메뉴 건너뛰기
Journal of Virology
Volumn 88, Issue 8, 2014, Pages 4304-4318
Reversible and efficient activation of HIV-1 cell entry by a tyrosine-sulfated peptide dissects endocytic entry and inhibitor mechanisms
Author keywords

[No Author keywords available]
Indexed keywords

CHEMOKINE RECEPTOR CCR5; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; NEUTRALIZING ANTIBODY; PEPTIDE; TYROSINE SULFATED PEPTIDE; UNCLASSIFIED DRUG;
EID: 84896939482     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03447-13     Document Type: Article
Times cited : (12)
References (69)
  • 1
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810. http://dx.doi.org/10.1146/annurev.biochem.70.1.777.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 2
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, Markosyan RM, Hemmati H, Delmedico MK, Lambert DM, Cohen FS. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423. http://dx.doi.org/10.1083/jcb.151.2.413.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 3
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn CA, Decker JM, Sfakianos JN, Zhang Z, O'Brien WA, Ratner L, Shaw GM, Hunter E. 2001. Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J. Virol. 75:8605-8614. http://dx.doi.org/10.1128/JVI.75.18.8605-8614.2001.
    • (2001) J. Virol. , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Zhang, Z.4    O'Brien, W.A.5    Ratner, L.6    Shaw, G.M.7    Hunter, E.8
  • 4
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt EJ, Durnin JP, Kabat D. 2005. Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J. Virol. 79:4347-4356. http://dx.doi.org/10.1128/JVI.79.7.4347-4356.2005.
    • (2005) J. Virol. , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 5
    • 35348955835 scopus 로고    scopus 로고
    • An allosteric rheostat in HIV-1 gp120 reduces CCR5 stoichiometry required for membrane fusion and overcomes diverse entry limitations
    • Platt EJ, Durnin JP, Shinde U, Kabat D. 2007. An allosteric rheostat in HIV-1 gp120 reduces CCR5 stoichiometry required for membrane fusion and overcomes diverse entry limitations. J. Mol. Biol. 374:64-79. http://dx.doi.org/10.1016/j.jmb.2007.09.016.
    • (2007) J. Mol. Biol. , vol.374 , pp. 64-79
    • Platt, E.J.1    Durnin, J.P.2    Shinde, U.3    Kabat, D.4
  • 6
    • 15244353557 scopus 로고    scopus 로고
    • Variants of human immunodeficiency virus type 1 that efficiently use CCR5 lacking the tyrosinesulfated amino terminus have adaptive mutations in gp120, including loss of a functional N-glycan
    • Platt EJ, Shea DM, Rose PP, Kabat D. 2005. Variants of human immunodeficiency virus type 1 that efficiently use CCR5 lacking the tyrosinesulfated amino terminus have adaptive mutations in gp120, including loss of a functional N-glycan. J. Virol. 79:4357-4368. http://dx.doi.org/10.1128/JVI.79.7.4357-4368.2005.
    • (2005) J. Virol. , vol.79 , pp. 4357-4368
    • Platt, E.J.1    Shea, D.M.2    Rose, P.P.3    Kabat, D.4
  • 8
    • 0030053308 scopus 로고    scopus 로고
    • Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1
    • Cao J, Park IW, Cooper A, Sodroski J. 1996. Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1. J. Virol. 70:1340-1354.
    • (1996) J. Virol. , vol.70 , pp. 1340-1354
    • Cao, J.1    Park, I.W.2    Cooper, A.3    Sodroski, J.4
  • 9
    • 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. http://dx.doi.org/10.1126/science.2251501.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 10
    • 0025866185 scopus 로고
    • Conformational changes induced in the humanimmunodeficiency virus envelope glycoprotein by solubleCD4binding
    • Sattentau QJ, Moore JP. 1991. Conformational changes induced in the humanimmunodeficiency virus envelope glycoprotein by solubleCD4binding. J. Exp. Med. 174:407-415. http://dx.doi.org/10.1084/jem.174.2.407.
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 11
    • 33846087827 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus envelope glycoproteinmediated single cell lysis by low-molecular-weight antagonists of viral entry
    • Madani N, Hubicki AM, Perdigoto AL, Springer M, Sodroski J. 2007. Inhibition of human immunodeficiency virus envelope glycoproteinmediated single cell lysis by low-molecular-weight antagonists of viral entry. J. Virol. 81:532-538. http://dx.doi.org/10.1128/JVI.01079-06.
    • (2007) J. Virol. , vol.81 , pp. 532-538
    • Madani, N.1    Hubicki, A.M.2    Perdigoto, A.L.3    Springer, M.4    Sodroski, J.5
  • 12
    • 77649171305 scopus 로고    scopus 로고
    • Rapid dissociation of HIV-1 from cultured cells severely limits infectivity assays, causes the inactivation ascribed to entry inhibitors, and masks the inherently high level of infectivity of virions
    • Platt EJ, Kozak SL, Durnin JP, Hope TJ, Kabat D. 2010. Rapid dissociation of HIV-1 from cultured cells severely limits infectivity assays, causes the inactivation ascribed to entry inhibitors, and masks the inherently high level of infectivity of virions. J. Virol. 84:3106-3110. http://dx.doi.org/10.1128/JVI.01958-09.
    • (2010) J. Virol. , vol.84 , pp. 3106-3110
    • Platt, E.J.1    Kozak, S.L.2    Durnin, J.P.3    Hope, T.J.4    Kabat, D.5
  • 13
    • 16244380203 scopus 로고    scopus 로고
    • Enfuvirtide resistance mutations: impact onhumanimmunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization
    • Reeves JD, Lee FH, Miamidian JL, Jabara CB, Juntilla MM, Doms RW. 2005. Enfuvirtide resistance mutations: impact onhumanimmunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization. J. Virol. 79:4991-4999. http://dx.doi.org/10.1128/JVI.79.8.4991-4999.2005.
    • (2005) J. Virol. , vol.79 , pp. 4991-4999
    • Reeves, J.D.1    Lee, F.H.2    Miamidian, J.L.3    Jabara, C.B.4    Juntilla, M.M.5    Doms, R.W.6
  • 17
    • 0034721834 scopus 로고    scopus 로고
    • A tyrosine-sulfated peptide based on the N terminus of CCR5 interacts with a CD4-enhanced epitope of the HIV-1 gp120 envelope glycoprotein and inhibits HIV-1 entry
    • Farzan M, Vasilieva N, Schnitzler CE, Chung S, Robinson J, Gerard NP, Gerard C, Choe H, Sodroski J. 2000. A tyrosine-sulfated peptide based on the N terminus of CCR5 interacts with a CD4-enhanced epitope of the HIV-1 gp120 envelope glycoprotein and inhibits HIV-1 entry. J. Biol. Chem. 275:33516-33521. http://dx.doi.org/10.1074/jbc. M007228200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33516-33521
    • Farzan, M.1    Vasilieva, N.2    Schnitzler, C.E.3    Chung, S.4    Robinson, J.5    Gerard, N.P.6    Gerard, C.7    Choe, H.8    Sodroski, J.9
  • 19
    • 0035202075 scopus 로고    scopus 로고
    • Adaptive mutations in the V3 loop of gp120 enhance fusogenicity of human immunodeficiency virus type 1 and enable use of a CCR5 coreceptor that lacks the aminoterminal sulfated region
    • Platt EJ, Kuhmann SE, Rose PP, Kabat D. 2001. Adaptive mutations in the V3 loop of gp120 enhance fusogenicity of human immunodeficiency virus type 1 and enable use of a CCR5 coreceptor that lacks the aminoterminal sulfated region. J. Virol. 75:12266-12278. http://dx.doi.org/10.1128/JVI.75.24.12266-12278.2001.
    • (2001) J. Virol. , vol.75 , pp. 12266-12278
    • Platt, E.J.1    Kuhmann, S.E.2    Rose, P.P.3    Kabat, D.4
  • 22
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt EJ, Wehrly K, Kuhmann SE, Chesebro B, Kabat D. 1998. Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J. Virol. 72: 2855-2864.
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 23
    • 0028293288 scopus 로고
    • Differences in CD4 dependence for infectivity of laboratory-adapted and primary patient isolates of human immunodeficiency virus type 1
    • Kabat D, Kozak SL, Wehrly K, Chesebro B. 1994. Differences in CD4 dependence for infectivity of laboratory-adapted and primary patient isolates of human immunodeficiency virus type 1. J. Virol. 68:2570-2577.
    • (1994) J. Virol. , vol.68 , pp. 2570-2577
    • Kabat, D.1    Kozak, S.L.2    Wehrly, K.3    Chesebro, B.4
  • 24
    • 0028839609 scopus 로고
    • Hightiter packaging cells producing recombinant retroviruses resistant to human serum
    • Cosset FL, Takeuchi Y, Battini JL, Weiss RA, Collins MK. 1995. Hightiter packaging cells producing recombinant retroviruses resistant to human serum. J. Virol. 69:7430-7436.
    • (1995) J. Virol. , vol.69 , pp. 7430-7436
    • Cosset, F.L.1    Takeuchi, Y.2    Battini, J.L.3    Weiss, R.A.4    Collins, M.K.5
  • 25
    • 33746927623 scopus 로고    scopus 로고
    • Vaccination of mice with replication-defective human immunodeficiency virus induces cellular and humoral immunity and protects against vaccinia virus-gag challenge
    • Baliga CS, van Maanen M, Chastain M, Sutton RE. 2006. Vaccination of mice with replication-defective human immunodeficiency virus induces cellular and humoral immunity and protects against vaccinia virus-gag challenge. Mol. Ther. 14:432-441. http://dx.doi.org/10.1016/j.ymthe.2006.02.021.
    • (2006) Mol. Ther. , vol.14 , pp. 432-441
    • Baliga, C.S.1    van Maanen, M.2    Chastain, M.3    Sutton, R.E.4
  • 26
    • 0033941573 scopus 로고    scopus 로고
    • Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • Kuhmann SE, Platt EJ, Kozak SL, Kabat D. 2000. Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1. J. Virol. 74:7005-7015. http://dx.doi.org/10.1128/JVI.74.15.7005-7015.2000.
    • (2000) J. Virol. , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 27
    • 0030812844 scopus 로고    scopus 로고
    • Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses
    • Kuhmann SE, Platt EJ, Kozak SL, Kabat D. 1997. Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses. J. Virol. 71:8642-8656.
    • (1997) J. Virol. , vol.71 , pp. 8642-8656
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 29
    • 0025005828 scopus 로고
    • Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity
    • Page KA, Landau NR, Littman DR. 1990. Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity. J. Virol. 64:5270-5276.
    • (1990) J. Virol. , vol.64 , pp. 5270-5276
    • Page, K.A.1    Landau, N.R.2    Littman, D.R.3
  • 30
    • 33749410635 scopus 로고    scopus 로고
    • A tyrosinesulfated peptide derived from the heavy-chain CDR3 region of an HIV-1-neutralizing antibody binds gp120 and inhibits HIV-1 infection
    • Dorfman T, Moore MJ, Guth AC, Choe H, Farzan M. 2006. A tyrosinesulfated peptide derived from the heavy-chain CDR3 region of an HIV-1-neutralizing antibody binds gp120 and inhibits HIV-1 infection. J. Biol. Chem. 281:28529-28535. http://dx.doi.org/10.1074/jbc. M602732200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28529-28535
    • Dorfman, T.1    Moore, M.J.2    Guth, A.C.3    Choe, H.4    Farzan, M.5
  • 32
    • 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, Moore JP. 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. http://dx.doi.org/10.1016/j.pep.2006.02.017.
    • (2006) Protein Expr. Purif. , vol.48 , pp. 61-68
    • Kirschner, M.1    Monrose, V.2    Paluch, M.3    Techodamrongsin, N.4    Rethwilm, A.5    Moore, J.P.6
  • 33
    • 0023761449 scopus 로고
    • Development of a sensitive quantitative focal assay for human immunodeficiency virus infectivity
    • Chesebro B, Wehrly K. 1988. Development of a sensitive quantitative focal assay for human immunodeficiency virus infectivity. J. Virol. 62: 3779-3788.
    • (1988) J. Virol. , vol.62 , pp. 3779-3788
    • Chesebro, B.1    Wehrly, K.2
  • 34
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-celltropic isolates: definition of critical amino acids involved in cell tropism
    • Chesebro B, Wehrly K, Nishio J, Perryman S. 1992. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-celltropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 37
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang LH, Rothberg KG, Anderson RG. 1993. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Cell Biol. 123:1107-1117. http://dx.doi.org/10.1083/jcb.123.5.1107.
    • (1993) J. Cell Biol. , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 38
    • 84861208332 scopus 로고    scopus 로고
    • Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry
    • Platt EJ, Gomes MM, Kabat D. 2012. Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry. Proc. Natl. Acad. Sci. U. S. A. 109:7829-7834. http://dx.doi.org/10.1073/pnas.1109728109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 7829-7834
    • Platt, E.J.1    Gomes, M.M.2    Kabat, D.3
  • 40
    • 70349677167 scopus 로고    scopus 로고
    • Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation
    • Miyauchi K, Kozlov MM, Melikyan GB. 2009. Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation. PLoS Pathog. 5:e1000585. http://dx.doi.org/10.1371/journal.ppat.1000585.
    • (2009) PLoS Pathog. , vol.5
    • Miyauchi, K.1    Kozlov, M.M.2    Melikyan, G.B.3
  • 42
    • 77949401834 scopus 로고    scopus 로고
    • A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer
    • Xiang SH, Finzi A, Pacheco B, Alexander K, Yuan W, Rizzuto C, Huang CC, Kwong PD, Sodroski J. 2010. A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer. J. Virol. 84:3147-3161. http://dx.doi.org/10.1128/JVI.02587-09.
    • (2010) J. Virol. , vol.84 , pp. 3147-3161
    • Xiang, S.H.1    Finzi, A.2    Pacheco, B.3    Alexander, K.4    Yuan, W.5    Rizzuto, C.6    Huang, C.C.7    Kwong, P.D.8    Sodroski, J.9
  • 46
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB. 2009. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137:433-444. http://dx.doi.org/10.1016/j.cell.2009.02.046.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 47
    • 84869106867 scopus 로고    scopus 로고
    • Enhanced recognition and neutralization of HIV-1 by antibodyderived CCR5-mimetic peptide variants
    • Chiang JJ, Gardner MR, Quinlan BD, Dorfman T, Choe H, Farzan M. 2012. Enhanced recognition and neutralization of HIV-1 by antibodyderived CCR5-mimetic peptide variants. J. Virol. 86:12417-12421. http://dx.doi.org/10.1128/JVI.00967-12.
    • (2012) J. Virol. , vol.86 , pp. 12417-12421
    • Chiang, J.J.1    Gardner, M.R.2    Quinlan, B.D.3    Dorfman, T.4    Choe, H.5    Farzan, M.6
  • 48
    • 0036499181 scopus 로고    scopus 로고
    • Follicular dendritic cells and the persistence of HIV infectivity: the role of antibodies and Fcgamma receptors
    • Smith-Franklin BA, Keele BF, Tew JG, Gartner S, Szakal AK, Estes JD, Thacker TC, Burton GF. 2002. Follicular dendritic cells and the persistence of HIV infectivity: the role of antibodies and Fcgamma receptors. J. Immunol. 168:2408-2414. http://www.jimmunol.org/content/168/5/2408.
    • (2002) J. Immunol. , vol.168 , pp. 2408-2414
    • Smith-Franklin, B.A.1    Keele, B.F.2    Tew, J.G.3    Gartner, S.4    Szakal, A.K.5    Estes, J.D.6    Thacker, T.C.7    Burton, G.F.8
  • 49
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta RA, Wild CT, Weng Y, Weiss CD. 1998. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5:276-279. http://dx.doi.org/10.1038/nsb0498-276.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 50
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • Daecke J, Fackler OT, Dittmar MT, Krausslich HG. 2005. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J. Virol. 79:1581-1594. http://dx.doi.org/10.1128/JVI.79.3.1581-1594.2005.
    • (2005) J. Virol. , vol.79 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Krausslich, H.G.4
  • 51
    • 0036827862 scopus 로고    scopus 로고
    • Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus
    • Fredericksen BL, Wei BL, Yao J, Luo T, Garcia JV. 2002. Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus. J. Virol. 76:11440-11446. http://dx.doi.org/10.1128/JVI.76.22.11440-11446.2002.
    • (2002) J. Virol. , vol.76 , pp. 11440-11446
    • Fredericksen, B.L.1    Wei, B.L.2    Yao, J.3    Luo, T.4    Garcia, J.V.5
  • 52
    • 0347003570 scopus 로고    scopus 로고
    • Compensatory link between fusion and endocytosis of human immunodeficiency virus type 1 in human CD4 T lymphocytes
    • Schaeffer E, Soros VB, Greene WC. 2004. Compensatory link between fusion and endocytosis of human immunodeficiency virus type 1 in human CD4 T lymphocytes. J. Virol. 78:1375-1383. http://dx.doi.org/10.1128/JVI.78.3.1375-1383.2004.
    • (2004) J. Virol. , vol.78 , pp. 1375-1383
    • Schaeffer, E.1    Soros, V.B.2    Greene, W.C.3
  • 53
  • 54
    • 80052248915 scopus 로고    scopus 로고
    • Dynamin: functional design of a membrane fission catalyst
    • Schmid SL, Frolov VA. 2011. Dynamin: functional design of a membrane fission catalyst. Annu. Rev. Cell Dev. Biol. 27:79-105. http://dx.doi.org/10.1146/annurev-cellbio-100109-104016.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 79-105
    • Schmid, S.L.1    Frolov, V.A.2
  • 55
    • 84857359495 scopus 로고    scopus 로고
    • The intracellular trafficking pathway of transferrin
    • Mayle KM, Le AM, Kamei DT. 2012. The intracellular trafficking pathway of transferrin. Biochim. Biophys. Acta 1820:264-281. http://dx.doi.org/10.1016/j.bbagen.2011.09.009.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 264-281
    • Mayle, K.M.1    Le, A.M.2    Kamei, D.T.3
  • 56
    • 78649316355 scopus 로고    scopus 로고
    • Endocytosis of HIV: anything goes
    • Permanyer M, Ballana E, Este JA. 2010. Endocytosis of HIV: anything goes. Trends Microbiol. 18:543-551. http://dx.doi.org/10.1016/j.tim.2010.09.003.
    • (2010) Trends Microbiol. , vol.18 , pp. 543-551
    • Permanyer, M.1    Ballana, E.2    Este, J.A.3
  • 57
    • 80053959566 scopus 로고    scopus 로고
    • Spinoculation triggers dynamic actin and cofilin activity that facilitates HIV-1 infection of transformed and resting CD4 T cells
    • Guo J, Wang W, Yu D, Wu Y. 2011. Spinoculation triggers dynamic actin and cofilin activity that facilitates HIV-1 infection of transformed and resting CD4 T cells. J. Virol. 85:9824-9833. http://dx.doi.org/10.1128/JVI.05170-11.
    • (2011) J. Virol. , vol.85 , pp. 9824-9833
    • Guo, J.1    Wang, W.2    Yu, D.3    Wu, Y.4
  • 59
    • 77952692673 scopus 로고    scopus 로고
    • Virus entry by endocytosis
    • Mercer J, Schelhaas M, Helenius A. 2010. Virus entry by endocytosis. Annu. Rev. Biochem. 79:803-833. http://dx.doi.org/10.1146/annurev-biochem-060208-104626.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 803-833
    • Mercer, J.1    Schelhaas, M.2    Helenius, A.3
  • 60
    • 2142759185 scopus 로고    scopus 로고
    • Cytosolic Gag p24 as an index of productive entry of human immunodeficiency virus type 1
    • Marechal V, Clavel F, Heard JM, Schwartz O. 1998. Cytosolic Gag p24 as an index of productive entry of human immunodeficiency virus type 1. J. Virol. 72:2208-2212.
    • (1998) J. Virol. , vol.72 , pp. 2208-2212
    • Marechal, V.1    Clavel, F.2    Heard, J.M.3    Schwartz, O.4
  • 61
    • 70350319097 scopus 로고    scopus 로고
    • Receptor binding and low pH coacti-vate oncogenic retrovirus envelope-mediated fusion
    • Cote M, Zheng YM, Liu SL. 2009. Receptor binding and low pH coacti-vate oncogenic retrovirus envelope-mediated fusion. J. Virol. 83:11447-11455. http://dx.doi.org/10.1128/JVI.00748-09.
    • (2009) J. Virol. , vol.83 , pp. 11447-11455
    • Cote, M.1    Zheng, Y.M.2    Liu, S.L.3
  • 62
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W, Boerger AL, Narayan S, Cunningham JM, Young JA. 2000. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103:679-689. http://dx.doi.org/10.1016/S0092-8674(00)00170-7.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 63
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne CB, Bergelson JM. 2006. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 124: 119-131. http://dx.doi.org/10.1016/j.cell.2005.10.035.
    • (2006) Cell , vol.124 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 64
    • 38549086984 scopus 로고    scopus 로고
    • Hepatitis C virus entry into host cells
    • Helle F, Dubuisson J. 2008. Hepatitis C virus entry into host cells. Cell. Mol. Life Sci. 65:100-112. http://dx.doi.org/10.1007/s00018-007-7291-8.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 100-112
    • Helle, F.1    Dubuisson, J.2
  • 65
    • 0034663422 scopus 로고    scopus 로고
    • Cell receptors involved in adenovirus entry
    • Nemerow GR. 2000. Cell receptors involved in adenovirus entry. Virology 274:1-4. http://dx.doi.org/10.1006/viro.2000.0468.
    • (2000) Virology , vol.274 , pp. 1-4
    • Nemerow, G.R.1
  • 66
    • 0001373810 scopus 로고
    • Virus particle adsorption. III. Adsorption of viruses by cell monolayers and effects of some variables on adsorption
    • Allison AC, Valentine RC. 1960. Virus particle adsorption. III. Adsorption of viruses by cell monolayers and effects of some variables on adsorption. Biochim. Biophys. Acta 40:400-410.
    • (1960) Biochim. Biophys. Acta , vol.40 , pp. 400-410
    • Allison, A.C.1    Valentine, R.C.2
  • 69
    • 79960411519 scopus 로고    scopus 로고
    • A tyrosine-sulfated CCR5-mimetic peptide promotes conformational transitions in the HIV-1 envelope glycoprotein
    • Kwong JA, Dorfman T, Quinlan BD, Chiang JJ, Ahmed AA, Choe H, Farzan M. 2011. A tyrosine-sulfated CCR5-mimetic peptide promotes conformational transitions in the HIV-1 envelope glycoprotein. J. Virol. 85:7563-7571. http://dx.doi.org/10.1128/JVI.00630-11.
    • (2011) J. Virol. , vol.85 , pp. 7563-7571
    • Kwong, J.A.1    Dorfman, T.2    Quinlan, B.D.3    Chiang, J.J.4    Ahmed, A.A.5    Choe, H.6    Farzan, M.7

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.