woman have distinct biological properties. J Virol 73: 5255-5264.
    • (1999) J Virol , vol.73 , pp. 5255-5264
    • Poss, M.1    Overbaugh, J.2
  • 69
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • Freed EO, Martin MA, (1996) Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions. J Virol 70: 341-351.
    • (1996) J Virol , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 70
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger H, Cramer WA, von Jagow G, (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal Biochem 217: 220-230.
    • (1994) Anal Biochem , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 71
    • 0036315133 scopus 로고    scopus 로고
    • Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein
    • Schulke N, Vesanen MS, Sanders RW, Zhu P, Lu M, et al. (2002) Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein. J Virol 76: 7760-7776.
    • (2002) J Virol , vol.76 , pp. 7760-7776
    • Schulke, N.1    Vesanen, M.S.2    Sanders, R.W.3    Zhu, P.4    Lu, M.5
  • 72
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme Digests Eliminate Non-Functional Env from HIV-1 Particle Surfaces Leaving Native Env Trimers Intact and Viral Infectivity Unaffected
    • In Press
    • Crooks ET, Tong T, Osawa K, Binley JM, (2011) Enzyme Digests Eliminate Non-Functional Env from HIV-1 Particle Surfaces Leaving Native Env Trimers Intact and Viral Infectivity Unaffected. J Virol In Press.
    • (2011) J Virol
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 73
    • 0041823452 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: virion-associated cholesterol is required for fusion and infection of susceptible cells
    • Liao Z, Graham DR, Hildreth JE, (2003) Lipid rafts and HIV pathogenesis: virion-associated cholesterol is required for fusion and infection of susceptible cells. AIDS Res Hum Retroviruses 19: 675-687.
    • (2003) AIDS Res Hum Retroviruses , vol.19 , pp. 675-687
    • Liao, Z.1    Graham, D.R.2    Hildreth, J.E.3
  • 74
    • 0026356172 scopus 로고
    • Identification of a determinant within the human immunodeficiency virus 1 surface envelope glycoprotein critical for productive infection of primary monocytes
    • Westervelt P, Gendelman HE, Ratner L, (1991) Identification of a determinant within the human immunodeficiency virus 1 surface envelope glycoprotein critical for productive infection of primary monocytes. Proc Natl Acad Sci U S A 88: 3097-3101.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3097-3101
    • Westervelt, P.1    Gendelman, H.E.2    Ratner, L.3
  • 75
    • 0023898273 scopus 로고
    • Efficient isolation and propagation of human immunodeficiency virus on recombinant colony-stimulating factor 1-treated monocytes
    • Gendelman HE, Orenstein JM, Martin MA, Ferrua C, Mitra R, et al. (1988) Efficient isolation and propagation of human immunodeficiency virus on recombinant colony-stimulating factor 1-treated monocytes. J Exp Med 167: 1428-1441.
    • (1988) J Exp Med , vol.167 , pp. 1428-1441
    • Gendelman, H.E.1    Orenstein, J.M.2    Martin, M.A.3    Ferrua, C.4    Mitra, R.5
  • 76
    • 0023214674 scopus 로고
    • Dual infection of the central nervous system by AIDS viruses with distinct cellular tropisms
    • Koyanagi Y, Miles S, Mitsuyasu RT, Merrill JE, Vinters HV, et al. (1987) Dual infection of the central nervous system by AIDS viruses with distinct cellular tropisms. Science 236: 819-822.
    • (1987) Science , vol.236 , pp. 819-822
    • Koyanagi, Y.1    Miles, S.2    Mitsuyasu, R.T.3    Merrill, J.E.4    Vinters, H.V.5
  • 77
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel K, West JT, Hunter E, (1999) A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J Virol 73: 2469-2480.
    • (1999) J Virol , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 78
    • 0029836434 scopus 로고    scopus 로고
    • Increased envelope spike density and stability are not required for the neutralization resistance of primary human immunodeficiency viruses
    • Karlsson GB, Gao F, Robinson J, Hahn B, Sodroski J, (1996) Increased envelope spike density and stability are not required for the neutralization resistance of primary human immunodeficiency viruses. J Virol 70: 6136-6142.
    • (1996) J Virol , vol.70 , pp. 6136-6142
    • Karlsson, G.B.1    Gao, F.2    Robinson, J.3    Hahn, B.4    Sodroski, J.5
  • 79
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu X, Zhou T, O'Dell S, Wyatt RT, Kwong PD, et al. (2009) Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J Virol 83: 10892-10907.
    • (2009) J Virol , vol.83 , pp. 10892-10907
    • Wu, X.1    Zhou, T.2    O'Dell, S.3    Wyatt, R.T.4    Kwong, P.D.5
  • 80
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley JM, Cayanan CS, Wiley C, Schulke N, Olson WC, et al. (2003) Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J Virol 77: 5678-5684.
    • (2003) J Virol , vol.77 , pp. 5678-5684
    • Binley, J.M.1    Cayanan, C.S.2    Wiley, C.3    Schulke, N.4    Olson, W.C.5
  • 81
    • 66149136375 scopus 로고    scopus 로고
    • Identification of a human immunodeficiency virus type 1 envelope glycoprotein variant resistant to cold inactivation
    • Kassa A, Finzi A, Pancera M, Courter JR, Smith AB 3rd, et al. (2009) Identification of a human immunodeficiency virus type 1 envelope glycoprotein variant resistant to cold inactivation. J Virol 83: 4476-4488.
    • (2009) J Virol , vol.83 , pp. 4476-4488
    • Kassa, A.1    Finzi, A.2    Pancera, M.3    Courter, J.R.4    Smith III, A.B.5
  • 82
    • 69749111210 scopus 로고    scopus 로고
    • Increased thermostability and fidelity of DNA synthesis of wild-type and mutant HIV-1 group O reverse transcriptases
    • Alvarez M, Matamoros T, Menendez-Arias L, (2009) Increased thermostability and fidelity of DNA synthesis of wild-type and mutant HIV-1 group O reverse transcriptases. J Mol Biol 392: 872-884.
    • (2009) J Mol Biol , vol.392 , pp. 872-884
    • Alvarez, M.1    Matamoros, T.2    Menendez-Arias, L.3
  • 83
    • 0025989856 scopus 로고
    • Blocking of human immunodeficiency virus infection depends on cell density and viral stock age
    • Layne SP, Merges MJ, Spouge JL, Dembo M, Nara PL, (1991) Blocking of human immunodeficiency virus infection depends on cell density and viral stock age. J Virol 65: 3293-3300.
    • (1991) J Virol , vol.65 , pp. 3293-3300
    • Layne, S.P.1    Merges, M.J.2    Spouge, J.L.3    Dembo, M.4    Nara, P.L.5
  • 84
    • 59749083598 scopus 로고    scopus 로고
    • Estimating the stoichiometry of human immunodeficiency virus entry
    • Magnus C, Rusert P, Bonhoeffer S, Trkola A, Regoes RR, (2009) Estimating the stoichiometry of human immunodeficiency virus entry. J Virol 83: 1523-1531.
    • (2009) J Virol , vol.83 , pp. 1523-1531
    • Magnus, C.1    Rusert, P.2    Bonhoeffer, S.3    Trkola, A.4    Regoes, R.R.5
  • 85
    • 0026755629 scopus 로고
    • Factors underlying spontaneous inactivation and susceptibility to neutralization of human immunodeficiency virus
    • Layne SP, Merges MJ, Dembo M, Spouge JL, Conley SR, et al. (1992) Factors underlying spontaneous inactivation and susceptibility to neutralization of human immunodeficiency virus. Virology 189: 695-714.
    • (1992) Virology , vol.189 , pp. 695-714
    • Layne, S.P.1    Merges, M.J.2    Dembo, M.3    Spouge, J.L.4    Conley, S.R.5
  • 86
    • 51649128064 scopus 로고    scopus 로고
    • Thermostability of model protocell membranes
    • Mansy SS, Szostak JW, (2008) Thermostability of model protocell membranes. Proc Natl Acad Sci U S A 105: 13351-13355.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13351-13355
    • Mansy, S.S.1    Szostak, J.W.2
  • 87
    • 49049109812 scopus 로고    scopus 로고
    • Suboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturation
    • Moore MD, Fu W, Soheilian F, Nagashima K, Ptak RG, et al. (2008) Suboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturation. Virology 379: 152-160.
    • (2008) Virology , vol.379 , pp. 152-160
    • Moore, M.D.1    Fu, W.2    Soheilian, F.3    Nagashima, K.4    Ptak, R.G.5
  • 88
    • 52049093876 scopus 로고    scopus 로고
    • Moloney murine leukemia virus decay mediated by retroviral reverse transcriptase degradation of genomic RNA
    • Casali M, Zambonelli C, Goldwasser J, Vu HN, Yarmush ML, (2008) Moloney murine leukemia virus decay mediated by retroviral reverse transcriptase degradation of genomic RNA. Virology 380: 91-98.
    • (2008) Virology , vol.380 , pp. 91-98
    • Casali, M.1    Zambonelli, C.2    Goldwasser, J.3    Vu, H.N.4    Yarmush, M.L.5
  • 89
    • 73549091727 scopus 로고    scopus 로고
    • Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding
    • Kahle KM, Steger HK, Root MJ, (2009) Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. PLoS Pathog 5: e1000674.
    • (2009) PLoS Pathog , vol.5
    • Kahle, K.M.1    Steger, H.K.2    Root, M.J.3
  • 90
    • 14644390952 scopus 로고    scopus 로고
    • Construction of stabilized proteins by combinatorial consensus mutagenesis
    • Amin N, Liu AD, Ramer S, Aehle W, Meijer D, et al. (2004) Construction of stabilized proteins by combinatorial consensus mutagenesis. Protein Eng Des Sel 17: 787-793.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 787-793
    • Amin, N.1    Liu, A.D.2    Ramer, S.3    Aehle, W.4    Meijer, D.5
  • 91
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: stability and function in aqueous and organic solvents
    • Cowan DA, (1997) Thermophilic proteins: stability and function in aqueous and organic solvents. Comp Biochem Physiol A Physiol 118: 429-438.
    • (1997) Comp Biochem Physiol A Physiol , vol.118 , pp. 429-438
    • Cowan, D.A.1
  • 92
    • 0042823437 scopus 로고    scopus 로고
    • Regional heterogeneity of cellular prion protein isoforms in the mouse brain
    • Beringue V, Mallinson G, Kaisar M, Tayebi M, Sattar Z, et al. (2003) Regional heterogeneity of cellular prion protein isoforms in the mouse brain. Brain 126: 2065-2073.
    • (2003) Brain , vol.126 , pp. 2065-2073
    • Beringue, V.1    Mallinson, G.2    Kaisar, M.3    Tayebi, M.4    Sattar, Z.5
  • 93
    • 79952732800 scopus 로고    scopus 로고
    • MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1
    • Ruprecht CR, Krarup A, Reynell L, Mann AM, Brandenberg OF, et al. (2011) MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1. J Exp Med 208: 439-454.
    • (2011) J Exp Med , vol.208 , pp. 439-454
    • Ruprecht, C.R.1    Krarup, A.2    Reynell, L.3    Mann, A.M.4    Brandenberg, O.F.5
  • 94
    • 0042389489 scopus 로고    scopus 로고
    • Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits
    • Yang X, Mahony E, Holm GH, Kassa A, Sodroski J, (2003) Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits. Virology 313: 117-125.
    • (2003) Virology , vol.313 , pp. 117-125
    • Yang, X.1    Mahony, E.2    Holm, G.H.3    Kassa, A.4    Sodroski, J.5
  • 95
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao J, Bergeron L, Helseth E, Thali M, Repke H, et al. (1993) Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J Virol 67: 2747-2755.
    • (1993) J Virol , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5
  • 96
    • 4544373403 scopus 로고    scopus 로고
    • Role of hydrophobic residues in the central ectodomain of gp41 in maintaining the association between human immunodeficiency virus type 1 envelope glycoprotein subunits gp120 and gp41
    • York J, Nunberg JH, (2004) Role of hydrophobic residues in the central ectodomain of gp41 in maintaining the association between human immunodeficiency virus type 1 envelope glycoprotein subunits gp120 and gp41. J Virol 78: 4921-4926.
    • (2004) J Virol , vol.78 , pp. 4921-4926
    • York, J.1    Nunberg, J.H.2
  • 97
    • 33845266437 scopus 로고    scopus 로고
    • Structural analysis and assembly of the HIV-1 Gp41 amino-terminal fusion peptide and the pretransmembrane amphipathic-at-interface sequence
    • Lorizate M, de la Arada I, Huarte N, Sanchez-Martinez S, de la Torre BG, et al. (2006) Structural analysis and assembly of the HIV-1 Gp41 amino-terminal fusion peptide and the pretransmembrane amphipathic-at-interface sequence. Biochemistry 45: 14337-14346.
    • (2006) Biochemistry , vol.45 , pp. 14337-14346
    • Lorizate, M.1    de la Arada, I.2    Huarte, N.3    Sanchez-Martinez, S.4    de la Torre, B.G.5
  • 98
    • 79959616682 scopus 로고    scopus 로고
    • Targeting HIV-1 gp41 in close proximity to the membrane using antibody and other molecules
    • In Press
    • Gach JS, Leaman DP, Zwick M, (2011) Targeting HIV-1 gp41 in close proximity to the membrane using antibody and other molecules. Curr Top Med Chem In Press.
    • (2011) Curr Top Med Chem
    • Gach, J.S.1    Leaman, D.P.2    Zwick, M.3
  • 99
    • 0346220015 scopus 로고    scopus 로고
    • Peptide-induced formation of cholesterol-rich domains
    • Epand RM, Sayer BG, Epand RF, (2003) Peptide-induced formation of cholesterol-rich domains. Biochemistry 42: 14677-14689.
    • (2003) Biochemistry , vol.42 , pp. 14677-14689
    • Epand, R.M.1    Sayer, B.G.2    Epand, R.F.3
  • 100
    • 69249202492 scopus 로고    scopus 로고
    • Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain
    • Kassa A, Madani N, Schon A, Haim H, Finzi A, et al. (2009) Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain. J Virol 83: 8364-8378.
    • (2009) J Virol , vol.83 , pp. 8364-8378
    • Kassa, A.1    Madani, N.2    Schon, A.3    Haim, H.4    Finzi, A.5
  • 101
    • 77749329921 scopus 로고    scopus 로고
    • Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions
    • Finzi A, Xiang SH, Pacheco B, Wang L, Haight J, et al. (2010) Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol Cell 37: 656-667.
    • (2010) Mol Cell , vol.37 , pp. 656-667
    • Finzi, A.1    Xiang, S.H.2    Pacheco, B.3    Wang, L.4    Haight, J.5
  • 102
    • 19444376783 scopus 로고    scopus 로고
    • Neutralization sensitivity of HIV-1 Env-pseudotyped virus clones is determined by co-operativity between mutations which modulate the CD4-binding site and those that affect gp120-gp41 stability
    • Beddows S, Zheng NN, Herrera C, Michael E, Barnes K, et al. (2005) Neutralization sensitivity of HIV-1 Env-pseudotyped virus clones is determined by co-operativity between mutations which modulate the CD4-binding site and those that affect gp120-gp41 stability. Virology 337: 136-148.
    • (2005) Virology , vol.337 , pp. 136-148
    • Beddows, S.1    Zheng, N.N.2    Herrera, C.3    Michael, E.4    Barnes, K.5
  • 103
    • 41149099165 scopus 로고    scopus 로고
    • Variation in HIV-1 R5 macrophage-tropism correlates with sensitivity to reagents that block envelope: CD4 interactions but not with sensitivity to other entry inhibitors
    • Peters PJ, Duenas-Decamp MJ, Sullivan WM, Brown R, Ankghuambom C, et al. (2008) Variation in HIV-1 R5 macrophage-tropism correlates with sensitivity to reagents that block envelope: CD4 interactions but not with sensitivity to other entry inhibitors. Retrovirology 5: 5.
    • (2008) Retrovirology , vol.5 , pp. 5
    • Peters, P.J.1    Duenas-Decamp, M.J.2    Sullivan, W.M.3    Brown, R.4    Ankghuambom, C.5
  • 104
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves JD, Gallo SA, Ahmad N, Miamidian JL, Harvey PE, et al. (2002) Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc Natl Acad Sci U S A 99: 16249-16254.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmad, N.3    Miamidian, J.L.4    Harvey, P.E.5
  • 105
    • 0030023304 scopus 로고    scopus 로고
    • Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation
    • Poignard P, Fouts T, Naniche D, Moore JP, Sattentau QJ, (1996) Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J Exp Med 183: 473-484.
    • (1996) J Exp Med , vol.183 , pp. 473-484
    • Poignard, P.1    Fouts, T.2    Naniche, D.3    Moore, J.P.4    Sattentau, Q.J.5
  • 106
    • 26844552845 scopus 로고    scopus 로고
    • Persistence of HIV-1 structural proteins and glycoproteins in lymph nodes of patients under highly active antiretroviral therapy
    • Popovic M, Tenner-Racz K, Pelser C, Stellbrink HJ, van Lunzen J, et al. (2005) Persistence of HIV-1 structural proteins and glycoproteins in lymph nodes of patients under highly active antiretroviral therapy. Proc Natl Acad Sci U S A 102: 14807-14812.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14807-14812
    • Popovic, M.1    Tenner-Racz, K.2    Pelser, C.3    Stellbrink, H.J.4    van Lunzen, J.5
  • 107
    • 70349326548 scopus 로고    scopus 로고
    • HIV-1 envelope protein gp120 is present at high concentrations in secondary lymphoid organs of individuals with chronic HIV-1 infection
    • Santosuosso M, Righi E, Lindstrom V, Leblanc PR, Poznansky MC, (2009) HIV-1 envelope protein gp120 is present at high concentrations in secondary lymphoid organs of individuals with chronic HIV-1 infection. J Infect Dis 200: 1050-1053.
    • (2009) J Infect Dis , vol.200 , pp. 1050-1053
    • Santosuosso, M.1    Righi, E.2    Lindstrom, V.3    Leblanc, P.R.4    Poznansky, M.C.5
  • 108
    • 77954042425 scopus 로고    scopus 로고
    • Few and far between: how HIV may be evading antibody avidity
    • Klein JS, Bjorkman PJ, (2010) Few and far between: how HIV may be evading antibody avidity. PLoS Pathog 6: e1000908.
    • (2010) PLoS Pathog , vol.6
    • Klein, J.S.1    Bjorkman, P.J.2
  • 109
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, Liu J, Bess J Jr, Chertova E, Lifson JD, et al. (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441: 847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess Jr., J.3    Chertova, E.4    Lifson, J.D.5
  • 110
    • 33947212334 scopus 로고    scopus 로고
    • Recirculation of germinal center B cells: a multilevel selection strategy for antibody maturation
    • Or-Guil M, Wittenbrink N, Weiser AA, Schuchhardt J, (2007) Recirculation of germinal center B cells: a multilevel selection strategy for antibody maturation. Immunol Rev 216: 130-141.
    • (2007) Immunol Rev , vol.216 , pp. 130-141
    • Or-Guil, M.1    Wittenbrink, N.2    Weiser, A.A.3    Schuchhardt, J.4
  • 111
    • 0032905728 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 neutralizing antibodies accelerate clearance of cell-free virions from blood plasma
    • Igarashi T, Brown C, Azadegan A, Haigwood N, Dimitrov D, et al. (1999) Human immunodeficiency virus type 1 neutralizing antibodies accelerate clearance of cell-free virions from blood plasma. Nat Med 5: 211-216.
    • (1999) Nat Med , vol.5 , pp. 211-216
    • Igarashi, T.1    Brown, C.2    Azadegan, A.3    Haigwood, N.4    Dimitrov, D.5
  • 112
    • 33845288582 scopus 로고    scopus 로고
    • Complement lysis activity in autologous plasma is associated with lower viral loads during the acute phase of HIV-1 infection
    • Huber M, Fischer M, Misselwitz B, Manrique A, Kuster H, et al. (2006) Complement lysis activity in autologous plasma is associated with lower viral loads during the acute phase of HIV-1 infection. PLoS Med 3: e441.
    • (2006) PLoS Med , vol.3
    • Huber, M.1    Fischer, M.2    Misselwitz, B.3    Manrique, A.4    Kuster, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.