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Volumn 82, Issue 3, 2008, Pages 1389-1398

Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; VIRUS RNA; ZINC FINGER PROTEIN;

EID: 38349174466     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01912-07     Document Type: Article
Times cited : (93)

References (55)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola, M. A., B. Strack, and H. G. Gottlinger. 2000. Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74:5395-5402.
    • (2000) J. Virol , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 2
    • 0034636984 scopus 로고    scopus 로고
    • Amarasinghe, G. K., R. N. De Guzman, R. B. Turner, K. J. Chancellor, Z. R. Wu, and M. F. Summers. 2000. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the ψ-RNA packaging signal. Implications for genome recognition. fsJ. Mol. Biol. 301:491-511.
    • Amarasinghe, G. K., R. N. De Guzman, R. B. Turner, K. J. Chancellor, Z. R. Wu, and M. F. Summers. 2000. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the ψ-RNA packaging signal. Implications for genome recognition. fsJ. Mol. Biol. 301:491-511.
  • 3
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst, M. 2005. A protein's final ESCRT. Traffic 6:2-9.
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 4
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., B. Wendland, E. J. Estepa, and S. D. Emr. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 7
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly
    • Borsetti, A., A. Ohagen, and H. G. Gottlinger. 1998. The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly. J. Virol. 72:9313-9317.
    • (1998) J. Virol , vol.72 , pp. 9313-9317
    • Borsetti, A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 8
    • 0031684590 scopus 로고    scopus 로고
    • Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue
    • Bowzard, J. B., R. P. Bennett, N. K. Krishna, S. M. Ernst, A. Rein, and J. W. Wills. 1998. Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue. J. Virol. 72:9034-9044.
    • (1998) J. Virol , vol.72 , pp. 9034-9044
    • Bowzard, J.B.1    Bennett, R.P.2    Krishna, N.K.3    Ernst, S.M.4    Rein, A.5    Wills, J.W.6
  • 9
    • 0032874018 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein
    • Burniston, M. T., A. Cimarelli, J. Colgan, S. P. Curtis, and J. Luban. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J. Virol. 73:8527-8540.
    • (1999) J. Virol , vol.73 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 10
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • Carlton, J. G., and J. Martin-Serrano. 2007. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316:1908-1912.
    • (2007) Science , vol.316 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 11
    • 28844506638 scopus 로고    scopus 로고
    • Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding
    • Chen, C., O. Vincent, J. Jin, O. A. Weisz, and R. C. Montelaro. 2005. Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding. J. Biol. Chem. 280:40474-40480.
    • (2005) J. Biol. Chem , vol.280 , pp. 40474-40480
    • Chen, C.1    Vincent, O.2    Jin, J.3    Weisz, O.A.4    Montelaro, R.C.5
  • 12
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Perryman. 1992. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic 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
  • 13
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057.
    • (2000) J. Virol , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 14
    • 0032506295 scopus 로고    scopus 로고
    • The role of nucleocapsid of HIV-1 in virus assembly
    • Dawson, L., and X. F. Yu. 1998. The role of nucleocapsid of HIV-1 in virus assembly. Virology 251:141-157.
    • (1998) Virology , vol.251 , pp. 141-157
    • Dawson, L.1    Yu, X.F.2
  • 15
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element
    • De Guzman, R. N., Z. R. Wu, C. C. Stalling, L. Pappalardo, P. N. Borer, and M. F. Summers. 1998. Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element. Science 279:384-388.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 16
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov, D. G., J. M. Orenstein, and E. O. Freed. 2002. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J. Virol. 76:105-117.
    • (2002) J. Virol , vol.76 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 18
    • 0027220120 scopus 로고
    • Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein
    • Dorfman, T., J. Luban, S. P. Goff, W. A. Haseltine, and H. G. Gottlinger. 1993. Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 67:6159-6169.
    • (1993) J. Virol , vol.67 , pp. 6159-6169
    • Dorfman, T.1    Luban, J.2    Goff, S.P.3    Haseltine, W.A.4    Gottlinger, H.G.5
  • 19
    • 0027979135 scopus 로고
    • Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
    • Dorfman, T., F. Mammano, W. A. Haseltine, and H. G. Gottlinger. 1994. Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 68:1689-1696.
    • (1994) J. Virol , vol.68 , pp. 1689-1696
    • Dorfman, T.1    Mammano, F.2    Haseltine, W.A.3    Gottlinger, H.G.4
  • 20
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • Fisher, R. D., H. Y. Chung, Q. Zhai, H. Robinson, W. I. Sundquist, and C. P. Hill. 2007. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128:841-852.
    • (2007) Cell , vol.128 , pp. 841-852
    • Fisher, R.D.1    Chung, H.Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 22
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger, H. G., T. Dorfman, J. G. Sodroski, and W. A. Haseltine. 1991. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc. Natl. Acad. Sci. USA 88:3195-3199.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 23
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg, J., and H. Stenmark. 2004. The biogenesis of multivesicular endosomes. Nat. Rev. Mol. Cell Biol. 5:317-323.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 24
    • 0028971135 scopus 로고
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69:6810-6818.
    • (1995) J. Virol , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 25
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H., and S. D. Emr. 2006. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35:277-298.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 26
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J., M. Babst, and S. D. Emr. 2001. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106:145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 27
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., G. Odorizzi, and S. D. Emr. 2002. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3:893-905.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 28
    • 33645027316 scopus 로고    scopus 로고
    • Deletion of a Cys-His motif from the alpharetrovirus nucleocapsid domain reveals late domain mutant-like budding defects
    • Lee, E. G., and M. L. Linial. 2006. Deletion of a Cys-His motif from the alpharetrovirus nucleocapsid domain reveals late domain mutant-like budding defects. Virology 347:226-233.
    • (2006) Virology , vol.347 , pp. 226-233
    • Lee, E.G.1    Linial, M.L.2
  • 30
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano, J., A. Yarovoy, D. Perez-Caballero, and P. D. Bieniasz. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 31
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 32
    • 0034035072 scopus 로고    scopus 로고
    • The double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: Evidence for a role in genomic RNA encapsidation
    • Mouland, A. J., J. Mercier, M. Luo, L. Bernier, L. DesGroseillers, and E. A. Cohen. 2000. The double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: evidence for a role in genomic RNA encapsidation. J. Virol. 74:5441-5451.
    • (2000) J. Virol , vol.74 , pp. 5441-5451
    • Mouland, A.J.1    Mercier, J.2    Luo, M.3    Bernier, L.4    DesGroseillers, L.5    Cohen, E.A.6
  • 33
    • 33947544434 scopus 로고    scopus 로고
    • An Alix fragment potently inhibits HIV-1 budding: Characterization of binding to retroviral YPXL late domains
    • Munshi, U. M., J. Kim, K. Nagashima, J. H. Hurley, and E. O. Freed. 2007. An Alix fragment potently inhibits HIV-1 budding: characterization of binding to retroviral YPXL late domains. J. Biol. Chem. 282:3847-3855.
    • (2007) J. Biol. Chem , vol.282 , pp. 3847-3855
    • Munshi, U.M.1    Kim, J.2    Nagashima, K.3    Hurley, J.H.4    Freed, E.O.5
  • 36
    • 33748302008 scopus 로고    scopus 로고
    • The multiple personalities of Alix
    • Odorizzi, G. 2006. The multiple personalities of Alix. J. Cell Sci. 119:3025-3032.
    • (2006) J. Cell Sci , vol.119 , pp. 3025-3032
    • Odorizzi, G.1
  • 37
    • 27644522295 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Gag with membrane does not require highly basic sequences in the nucleocapsid: Use of a novel Gag multimerization assay
    • Ono, A., A. A. Waheed, A. Joshi, and E. O. Freed. 2005. Association of human immunodeficiency virus type 1 Gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assay. J. Virol. 79:14131-14140.
    • (2005) J. Virol , vol.79 , pp. 14131-14140
    • Ono, A.1    Waheed, A.A.2    Joshi, A.3    Freed, E.O.4
  • 38
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott, D. E., L. V. Coren, E. N. Chertova, T. D. Gagliardi, K. Nagashima, R. C. Sowder II, D. T. Poon, and R. J. Gorelick. 2003. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol. 77:5547-5556.
    • (2003) J. Virol , vol.77 , pp. 5547-5556
    • Ott, D.E.1    Coren, L.V.2    Chertova, E.N.3    Gagliardi, T.D.4    Nagashima, K.5    Sowder II, R.C.6    Poon, D.T.7    Gorelick, R.J.8
  • 40
    • 4143061388 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on Gag precursor-membrane interactions
    • Perez-Caballero, D., T. Hatziioannou, J. Martin-Serrano, and P. D. Bieniasz. 2004. Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on Gag precursor-membrane interactions. J. Virol. 78:9560-9563.
    • (2004) J. Virol , vol.78 , pp. 9560-9563
    • Perez-Caballero, D.1    Hatziioannou, T.2    Martin-Serrano, J.3    Bieniasz, P.D.4
  • 41
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer, B. A., L. J. Parent, J. W. Wills, and R. C. Montelaro. 1997. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71:6541-6546.
    • (1997) J. Virol , vol.71 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 43
    • 34447527768 scopus 로고    scopus 로고
    • Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain
    • Shim, S., L. A. Kimpler, and P. I. Hanson. 2007. Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 8:1068-1079.
    • (2007) Traffic , vol.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 44
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., A. Calistri, S. Craig, E. Popova, and H. G. Gottlinger. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 45
    • 0036094492 scopus 로고    scopus 로고
    • Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis
    • Strack, B., A. Calistri, and H. G. Gottlinger. 2002. Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis. J. Virol. 76:5472-5479.
    • (2002) J. Virol , vol.76 , pp. 5472-5479
    • Strack, B.1    Calistri, A.2    Gottlinger, H.G.3
  • 46
    • 34249943479 scopus 로고    scopus 로고
    • Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site
    • Usami, Y., S. Popov, and H. G. Gottlinger. 2007. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J. Virol. 81:6614-6622.
    • (2007) J. Virol , vol.81 , pp. 6614-6622
    • Usami, Y.1    Popov, S.2    Gottlinger, H.G.3
  • 49
    • 0028070639 scopus 로고
    • An assembly domain of the Rous sarcoma virus Gag protein required late in budding
    • Wills, J. W., C. E. Cameron, C. B. Wilson, Y. Xiang, R. P. Bennett, and J. Leis. 1994. An assembly domain of the Rous sarcoma virus Gag protein required late in budding. J. Virol. 68:6605-6618.
    • (1994) J. Virol , vol.68 , pp. 6605-6618
    • Wills, J.W.1    Cameron, C.E.2    Wilson, C.B.3    Xiang, Y.4    Bennett, R.P.5    Leis, J.6
  • 50
    • 0031968983 scopus 로고    scopus 로고
    • A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release
    • Yasuda, J., and E. Hunter. 1998. A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release. J. Virol. 72:4095-4103.
    • (1998) J. Virol , vol.72 , pp. 4095-4103
    • Yasuda, J.1    Hunter, E.2
  • 51
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan, B., S. Campbell, E. Bacharach, A. Rein, and S. P. Goff. 2000. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74:7250-7260.
    • (2000) J. Virol , vol.74 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 52
    • 0344035661 scopus 로고    scopus 로고
    • Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle
    • Yuan, B., X. Li, and S. P. Goff. 1999. Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle. EMBO J. 18:4700-4710.
    • (1999) EMBO J , vol.18 , pp. 4700-4710
    • Yuan, B.1    Li, X.2    Goff, S.P.3
  • 54
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou, V., D. Perez-Caballero, H. Gottlinger, and P. D. Bieniasz. 2004. APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J. Virol. 78:12058-12061.
    • (2004) J. Virol , vol.78 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Gottlinger, H.3    Bieniasz, P.D.4
  • 55
    • 0030795040 scopus 로고    scopus 로고
    • Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation
    • Zhang, Y., and E. Barklis. 1997. Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation. J. Virol. 71:6765-6776.
    • (1997) J. Virol , vol.71 , pp. 6765-6776
    • Zhang, Y.1    Barklis, E.2


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