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Volumn 8, Issue 11, 2013, Pages

The influence of N-linked glycans on the molecular dynamics of the HIV-1 gp120 V3 loop

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN DERIVATIVE; GLYCOPROTEIN GP 120; MANNOSE;

EID: 84896716465     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080301     Document Type: Article
Times cited : (34)

References (97)
  • 1
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • DOI 10.1126/science.280.5371.1884
    • Wyatt R, Sodroski J (1998) The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280: 1884-1888. (Pubitemid 28299385)
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 2
    • 33747262026 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus (HIV) glycans with lectins of the human immune system
    • Ji X, Chen Y, Faro J, Gewurz H, Bremer J, et al. (2006) Interaction of human immunodeficiency virus (HIV) glycans with lectins of the human immune system. Curr Protein Pept Sci 7: 317-324.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 317-324
    • Ji, X.1    Chen, Y.2    Faro, J.3    Gewurz, H.4    Bremer, J.5
  • 3
    • 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
  • 4
    • 0023807495 scopus 로고
    • Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells
    • Mizuochi T, Spellman MW, Larkin M, Solomon J, Basa LJ, et al. (1988) Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells. Biochem J 254: 599-603.
    • (1988) Biochem J , vol.254 , pp. 599-603
    • Mizuochi, T.1    Spellman, M.W.2    Larkin, M.3    Solomon, J.4    Basa, L.J.5
  • 5
    • 0026606297 scopus 로고
    • The emergence of simian/human immunodeficiency viruses
    • Myers G, MacInnes K, Korber B (1992) The emergence of simian/human immunodeficiency viruses. AIDS Res Hum Retroviruses 8: 373-386.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 373-386
    • Myers, G.1    MacInnes, K.2    Korber, B.3
  • 7
    • 0034845609 scopus 로고    scopus 로고
    • Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum
    • DOI 10.1016/S0300-9084(01)01314-1
    • Land A, Braakman I (2001) Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. Biochimie 83: 783-790. (Pubitemid 32821244)
    • (2001) Biochimie , vol.83 , Issue.8 , pp. 783-790
    • Land, A.1    Braakman, I.2
  • 8
    • 0027535672 scopus 로고
    • Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding
    • Li Y, Luo L, Rasool N, Kang CY (1993) Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding. J Virol 67: 584-588. (Pubitemid 23003026)
    • (1993) Journal of Virology , vol.67 , Issue.1 , pp. 584-588
    • Li, Y.1    Luo, L.2    Rasool, N.3    Kang, C.Y.4
  • 10
    • 0031713177 scopus 로고    scopus 로고
    • Location-specific, unequal contribution of the N glycans in simian immunodeficiency virus gp120 to viral infectivity and removal of multiple glycans without disturbing infectivity
    • Ohgimoto S, Shioda T, Mori K, Nakayama EE, Hu H, et al. (1998) Location-specific, unequal contribution of the N glycans in simian immunodeficiency virus gp120 to viral infectivity and removal of multiple glycans without disturbing infectivity. J Virol 72: 8365-8370. (Pubitemid 28421840)
    • (1998) Journal of Virology , vol.72 , Issue.10 , pp. 8365-8370
    • Ohgimoto, S.1    Shioda, T.2    Mori, K.3    Nakayama, E.E.4    Hu, H.5    Nagai, Y.6
  • 11
    • 0029940696 scopus 로고    scopus 로고
    • Rapid selection for an N-linked oligosaccharide by monoclonal antibodies directed against the V3 loop of human immunodeficiency virus type 1
    • Schonning K, Jansson B, Olofsson S, Hansen JE (1996) Rapid selection for an N-linked oligosaccharide by monoclonal antibodies directed against the V3 loop of human immunodeficiency virus type 1. J Gen Virol 77 (Pt 4): 753-758. (Pubitemid 26121808)
    • (1996) Journal of General Virology , vol.77 , Issue.4 , pp. 753-758
    • Schonning, K.1    Jansson, B.2    Olofsson, S.3    Hansen, J.-E.S.4
  • 12
    • 0035851347 scopus 로고    scopus 로고
    • Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals: Effects of elimination of the V3 N306 glycan
    • DOI 10.1016/S0264-410X(01)00358-9, PII S0264410X01003589
    • Bolmstedt A, Hinkula J, Rowcliffe E, Biller M, Wahren B, et al. (2001) Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals. Effects of elimination of the V3 N306 glycan. Vaccine 20: 397-405. (Pubitemid 32973781)
    • (2001) Vaccine , vol.20 , Issue.3-4 , pp. 397-405
    • Bolmstedt, A.1    Hinkula, J.2    Rowcliffe, E.3    Biller, M.4    Wahren, B.5    Olofsson, S.6
  • 13
    • 0030842609 scopus 로고    scopus 로고
    • Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies
    • Chackerian B, Rudensey LM, Overbaugh J (1997) Specific N-linked and Olinked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies. J Virol 71: 7719-7727. (Pubitemid 27391717)
    • (1997) Journal of Virology , vol.71 , Issue.10 , pp. 7719-7727
    • Chackerian, B.1    Rudensey, L.M.2    Overbaugh, J.3
  • 14
    • 0033033625 scopus 로고    scopus 로고
    • Selection for neutralization resistance of the simian/human immunodeficiency virus SHIV(SF33A) variant in vivo by virtue of sequence changes in the extracellular envelope glycoprotein that modify N-linked glycosylation
    • Cheng-Mayer C, Brown A, Harouse J, Luciw PA, Mayer AJ (1999) Selection for neutralization resistance of the simian/human immunodeficiency virus SHIVSF33A variant in vivo by virtue of sequence changes in the extracellular envelope glycoprotein that modify N-linked glycosylation. J Virol 73: 5294-5300. (Pubitemid 29274810)
    • (1999) Journal of Virology , vol.73 , Issue.7 , pp. 5294-5300
    • Cheng-Mayer, C.1    Brown, A.2    Harouse, J.3    Luciw, P.A.4    Mayer, A.J.5
  • 15
    • 9944225582 scopus 로고    scopus 로고
    • Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies
    • DOI 10.1016/j.virol.2004.10.005, PII S0042682204006518
    • Kang SM, Quan FS, Huang C, Guo L, Ye L, et al. (2005) Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies. Virology 331: 20-32. (Pubitemid 39593630)
    • (2005) Virology , vol.331 , Issue.1 , pp. 20-32
    • Kang, S.-M.1    Shi, Q.F.2    Huang, C.3    Guo, L.4    Ye, L.5    Yang, C.6    Compans, R.W.7
  • 16
    • 1842562419 scopus 로고    scopus 로고
    • N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies
    • DOI 10.1128/JVI.78.7.3279-3295.2004
    • McCaffrey RA, Saunders C, Hensel M, Stamatatos L (2004) N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J Virol 78: 3279-3295. (Pubitemid 38568268)
    • (2004) Journal of Virology , vol.78 , Issue.7 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 17
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, Huber M, Doores KJ, Falkowska E, Pejchal R, et al. (2011) Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477: 466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3    Falkowska, E.4    Pejchal, R.5
  • 18
    • 71049141219 scopus 로고    scopus 로고
    • Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1
    • Nandi A, Lavine CL, Wang P, Lipchina I, Goepfert PA, et al. (2010) Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1. Virology 396: 339-348.
    • (2010) Virology , vol.396 , pp. 339-348
    • Nandi, A.1    Lavine, C.L.2    Wang, P.3    Lipchina, I.4    Goepfert, P.A.5
  • 19
    • 84869155712 scopus 로고    scopus 로고
    • Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape
    • Moore PL, Gray ES, Wibmer CK, Bhiman JN, Nonyane M, et al. (2012) Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat Med.
    • (2012) Nat Med
    • Moore, P.L.1    Gray, E.S.2    Wibmer, C.K.3    Bhiman, J.N.4    Nonyane, M.5
  • 20
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, Doores KJ, Walker LM, Khayat R, Huang P-S, et al. (2011) A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334: 1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1    Doores, K.J.2    Walker, L.M.3    Khayat, R.4    Huang, P.-S.5
  • 22
    • 0035918220 scopus 로고    scopus 로고
    • N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization
    • Pollakis G, Kang S, Kliphuis A, Chalaby MI, Goudsmit J, et al. (2001) N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. J Biol Chem 276: 13433-13441.
    • (2001) J Biol Chem , vol.276 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5
  • 23
    • 84857564233 scopus 로고    scopus 로고
    • Glycosylation assists binding of HIV protein gp120 to human CD4 receptor
    • Wilhelm D, Behnken HN, Meyer B (2012) Glycosylation assists binding of HIV protein gp120 to human CD4 receptor. Chembiochem 13: 524-527.
    • (2012) Chembiochem , vol.13 , pp. 524-527
    • Wilhelm, D.1    Behnken, H.N.2    Meyer, B.3
  • 24
    • 84865066445 scopus 로고    scopus 로고
    • Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120
    • Guttman M, Kahn M, Garcia NK, Hu SL, Lee KK (2012) Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120. J Virol 86: 8750-8764.
    • (2012) J Virol , vol.86 , pp. 8750-8764
    • Guttman, M.1    Kahn, M.2    Garcia, N.K.3    Hu, S.L.4    Lee, K.K.5
  • 25
    • 16044364731 scopus 로고    scopus 로고
    • HIV-1 subtype and second-receptor use
    • Zhang L, Huang Y, He T, Cao Y, Ho DD (1996) HIV-1 subtype and second-receptor use. Nature 383: 768.
    • (1996) Nature , vol.383 , pp. 768
    • Zhang, L.1    Huang, Y.2    He, T.3    Cao, Y.4    Ho, D.D.5
  • 26
    • 0035173908 scopus 로고    scopus 로고
    • HIV-1 receptors and cell tropism
    • DOI 10.1093/bmb/58.1.43
    • Clapham PR, McKnight A (2001) HIV-1 receptors and cell tropism. Br Med Bull 58: 43-59. (Pubitemid 33070763)
    • (2001) British Medical Bulletin , vol.58 , pp. 43-59
    • Clapham, P.R.1    McKnight, A.2
  • 27
    • 63149107038 scopus 로고    scopus 로고
    • Relationship between HIV coreceptor tropism and disease progression in persons with untreated chronic HIV infection
    • Goetz MB, Leduc R, Kostman JR, Labriola AM, Lie Y, et al. (2009) Relationship between HIV coreceptor tropism and disease progression in persons with untreated chronic HIV infection. J Acquir Immune Defic Syndr 50: 259-266.
    • (2009) J Acquir Immune Defic Syndr , vol.50 , pp. 259-266
    • Goetz, M.B.1    Leduc, R.2    Kostman, J.R.3    Labriola, A.M.4    Lie, Y.5
  • 30
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272: 872-877. (Pubitemid 26154590)
    • (1996) Science , vol.272 , Issue.5263 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 31
    • 0027154014 scopus 로고
    • A single amino acid substitution in the V1 loop of human immunodeficiency virus type 1 gp120 alters cellular tropism
    • Boyd MT, Simpson GR, Cann AJ, Johnson MA, Weiss RA (1993) A single amino acid substitution in the V1 loop of human immunodeficiency virus type 1 gp120 alters cellular tropism. J Virol 67: 3649-3652. (Pubitemid 23143749)
    • (1993) Journal of Virology , vol.67 , Issue.6 , pp. 3649-3652
    • Boyd, M.T.1    Simpson, G.R.2    Cann, A.J.3    Johnson, M.A.4    Weiss, R.A.5
  • 32
    • 0030053670 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 tropism for T-lymphoid cell lines: Role of the V3 loop and C4 envelope determinants
    • Carrillo A, Ratner L (1996) Human immunodeficiency virus type 1 tropism for T-lymphoid cell lines: role of the V3 loop and C4 envelope determinants. J Virol 70: 1301-1309. (Pubitemid 26029061)
    • (1996) Journal of Virology , vol.70 , Issue.2 , pp. 1301-1309
    • Carrillo, A.1    Ratner, L.2
  • 34
    • 0031978550 scopus 로고    scopus 로고
    • Determinants of entry cofactor utilization and tropism in a dualtropic human immunodeficiency virus type 1 primary isolate
    • Smyth RJ, Yi Y, Singh A, Collman RG (1998) Determinants of entry cofactor utilization and tropism in a dualtropic human immunodeficiency virus type 1 primary isolate. J Virol 72: 4478-4484. (Pubitemid 28188761)
    • (1998) Journal of Virology , vol.72 , Issue.5 , pp. 4478-4484
    • Smyth, R.J.1    Yi, Y.2    Singh, A.3    Collman, R.G.4
  • 35
    • 0029955497 scopus 로고    scopus 로고
    • The V3 domain of the HIV-1 gp120 envelope glycoprotein is critical for chemokine-mediated blockade of infection
    • DOI 10.1038/nm1196-1244
    • Cocchi F, DeVico AL, Garzino-Demo A, Cara A, Gallo RC, et al. (1996) The V3 domain of the HIV-1 gp120 envelope glycoprotein is critical for chemokine-mediated blockade of infection. Nat Med 2: 1244-1247. (Pubitemid 26375410)
    • (1996) Nature Medicine , vol.2 , Issue.11 , pp. 1244-1247
    • Cocchi, F.1    DeVico, A.L.2    Garzino-Demo, A.3    Cara, A.4    Gallo, R.C.5    Lusso, P.6
  • 36
    • 0346365289 scopus 로고    scopus 로고
    • Intrapatient Alterations in the Human Immunodeficiency Virus Type 1 gp120 V1V2 and V3 Regions Differentially Modulate Coreceptor Usage, Virus Inhibition by CC/CXC Chemokines, Soluble CD4, and the b12 and 2G12 Monoclonal Antibodies
    • DOI 10.1128/JVI.78.1.524-530.2004
    • Nabatov AA, Pollakis G, Linnemann T, Kliphius A, Chalaby MI, et al. (2004) Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies. J Virol 78: 524-530. (Pubitemid 37549764)
    • (2004) Journal of Virology , vol.78 , Issue.1 , pp. 524-530
    • Nabatov, A.A.1    Pollakis, G.2    Linnemann, T.3    Kliphius, A.4    Chalaby, M.I.M.5    Paxton, W.A.6
  • 37
    • 34047202703 scopus 로고    scopus 로고
    • Structural descriptors of gp120 V3 loop for the prediction of HIV-1 coreceptor usage
    • Sander O, Sing T, Sommer I, Low AJ, Cheung PK, et al. (2007) Structural descriptors of gp120 V3 loop for the prediction of HIV-1 coreceptor usage. PLoS Comput Biol 3: e58.
    • (2007) PLoS Comput Biol , vol.3
    • Sander, O.1    Sing, T.2    Sommer, I.3    Low, A.J.4    Cheung, P.K.5
  • 38
    • 0030810706 scopus 로고    scopus 로고
    • Selective employment of chemokine receptors as human immunodeficiency virus type 1 coreceptors determined by individual amino acids within the envelope V3 loop
    • Speck RF, Wehrly K, Platt EJ, Atchison RE, Charo IF, et al. (1997) Selective employment of chemokine receptors as human immunodeficiency virus type 1 coreceptors determined by individual amino acids within the envelope V3 loop. J Virol 71: 7136-7139. (Pubitemid 27355386)
    • (1997) Journal of Virology , vol.71 , Issue.9 , pp. 7136-7139
    • Speck, R.F.1    Wehrly, K.2    Platt, E.J.3    Atchison, R.E.4    Charo, I.F.5    Kabat, D.6    Chesebro, B.7    Goldsmith, M.A.8
  • 40
    • 0026702003 scopus 로고
    • Minimal requirements for the human immunodeficiency virus type 1 V3 domain to support the syncytium-inducing phenotype: Analysis by single amino acid substitution
    • De Jong JJ, De Ronde A, Keulen W, Tersmette M, Goudsmit J (1992) Minimal requirements for the human immunodeficiency virus type 1 V3 domain to support the syncytium-inducing phenotype: analysis by single amino acid substitution. J Virol 66: 6777-6780.
    • (1992) J Virol , vol.66 , pp. 6777-6780
    • De Jong, J.J.1    De Ronde, A.2    Keulen, W.3    Tersmette, M.4    Goudsmit, J.5
  • 41
    • 33644609596 scopus 로고    scopus 로고
    • CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop Nlinked glycosylation site
    • Clevestig P, Pramanik L, Leitner T, Ehrnst A (2006) CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop Nlinked glycosylation site. J Gen Virol 87: 607-612.
    • (2006) J Gen Virol , vol.87 , pp. 607-612
    • Clevestig, P.1    Pramanik, L.2    Leitner, T.3    Ehrnst, A.4
  • 42
    • 0026606727 scopus 로고
    • Phenotype-associated sequence variation in the third variable domain of the human immunodeficiency virus type 1 gp120 molecule
    • Fouchier RA, Groenink M, Kootstra NA, Tersmette M, Huisman HG, et al. (1992) Phenotype-associated sequence variation in the third variable domain of the human immunodeficiency virus type 1 gp120 molecule. J Virol 66: 3183-3187.
    • (1992) J Virol , vol.66 , pp. 3183-3187
    • Fouchier, R.A.1    Groenink, M.2    Kootstra, N.A.3    Tersmette, M.4    Huisman, H.G.5
  • 43
    • 0036935266 scopus 로고    scopus 로고
    • The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization
    • DOI 10.1006/viro.2002.1760
    • Polzer S, Dittmar MT, Schmitz H, Schreiber M (2002) The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization. Virology 304: 70-80. (Pubitemid 36062833)
    • (2002) Virology , vol.304 , Issue.1 , pp. 70-80
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Schreiber, M.4
  • 44
    • 0035884899 scopus 로고    scopus 로고
    • Improved success of phenotype prediction of the human immunodeficiency virus type 1 from envelope variable loop 3 sequence using neural networks
    • DOI 10.1006/viro.2001.1087
    • Resch W, Hoffman N, Swanstrom R (2001) Improved success of phenotype prediction of the human immunodeficiency virus type 1 from envelope variable loop 3 sequence using neural networks. Virology 288: 51-62. (Pubitemid 32846473)
    • (2001) Virology , vol.288 , Issue.1 , pp. 51-62
    • Resch, W.1    Hoffman, N.2    Swanstrom, R.3
  • 46
    • 0034523325 scopus 로고    scopus 로고
    • Envelope V3 amino acid sequence predicts HIV-1 phenotype (co-receptor usage and tropism for macrophages) [1]
    • DOI 10.1097/00002030-200012220-00016
    • Briggs DR, Tuttle DL, Sleasman JW, Goodenow MM (2000) Envelope V3 amino acid sequence predicts HIV-1 phenotype (co-receptor usage and tropism for macrophages). AIDS 14: 2937-2939. (Pubitemid 32042758)
    • (2000) AIDS , vol.14 , Issue.18 , pp. 2937-2939
    • Briggs, D.R.1    Tuttle, D.L.2    Sleasman, J.W.3    Goodenow, M.M.4
  • 50
    • 84863788697 scopus 로고    scopus 로고
    • Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers
    • Depetris RS, Julien JP, Khayat R, Lee JH, Pejchal R, et al. (2012) Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers. J Biol Chem 287: 24239-24254.
    • (2012) J Biol Chem , vol.287 , pp. 24239-24254
    • Depetris, R.S.1    Julien, J.P.2    Khayat, R.3    Lee, J.H.4    Pejchal, R.5
  • 53
    • 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 PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393: 648-659. (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
  • 54
    • 84866061123 scopus 로고    scopus 로고
    • Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
    • Mao Y, Wang L, Gu C, Herschhorn A, Xiang SH, et al. (2012) Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer. Nat Struct Mol Biol 19: 893-899.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 893-899
    • Mao, Y.1    Wang, L.2    Gu, C.3    Herschhorn, A.4    Xiang, S.H.5
  • 55
    • 84880161438 scopus 로고    scopus 로고
    • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
    • Kong L, Lee JH, Doores KJ, Murin CD, Julien JP, et al. (2013) Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat Struct Mol Biol 20: 796-803.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 796-803
    • Kong, L.1    Lee, J.H.2    Doores, K.J.3    Murin, C.D.4    Julien, J.P.5
  • 56
    • 80054950510 scopus 로고    scopus 로고
    • Molecular dynamics simulations and drug discovery
    • Durrant JD, McCammon JA (2011) Molecular dynamics simulations and drug discovery. BMC Biol 9: 71.
    • (2011) BMC Biol , vol.9 , pp. 71
    • Durrant, J.D.1    McCammon, J.A.2
  • 57
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • DOI 10.1038/nsb0902-646
    • Karplus M, McCammon JA (2002) Molecular dynamics simulations of biomolecules. Nat Struct Biol 9: 646-652. (Pubitemid 34977295)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 58
    • 78049424266 scopus 로고    scopus 로고
    • Computational glycoscience: Characterizing the spatial and temporal properties of glycans and glycan-protein complexes
    • Woods RJ, Tessier MB (2010) Computational glycoscience: characterizing the spatial and temporal properties of glycans and glycan-protein complexes. Curr Opin Struct Biol 20: 575-583.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 575-583
    • Woods, R.J.1    Tessier, M.B.2
  • 60
    • 84869784812 scopus 로고    scopus 로고
    • Insights into the structure, correlated motions, and electrostatic properties of two HIV-1 gp120 V3 loops
    • Lopez de Victoria A, Tamamis P, Kieslich CA, Morikis D (2012) Insights into the structure, correlated motions, and electrostatic properties of two HIV-1 gp120 V3 loops. PLoS ONE 7: e49925.
    • (2012) PLoS ONE , vol.7
    • Lopez De Victoria, A.1    Tamamis, P.2    Kieslich, C.A.3    Morikis, D.4
  • 62
    • 34648816125 scopus 로고    scopus 로고
    • N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization
    • DOI 10.1128/JVI.01106-07
    • Gray ES, Moore PL, Pantophlet RA, Morris L (2007) N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization. J Virol 81: 10769-10776. (Pubitemid 47463349)
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10769-10776
    • Gray, E.S.1    Moore, P.L.2    Pantophlet, R.A.3    Morris, L.4
  • 63
    • 77952575336 scopus 로고    scopus 로고
    • Expression, glycoform characterization, and antibody-binding of HIV-1 V3 glycopeptide domain fused with human IgG1-Fc
    • Yang Q, Li C, Wei Y, Huang W, Wang L-X (2010) Expression, glycoform characterization, and antibody-binding of HIV-1 V3 glycopeptide domain fused with human IgG1-Fc. Bioconjug Chem 21: 875-883.
    • (2010) Bioconjug Chem , vol.21 , pp. 875-883
    • Yang, Q.1    Li, C.2    Wei, Y.3    Huang, W.4    Wang, L.-X.5
  • 64
    • 40449129088 scopus 로고    scopus 로고
    • The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion
    • Sanders RW, van Anken E, Nabatov AA, Liscaljet IM, Bontjer I, et al. (2008) The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion. Retrovirology 5: 10.
    • (2008) Retrovirology , vol.5 , pp. 10
    • Sanders, R.W.1    Van Anken, E.2    Nabatov, A.A.3    Liscaljet, I.M.4    Bontjer, I.5
  • 65
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders RW, Venturi M, Schiffner L, Kalyanaraman R, Katinger H, et al. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J Virol 76: 7293-7305.
    • (2002) J Virol , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5
  • 66
    • 77954224920 scopus 로고    scopus 로고
    • Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition
    • Raska M, Takahashi K, Czernekova L, Zachova K, Hall S, et al. (2010) Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition. J Biol Chem 285: 20860-20869.
    • (2010) J Biol Chem , vol.285 , pp. 20860-20869
    • Raska, M.1    Takahashi, K.2    Czernekova, L.3    Zachova, K.4    Hall, S.5
  • 67
    • 0032991878 scopus 로고    scopus 로고
    • The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant
    • DOI 10.1016/S0014-5793(99)00740-1, PII S0014579399007401
    • Losman B, Biller M, Olofsson S, Schonning K, Lund OS, et al. (1999) The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant. FEBS Letters 454: 47-52. (Pubitemid 29296923)
    • (1999) FEBS Letters , vol.454 , Issue.1-2 , pp. 47-52
    • Losman, B.1    Biller, M.2    Olofsson, S.3    Schonning, K.4    Lund, O.S.5    Svennerholm, B.6    Hansen, J.-E.S.7    Bolmstedt, A.8
  • 68
    • 35348992649 scopus 로고    scopus 로고
    • High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization
    • DOI 10.1016/j.virol.2007.06.029, PII S0042682207004382
    • Hu Q, Mahmood N, Shattock RJ (2007) High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization. Virology 368: 145-154. (Pubitemid 47599570)
    • (2007) Virology , vol.368 , Issue.1 , pp. 145-154
    • Hu, Q.1    Mahmood, N.2    Shattock, R.J.3
  • 72
    • 84869463517 scopus 로고    scopus 로고
    • Mechanical compressibility of the glycosylphosphatidylinositol (GPI) anchor backbone governed by independent glycosidic linkages
    • Wehle M, Vilotijevic I, Lipowsky R, Seeberger PH, Silva DV, et al. (2012) Mechanical compressibility of the glycosylphosphatidylinositol (GPI) anchor backbone governed by independent glycosidic linkages. J Am Chem Soc 134: 18964-18972.
    • (2012) J Am Chem Soc , vol.134 , pp. 18964-18972
    • Wehle, M.1    Vilotijevic, I.2    Lipowsky, R.3    Seeberger, P.H.4    Silva, D.V.5
  • 73
    • 77955817276 scopus 로고    scopus 로고
    • Equilibrium conformational dynamics in an RNA tetraloop from massively parallel molecular dynamics
    • DePaul AJ, Thompson EJ, Patel SS, Haldeman K, Sorin EJ (2010) Equilibrium conformational dynamics in an RNA tetraloop from massively parallel molecular dynamics. Nucleic Acids Res 38: 4856-4867.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4856-4867
    • DePaul, A.J.1    Thompson, E.J.2    Patel, S.S.3    Haldeman, K.4    Sorin, E.J.5
  • 74
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • DOI 10.1529/biophysj.104.051938
    • Sorin EJ, Pande VS (2005) Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys J 88: 2472-2493. (Pubitemid 40976118)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 75
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen H vdSD, Drunen R (1995) GROMACS: a message-passing parallel molecular dynamics implementation. Comp Phys Comm 91: 43-56.
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.1    VdS, D.2    Drunen, R.3
  • 76
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulations
    • Hess B KC, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulations. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    K, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 79
    • 77951157311 scopus 로고    scopus 로고
    • CCR5 antagonists: Host-targeted antiviral agents for the treatment of HIV infection, 4 years on
    • Westby M, van der Ryst E (2010) CCR5 antagonists: host-targeted antiviral agents for the treatment of HIV infection, 4 years on. Antivir Chem Chemother 20: 179-192.
    • (2010) Antivir Chem Chemother , vol.20 , pp. 179-192
    • Westby, M.1    Van Der Ryst, E.2
  • 80
  • 82
    • 0027438789 scopus 로고
    • Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms
    • DOI 10.1111/j.1432-1033.1993.tb18370.x
    • Joao HC, Dwek RA (1993) Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms. Eur J Biochem 218: 239-244. (Pubitemid 23350379)
    • (1993) European Journal of Biochemistry , vol.218 , Issue.1 , pp. 239-244
    • Joao, H.C.1    Dwek, R.A.2
  • 83
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • Zheng K, Bantog C, Bayer R (2011) The impact of glycosylation on monoclonal antibody conformation and stability. MAbs 3: 568-576.
    • (2011) MAbs , vol.3 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3
  • 84
    • 84873093812 scopus 로고    scopus 로고
    • Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: Observations from molecular dynamics simulations
    • Wang X, Kumar S, Buck PM, Singh SK (2013) Impact of deglycosylation and thermal stress on conformational stability of a full length murine IgG2a monoclonal antibody: observations from molecular dynamics simulations. Proteins 81: 443-460.
    • (2013) Proteins , vol.81 , pp. 443-460
    • Wang, X.1    Kumar, S.2    Buck, P.M.3    Singh, S.K.4
  • 86
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau QJ, Moore JP (1991) Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J Exp Med 174: 407-415.
    • (1991) J Exp Med , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 88
    • 35648983524 scopus 로고    scopus 로고
    • Improved prediction of coreceptor usage and phenotype of HIV-1 based on combined features of V3 loop sequence using random forest
    • Xu S, Huang X, Xu H, Zhang C (2007) Improved prediction of coreceptor usage and phenotype of HIV-1 based on combined features of V3 loop sequence using random forest. J Microbiol 45: 441-446.
    • (2007) J Microbiol , vol.45 , pp. 441-446
    • Xu, S.1    Huang, X.2    Xu, H.3    Zhang, C.4
  • 91
    • 56749176808 scopus 로고    scopus 로고
    • Dynameomics: Large-scale assessment of native protein flexibility
    • Benson NC, Daggett V (2008) Dynameomics: large-scale assessment of native protein flexibility. Protein Sci 17: 2038-2050.
    • (2008) Protein Sci , vol.17 , pp. 2038-2050
    • Benson, N.C.1    Daggett, V.2
  • 94
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen K, Piana S, Palmo K, Maragakis P, Klepeis JL, et al. (2010) Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78: 1950-1958.
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Palmo, K.3    Maragakis, P.4    Klepeis, J.L.5
  • 95
    • 84861367246 scopus 로고    scopus 로고
    • Biomolecular simulation: A computational microscope for molecular biology
    • Dror RO, Dirks RM, Grossman JP, Xu H, Shaw DE (2012) Biomolecular simulation: a computational microscope for molecular biology. Annu Rev Biophys 41: 429-452.
    • (2012) Annu Rev Biophys , vol.41 , pp. 429-452
    • Dror, R.O.1    Dirks, R.M.2    Grossman, J.P.3    Xu, H.4    Shaw, D.E.5
  • 96
    • 84884673669 scopus 로고    scopus 로고
    • Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex
    • Tan Q, Zhu Y, Li J, Chen Z, Han GW, et al. (2013) Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex. Science 341: 1387-1390.
    • (2013) Science , vol.341 , pp. 1387-1390
    • Tan, Q.1    Zhu, Y.2    Li, J.3    Chen, Z.4    Han, G.W.5
  • 97
    • 25144519185 scopus 로고    scopus 로고
    • Identification of two N-linked glycosylation sites within the core of the simian immunodeficiency virus glycoprotein whose removal enhances sensitivity to soluble CD4
    • DOI 10.1128/JVI.79.19.12575-12583.2005
    • Pikora C, Wittish C, Desrosiers RC (2005) Identification of two N-linked glycosylation sites within the core of the simian immunodeficiency virus glycoprotein whose removal enhances sensitivity to soluble CD4. J Virol 79: 12575-12583. (Pubitemid 41346120)
    • (2005) Journal of Virology , vol.79 , Issue.19 , pp. 12575-12583
    • Pikora, C.1    Wittish, C.2    Desrosiers, R.C.3


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