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Volumn 73, Issue 4, 1999, Pages 2901-2908

Interaction of the human immunedeficiency virus type 1 nucleocapsid with actin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CD4 ANTIGEN; F ACTIN; MUTANT PROTEIN; ZINC FINGER PROTEIN; GAG PROTEIN;

EID: 0032587326     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.4.2901-2908.1999     Document Type: Article
Times cited : (118)

References (70)
  • 1
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • Aldovini, A., and R. A. Young. 1990. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J. Virol. 64:1920-1926.
    • (1990) J. Virol. , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 2
    • 0028057881 scopus 로고
    • Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription ci the retroviral genome
    • Allain, B, M. Lapadat-Tapolsky, C. Berlioz, and J. L. Darlix. 1994. Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription ci the retroviral genome. EMBO J. 13:973-981.
    • (1994) EMBO J. , vol.13 , pp. 973-981
    • Allain, B.1    Lapadat-Tapolsky, M.2    Berlioz, C.3    Darlix, J.L.4
  • 3
    • 0031968819 scopus 로고    scopus 로고
    • The roles of Pol and Env in the assembly pathway of human foamy virus
    • Baldwin, D. N., and M. L. Linial. 1998. The roles of Pol and Env in the assembly pathway of human foamy virus, J. Virol. 72:3658-3665.
    • (1998) J. Virol. , vol.72 , pp. 3658-3665
    • Baldwin, D.N.1    Linial, M.L.2
  • 4
    • 0027336170 scopus 로고
    • Analysis of the interactions of HIV1 replication primer tRNA(Lys.3) with nucleocapsid protein and reverse transcriptase
    • Barat, C., O. Schatz, S. Le Grice, and J. L. Darlix. 1993. Analysis of the interactions of HIV1 replication primer tRNA(Lys.3) with nucleocapsid protein and reverse transcriptase. J. Mol. Biol. 231:185-190.
    • (1993) J. Mol. Biol. , vol.231 , pp. 185-190
    • Barat, C.1    Schatz, O.2    Le Grice, S.3    Darlix, J.L.4
  • 5
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Bennett, R. P., T. D. Nelle, and J. W. Wills. 1993. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J. Virol. 67:6487-6498.
    • (1993) J. Virol. , vol.67 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 6
    • 1842300493 scopus 로고    scopus 로고
    • Mutations in the N-terminal domain of human immunodeficiency virus type 1 nucleocapsid protein affect virion core structure and proviral DNA synthesis
    • Berthoux, L., C. Pechoux, M. Ottmann, G. Morel, and J. L. Darlix. 1997. Mutations in the N-terminal domain of human immunodeficiency virus type 1 nucleocapsid protein affect virion core structure and proviral DNA synthesis. J. Virol. 71:6973-6981.
    • (1997) J. Virol. , vol.71 , pp. 6973-6981
    • Berthoux, L.1    Pechoux, C.2    Ottmann, M.3    Morel, G.4    Darlix, J.L.5
  • 7
    • 0031684590 scopus 로고    scopus 로고
    • Importance of basic residues in nucleocapsid sequence for retrovirus Gag assembly and complementation rescue
    • Bowzard, J. B., R. B. Bennett, N. K. Krishna, S. M. Ernst, A. Rein, and J. W. Wills. 1998. Importance of basic residues in 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.B.2    Krishna, N.K.3    Ernst, S.M.4    Rein, A.5    Wills, J.W.6
  • 8
    • 0025176624 scopus 로고
    • Myristoylation-dependem replication and assembly of human immunodeficiency virus 1
    • Bryant, M., and L. Ratner. 1990. Myristoylation-dependem replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. USA 87: 523-527.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 9
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • Burtnick, L. D., E. K. Koepf, J. Grimes, E. Y. Jones, D. I. Stuart, P. J. McLaughlin, and R. C. Robinson. 1997. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell 90: 661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 10
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell, S., and V. M. Vogt. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69:6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 11
    • 0027363240 scopus 로고
    • Penetration of Autographa californica nuclear polyhedrosis virus nucleocapsids into IPLB Sf 21 cells induces actin cable formation
    • Charlton, C. A., and L. E. Volkman. 1993. Penetration of Autographa californica nuclear polyhedrosis virus nucleocapsids into IPLB Sf 21 cells induces actin cable formation. Virology 197:245-254.
    • (1993) Virology , vol.197 , pp. 245-254
    • Charlton, C.A.1    Volkman, L.E.2
  • 12
    • 0025043509 scopus 로고
    • A mutant of human immunodeficiency virus with reduced RNA packaging and abnormal particle morphology
    • Clavel, F., and J. M. Orenstein. 1990. A mutant of human immunodeficiency virus with reduced RNA packaging and abnormal particle morphology. J. Virol. 64:5230-5234.
    • (1990) J. Virol. , vol.64 , pp. 5230-5234
    • Clavel, F.1    Orenstein, J.M.2
  • 13
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 14
    • 0025598002 scopus 로고
    • Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1
    • Darlix, J. L., C. Gabus, M. T. Nugeyre, F. Clavel, and F. Barre-Sinoussi. 1990. Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1. J. Mol. Biol. 216:689-699.
    • (1990) J. Mol. Biol. , vol.216 , pp. 689-699
    • Darlix, J.L.1    Gabus, C.2    Nugeyre, M.T.3    Clavel, F.4    Barre-Sinoussi, F.5
  • 15
    • 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
  • 16
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein hound to the SL3 psi-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 hound to the SL3 psi-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
  • 17
    • 0026628854 scopus 로고
    • Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers
    • De Rocquigny, H., C. Gabus, A. Vincent, M. C. Fournie-Zaluski, B. Roques, and J. L. Darlix. 1992. Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers. Proc. Natl. Acad. Sci. USA 88:6472-6476.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6472-6476
    • De Rocquigny, H.1    Gabus, C.2    Vincent, A.3    Fournie-Zaluski, M.C.4    Roques, B.5    Darlix, J.L.6
  • 18
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
    • Doering, D. S., and P. Matsudaira. 1996. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35:12677-12685.
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.2
  • 19
    • 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
  • 20
    • 0027177935 scopus 로고
    • A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum
    • Facke, M., A. Janetzko, R. L. Shoeman, and H. G. Krausslich. 1993. A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum. J. Virol. 67:4972-4980.
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.G.4
  • 24
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed, E. O., J. M. Orenstein, A. J. Buckler-White, and M. A. Martin. 1994. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:5311-5320.
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Buckler-White, A.J.3    Martin, M.A.4
  • 25
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich, E., K. Vancompernolle, C. Huet, M. Goethals J. Finidori, J. Vandekerckhove, and D. Louvard. 1992. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70:81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 27
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Göttlinger, 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
    • Göttlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 28
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Göttlinger, H. G., J. G. Sodroski, and W. A. Haseltine. 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86:5781-5787.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5787
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 29
    • 0031007620 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA
    • Guo, J., L. E. Henderson, J. Bess, B. Kane, and J. G. Levin. 1997. Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA. J. Virol. 71:5178-5188.
    • (1997) J. Virol. , vol.71 , pp. 5178-5188
    • Guo, J.1    Henderson, L.E.2    Bess, J.3    Kane, B.4    Levin, J.G.5
  • 30
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processings, and complete amino acid sequences
    • Henderson, L. E., M. A. Bowers, R. C. N. Sowder, S. A. Serabyn, D. G. Johnson, J. W. Bess, Jr., L. O. Arthur, D. K. Bryant, and C. Fenselau. 1992. Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences. J. Virol. 66:1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder, R.C.N.3    Serabyn, S.A.4    Johnson, D.G.5    Bess J.W., Jr.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 31
    • 0021690345 scopus 로고
    • Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products
    • 30a. Henderson, L. E., R. Sowder, T. D. Copeland, G. Smythers, and S. Oroszlan. 1984. Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products. J. Virol. 52:492-500.
    • (1984) J. Virol. , vol.52 , pp. 492-500
    • Henderson, L.E.1    Sowder, R.2    Copeland, T.D.3    Smythers, G.4    Oroszlan, S.5
  • 32
    • 0028971135 scopus 로고
    • Gag is required for particle production from full-length human immunodeficiency virus type I molecular clones expressing protease
    • Gag is required for particle production from full-length human immunodeficiency virus type I 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
  • 33
    • 0002168907 scopus 로고
    • Macromolecular interations in the assembly of HIV and other retroviruses
    • Hunter, E. 1994. Macromolecular interations in the assembly of HIV and other retroviruses. Semin. Virol. 5:71-83.
    • (1994) Semin. Virol. , vol.5 , pp. 71-83
    • Hunter, E.1
  • 34
    • 0030067973 scopus 로고    scopus 로고
    • Effect of human immunodeficiency virus type 1 (HIV-I) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro
    • Ji, X., G. J. Klarmann, and B. D. Preston. 1996. Effect of human immunodeficiency virus type 1 (HIV-I) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro. Biochemistry 35:132-143.
    • (1996) Biochemistry , vol.35 , pp. 132-143
    • Ji, X.1    Klarmann, G.J.2    Preston, B.D.3
  • 35
    • 0027101766 scopus 로고
    • Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation
    • Erratum, 74: 943, 1993
    • Jowett, J. B., D. J. Hockley, M. V. Nermut, and I. M. Jones. 1992. Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation. J. Gen. Virol. 73:3079-3086. (Erratum, 74: 943, 1993.)
    • (1992) J. Gen. Virol. , vol.73 , pp. 3079-3086
    • Jowett, J.B.1    Hockley, D.J.2    Nermut, M.V.3    Jones, I.M.4
  • 36
    • 0030420089 scopus 로고    scopus 로고
    • Intracellular transport of retroviral capsid components
    • Krausslich, H. G., and R. Welker. 1996. Intracellular transport of retroviral capsid components. Curr. Top. Microbiol. Immunol. 214:25-63.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 25-63
    • Krausslich, H.G.1    Welker, R.2
  • 37
    • 0032579851 scopus 로고    scopus 로고
    • Actin binding and nucleation by Autographa California M nucleopolyhedrovirus
    • Lanier, L. M., and L. E. Volkman. 1998. Actin binding and nucleation by Autographa California M nucleopolyhedrovirus. Virology 243:167-177.
    • (1998) Virology , vol.243 , pp. 167-177
    • Lanier, L.M.1    Volkman, L.E.2
  • 38
    • 0031547959 scopus 로고    scopus 로고
    • Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability
    • Lapadat-Tapolsky, M., C. Gabus, M. Rau, and J. L. Darlix. 1997. Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability. J. Mol. Biol. 268:250-260.
    • (1997) J. Mol. Biol. , vol.268 , pp. 250-260
    • Lapadat-Tapolsky, M.1    Gabus, C.2    Rau, M.3    Darlix, J.L.4
  • 39
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen, P., E. V. Fedorov, A. A. Fedorov, S. C. Almo, and D. G. Drubin. 1997. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 16:5520-5530.
    • (1997) EMBO J. , vol.16 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 40
    • 0031663245 scopus 로고    scopus 로고
    • A bipartite membrane-binding signal in the human immunodeficiency virus type-1 matrix protein is required for the proteolytic processing of Gag precursors in a cell type-dependent manner
    • Lee, Y.-M., C.-J. Tian, and X.-F. Yu. 1998. A bipartite membrane-binding signal in the human immunodeficiency virus type-1 matrix protein is required for the proteolytic processing of Gag precursors in a cell type-dependent manner. J. Virol. 72:9061-9068.
    • (1998) J. Virol. , vol.72 , pp. 9061-9068
    • Lee, Y.-M.1    Tian, C.-J.2    Yu, X.-F.3
  • 44
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R. O., and S. W. Craig. 1997. The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94:5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 45
  • 46
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • Letter
    • McKnight, C. J., P. T. Matsudaira, and P. S. Kim. 1997. NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4:180-184. (Letter.)
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 49
    • 0028217413 scopus 로고
    • Role of the cytoskeleton in cell-to-cell transmission of human immunodeficiency virus
    • Pearce-Pratt, R., D. Malamud, and D. M. Phillips. 1994. Role of the cytoskeleton in cell-to-cell transmission of human immunodeficiency virus. J. Virol. 68:2898-2905.
    • (1994) J. Virol. , vol.68 , pp. 2898-2905
    • Pearce-Pratt, R.1    Malamud, D.2    Phillips, D.M.3
  • 50
    • 84937346333 scopus 로고
    • Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity
    • Peliska, J. A., S. Balasubramanian, D. P. Giedroc, and S. J. Benkovic. 1994. Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity. Biochemistry 33:13817-13823.
    • (1994) Biochemistry , vol.33 , pp. 13817-13823
    • Peliska, J.A.1    Balasubramanian, S.2    Giedroc, D.P.3    Benkovic, S.J.4
  • 51
    • 0029817030 scopus 로고    scopus 로고
    • Directional budding of human immunodeficiency virus from monocytes
    • Perotti, M. E., X. Tan, and D. M. Phillips. 1996. Directional budding of human immunodeficiency virus from monocytes. J. Virol. 70:5916-5921.
    • (1996) J. Virol. , vol.70 , pp. 5916-5921
    • Perotti, M.E.1    Tan, X.2    Phillips, D.M.3
  • 52
    • 0032005974 scopus 로고    scopus 로고
    • The modular structure of actin-rcgulatory proteins
    • Puius, Y. A., N. M. Mahoney, and S. C. Almo. 1998. The modular structure of actin-rcgulatory proteins. Curr. Opin. Cell Biol. 10:23-34.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 23-34
    • Puius, Y.A.1    Mahoney, N.M.2    Almo, S.C.3
  • 53
    • 0029941433 scopus 로고    scopus 로고
    • HIV-1 Gag protein associates with F-actin present in microfilaments
    • Rev, O., J. Canon, and P. Krogstad. 1996. HIV-1 Gag protein associates with F-actin present in microfilaments. Virology 220:530-534.
    • (1996) Virology , vol.220 , pp. 530-534
    • Rev, O.1    Canon, J.2    Krogstad, P.3
  • 54
    • 0029009007 scopus 로고
    • Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro
    • Rodriguez-Rodriguez, L., Z. Tsuchihashi, G. M. Fuentes, R. A. Bambara, and P. J. Fay. 1995. Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro. J. Biol. Chem. 270:15005-15011.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15005-15011
    • Rodriguez-Rodriguez, L.1    Tsuchihashi, Z.2    Fuentes, G.M.3    Bambara, R.A.4    Fay, P.J.5
  • 56
    • 0028901720 scopus 로고
    • Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells
    • Sasaki, H., M. Nakamura, T. Ohno, Y. Matsuda, Y. Yuda, and Y. Nonomura. 1995. Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells. Proc. Natl. Acad. Sci. USA 92: 2026-2030.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2026-2030
    • Sasaki, H.1    Nakamura, M.2    Ohno, T.3    Matsuda, Y.4    Yuda, Y.5    Nonomura, Y.6
  • 57
    • 0002855593 scopus 로고
    • Cis-acting genomic elements and trans-acting proteins involved in the assembly of RNA viruses
    • Schlesinger, S., S. Makino, and M. L. Linial. 1994. cis-acting genomic elements and trans-acting proteins involved in the assembly of RNA viruses. Semin. Virol. 5:39-49.
    • (1994) Semin. Virol. , vol.5 , pp. 39-49
    • Schlesinger, S.1    Makino, S.2    Linial, M.L.3
  • 58
    • 0030273297 scopus 로고    scopus 로고
    • HIV-1 particle release mediated by Vpu is distinct from that mediated by p6
    • Schwartz, M. D., R. J. Geraghty, and A. T. Panganiban. 1996. HIV-1 particle release mediated by Vpu is distinct from that mediated by p6. Virology 224: 302-309.
    • (1996) Virology , vol.224 , pp. 302-309
    • Schwartz, M.D.1    Geraghty, R.J.2    Panganiban, A.T.3
  • 59
    • 0028355603 scopus 로고
    • Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly
    • Spearman, P., J. J. Wang, N. Vander Heyden, and L. Ratner. 1994. Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly. J. Virol. 68:3232-3242.
    • (1994) J. Virol. , vol.68 , pp. 3232-3242
    • Spearman, P.1    Wang, J.J.2    Vander Heyden, N.3    Ratner, L.4
  • 60
    • 0030050591 scopus 로고    scopus 로고
    • Portals of entry: Uncovering HIV nuclear transport pathways
    • Stevenson, M. 1996. Portals of entry: uncovering HIV nuclear transport pathways. Trends Cell Biol. 6:9-15.
    • (1996) Trends Cell Biol. , vol.6 , pp. 9-15
    • Stevenson, M.1
  • 61
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. Coffin, S. Hughes, and H. Varmus (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Swanstrom, R., and J. Wills. 1998. Synthesis, assembly, and processing of viral proteins. p. 263-334. In J. Coffin, S. Hughes, and H. Varmus (ed.). Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1998) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.2
  • 62
    • 0029121697 scopus 로고
    • Formation of stable and functional HIV-1 nucleoprotein complexes in vitro
    • Tanchou, V., C. Gabus, V. Rogemond, and J. L. Darlix. 1995. Formation of stable and functional HIV-1 nucleoprotein complexes in vitro. J. Mol. Biol. 252:563-571.
    • (1995) J. Mol. Biol. , vol.252 , pp. 563-571
    • Tanchou, V.1    Gabus, C.2    Rogemond, V.3    Darlix, J.L.4
  • 63
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Editorial
    • Wills, J. W., and R. C. Craven. 1991. Form, function, and use of retroviral gag proteins. AIDS 5:639-654. (Editorial.)
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 64
    • 0029794295 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein reduces reverse transcriptase pausing at a secondary structure near the murine leukemia virus polypurine tract
    • Wu, W., L. E. Henderson, T. D. Copeland, R. J. Gorelick, W. J. Bosche, A. Rein, and J. G. Levin. 1996. Human immunodeficiency virus type 1 nucleocapsid protein reduces reverse transcriptase pausing at a secondary structure near the murine leukemia virus polypurine tract. J. Virol. 70:7132-7142.
    • (1996) J. Virol. , vol.70 , pp. 7132-7142
    • Wu, W.1    Henderson, L.E.2    Copeland, T.D.3    Gorelick, R.J.4    Bosche, W.J.5    Rein, A.6    Levin, J.G.7
  • 66
    • 0029582762 scopus 로고
    • Role of the C terminus Gag protein in human immunodeficiency virus type 1 virion assembly and maturation
    • Yu, X.-F., Z. Matsuda, Q. C. Yu, T. H. Lee, and M. Essex. 1995. Role of the C terminus Gag protein in human immunodeficiency virus type 1 virion assembly and maturation. J. Gen. Virol. 76:3171-3179.
    • (1995) J. Gen. Virol. , vol.76 , pp. 3171-3179
    • Yu, X.-F.1    Matsuda, Z.2    Yu, Q.C.3    Lee, T.H.4    Essex, M.5
  • 67
    • 0027381634 scopus 로고
    • Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor
    • Yuan, X., X. Yu, T. H. Lee, and M. Essex. 1993. Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor. J. Virol. 67:6387-6394.
    • (1993) J. Virol. , vol.67 , pp. 6387-6394
    • Yuan, X.1    Yu, X.2    Lee, T.H.3    Essex, M.4
  • 68
    • 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
  • 69
    • 0031910808 scopus 로고    scopus 로고
    • Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain
    • Zhang, Y., H. Qian, Z. Love, and E. Barklis. 1998. Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain. J. Virol. 72:1782-1789.
    • (1998) J. Virol. , vol.72 , pp. 1782-1789
    • Zhang, Y.1    Qian, H.2    Love, Z.3    Barklis, E.4
  • 70
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., L. J. Parent, J. W. Wills, and M. D. Resh. 1994. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68:2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4


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