메뉴 건너뛰기




Volumn 246, Issue 2, 1998, Pages 191-198

Retroviral matrix proteins: A structural perspective

Author keywords

[No Author keywords available]

Indexed keywords

NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; PROTEIN TRANSPORT; RETROVIRUS; SHORT SURVEY; VIRUS ASSEMBLY; VIRUS CELL INTERACTION;

EID: 0032486598     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9206     Document Type: Article
Times cited : (52)

References (92)
  • 1
    • 0026522457 scopus 로고
    • A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein
    • Brody B. A., Rhee S. S., Sommerfelt M. A., Hunter E. A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein. Proc. Natl. Acad. Sci. USA. 89:1992;3443-3447.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3443-3447
    • Brody, B.A.1    Rhee, S.S.2    Sommerfelt, M.A.3    Hunter, E.4
  • 2
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M., Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. USA. 87:1990;523-527.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 7
    • 0030596149 scopus 로고    scopus 로고
    • Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from different classes of pathogenic human retroviruses
    • Christensen A. M., Massiah M. A., Turner B., Sundquist W. I., Summers M. F. Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from different classes of pathogenic human retroviruses. J. Mol. Biol. 264:1996;1117-1131.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1117-1131
    • Christensen, A.M.1    Massiah, M.A.2    Turner, B.3    Sundquist, W.I.4    Summers, M.F.5
  • 8
    • 0030869124 scopus 로고    scopus 로고
    • The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly
    • Conte M. R., Klikova M., Hunter E., Ruml T., Matthews S. The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly. EMBO J. 16:1997;5819-5826.
    • (1997) EMBO J. , vol.16 , pp. 5819-5826
    • Conte, M.R.1    Klikova, M.2    Hunter, E.3    Ruml, T.4    Matthews, S.5
  • 9
    • 0029857253 scopus 로고    scopus 로고
    • Direct interaction between the envelope and matrix proteins of HIV-1
    • Cosson P. Direct interaction between the envelope and matrix proteins of HIV-1. EMBO J. 15:1996;5783-5788.
    • (1996) EMBO J. , vol.15 , pp. 5783-5788
    • Cosson, P.1
  • 10
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman T., Bukovsky A., Ohagen A., Hoglund S., Gottlinger H. G. Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68:1994a;8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.G.5
  • 11
    • 0027979135 scopus 로고
    • Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
    • Dorfman T., Mammano F., Haseltine W. A., Gottlinger H. G. Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 68:1994b;1689-1696.
    • (1994) J. Virol. , vol.68 , pp. 1689-1696
    • Dorfman, T.1    Mammano, F.2    Haseltine, W.A.3    Gottlinger, H.G.4
  • 12
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic tail blocks virus infectivity
    • Dubay J. W., Roberts S. J., Hahn B. H., Hunter E. Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic tail blocks virus infectivity. J. Virol. 66:1992;6616-6625.
    • (1992) J. Virol. , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 13
    • 0027177935 scopus 로고
    • A large deletion in the matrix protein of the human immunodeficiency virusgag
    • Facke M., Janetzko A., Shoeman R. L., Krausslich H.-G. A large deletion in the matrix protein of the human immunodeficiency virusgag. J. Virol. 67:1993;4972-4980.
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.-G.4
  • 14
    • 0030747461 scopus 로고    scopus 로고
    • HIV-1 infection of non-dividing cells: Evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import
    • Fouchier R. A. M., Meyer B. E., Simon J. H. M., Fisher U., Malim M. H. HIV-1 infection of non-dividing cells: Evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import. EMBO J. 16:1997;4531-4539.
    • (1997) EMBO J. , vol.16 , pp. 4531-4539
    • Fouchier, R.A.M.1    Meyer, B.E.2    Simon, J.H.M.3    Fisher, U.4    Malim, M.H.5
  • 15
    • 0031472241 scopus 로고    scopus 로고
    • Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection
    • Freed E. O., Englund G., Maldarelli F., Martin M. A. Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection. Cell. 88:1997;171-173.
    • (1997) Cell , vol.88 , pp. 171-173
    • Freed, E.O.1    Englund, G.2    Maldarelli, F.3    Martin, M.A.4
  • 16
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tail is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
    • Freed E. O., Martin M. A. Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tail is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix. J. Virol. 69:1995;1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 17
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • Freed E. O., Martin M. A. Domains of the immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions. J. Virol. 70:1996;341-351.
    • (1996) J. Virol. , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 18
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed E. O., Orestein J. M., Buckler-White A. J., Martin M. A. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:1994;5311-5320.
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orestein, J.M.2    Buckler-White, A.J.3    Martin, M.A.4
  • 19
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller S. D., Wilk T., Gowen B. E., Krausslick H.-G., Vogt V. M. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7:1997;729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krausslick, H.-G.4    Vogt, V.M.5
  • 20
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda D. H., Lever A., Terwillinger E., Sodroski J. Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 66:1992;3306-3315.
    • (1992) J. Virol. , vol.66 , pp. 3306-3315
    • Gabuzda, D.H.1    Lever, A.2    Terwillinger, E.3    Sodroski, J.4
  • 21
    • 0030987672 scopus 로고    scopus 로고
    • HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway
    • Gallay P., Hope T., Chin D., Trono D. HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. Proc. Natl. Acad. Sci. USA. 94:1997;9825-9830.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9825-9830
    • Gallay, P.1    Hope, T.2    Chin, D.3    Trono, D.4
  • 22
    • 0028821383 scopus 로고
    • HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is key regulator
    • Gallay P., Swingler S., Aiken C., Trono D. HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is key regulator. Cell. 80:1995a;379-388.
    • (1995) Cell , vol.80 , pp. 379-388
    • Gallay, P.1    Swingler, S.2    Aiken, C.3    Trono, D.4
  • 23
    • 0028839344 scopus 로고
    • HIV-1 nuclear import is governed by the phosphotyrosine-mediated binding of matrix to core domain of integrase
    • Gallay P., Swingler S., Song J., Bushman F., Trono D. HIV-1 nuclear import is governed by the phosphotyrosine-mediated binding of matrix to core domain of integrase. Cell. 83:1995b;569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 25
    • 0021591109 scopus 로고
    • Rous sarcoma virus p19 and gp35 can be chemically crosslinked to high molecular weight complexes
    • Gebhardt A., Bosch J. V., Ziemiecki A., Friis R. R. Rous sarcoma virus p19 and gp35 can be chemically crosslinked to high molecular weight complexes. J. Mol. Biol. 174:1984;297-317.
    • (1984) J. Mol. Biol. , vol.174 , pp. 297-317
    • Gebhardt, A.1    Bosch, J.V.2    Ziemiecki, A.3    Friis, R.R.4
  • 26
    • 0023099283 scopus 로고
    • Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • Gelderblom H. R., Hausmann E. H. S., Ozel M., Pauli G., Koch M. A. Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins. Virology. 156:1987;171-176.
    • (1987) Virology , vol.156 , pp. 171-176
    • Gelderblom, H.R.1    Hausmann, E.H.S.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 27
    • 0024400251 scopus 로고
    • Morphogenesis and morphology of HIV. Structure-function relations
    • Gelderblom H. R., Ozel M., Pauli G. Morphogenesis and morphology of HIV. Structure-function relations. Arch. Virol. 106:1989;1-13.
    • (1989) Arch. Virol. , vol.106 , pp. 1-13
    • Gelderblom, H.R.1    Ozel, M.2    Pauli, G.3
  • 28
    • 0027198787 scopus 로고
    • Assembly of matrix protein of simian immunodeficiency virus into virus-like particles
    • Gonzalez S. A., Affranchino J. L., Gelderblom H. R., Burny A. Assembly of matrix protein of simian immunodeficiency virus into virus-like particles. Virology. 194:1993;548-556.
    • (1993) Virology , vol.194 , pp. 548-556
    • Gonzalez, S.A.1    Affranchino, J.L.2    Gelderblom, H.R.3    Burny, A.4
  • 29
    • 0026317877 scopus 로고
    • Effects of mutations affecting the p6 Gag protein of human immunodeficiency virus particle release
    • Gottlinger H. G., Dorfman T., Sodroski J. G., Haseltine W. A. Effects of mutations affecting the p6 Gag protein of human immunodeficiency virus particle release. Proc. Natl. Acad. Sci. USA. 88:1991;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
  • 31
    • 0023152815 scopus 로고
    • Chemical and immunological characterizations of equine infectious anemia virusgag
    • Henderson L. E., Sowder R. C., Smythers G. W., Oroszlan S. Chemical and immunological characterizations of equine infectious anemia virusgag. J. Virol. 61:1987;1116-1124.
    • (1987) J. Virol. , vol.61 , pp. 1116-1124
    • Henderson, L.E.1    Sowder, R.C.2    Smythers, G.W.3    Oroszlan, S.4
  • 32
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structure of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • Hill C. P., Worthylake D., Bancroft D. P., Christensen A. M., Sundquist W. I. Crystal structure of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly. Proc. Natl. Acad. Sci. USA. 93:1996;3099-3104.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 33
    • 0015366101 scopus 로고
    • Cell cycle dependent activation of Rous sarcoma virus-infected stationary chicken cells: Avian leukosis virus group-specific antigen and ribonucleic acid
    • Humphries E. H., Temin H. M. Cell cycle dependent activation of Rous sarcoma virus-infected stationary chicken cells: Avian leukosis virus group-specific antigen and ribonucleic acid. J. Virol. 10:1972;82-87.
    • (1972) J. Virol. , vol.10 , pp. 82-87
    • Humphries, E.H.1    Temin, H.M.2
  • 34
    • 0016303594 scopus 로고
    • Requirement for cell division for initiation of transcription of Rous sarcoma virus RNA
    • Humphries E. H., Temin H. M. Requirement for cell division for initiation of transcription of Rous sarcoma virus RNA. J. Virol. 14:1974;531-546.
    • (1974) J. Virol. , vol.14 , pp. 531-546
    • Humphries, E.H.1    Temin, H.M.2
  • 35
    • 0002168907 scopus 로고
    • Macromolecular interactions in the assembly of HIV and other retroviruses
    • Hunter E. Macromolecular interactions in the assembly of HIV and other retroviruses. Semin. Virol. 5:1994;71-83.
    • (1994) Semin. Virol. , vol.5 , pp. 71-83
    • Hunter, E.1
  • 37
    • 0027191913 scopus 로고
    • Truncations of SIV transmembrane protein confer expanded virus host range by removing a block to virus entry into cells
    • Johnston P., Dubay J., Hunter E. Truncations of SIV transmembrane protein confer expanded virus host range by removing a block to virus entry into cells. J. Virol. 67:1993;3077-3086.
    • (1993) J. Virol. , vol.67 , pp. 3077-3086
    • Johnston, P.1    Dubay, J.2    Hunter, E.3
  • 39
    • 0026694599 scopus 로고
    • Matrix protein of Akv murine leukemia virus: Genetic mapping of region essential for particle formation
    • Jorgensen E. C., Pedersen F. S., Jorgensen P. Matrix protein of Akv murine leukemia virus: Genetic mapping of region essential for particle formation. J. Virol. 66:1992;4479-4487.
    • (1992) J. Virol. , vol.66 , pp. 4479-4487
    • Jorgensen, E.C.1    Pedersen, F.S.2    Jorgensen, P.3
  • 40
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. Molscript - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 41
    • 0026623010 scopus 로고
    • Packaging system for rapid production of murine leukemia virus vectors with variable tropism
    • Landau N. R., Littman D. R. Packaging system for rapid production of murine leukemia virus vectors with variable tropism. J. Virol. 66:1992;5110-5113.
    • (1992) J. Virol. , vol.66 , pp. 5110-5113
    • Landau, N.R.1    Littman, D.R.2
  • 42
    • 0029961533 scopus 로고    scopus 로고
    • Negative-strand virus M and retrovirus MA proteins: All in a family
    • Lenard J. Negative-strand virus M and retrovirus MA proteins: all in a family. Virology. 216:1996;289-298.
    • (1996) Virology , vol.216 , pp. 289-298
    • Lenard, J.1
  • 43
    • 0028055281 scopus 로고
    • Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus
    • Lewis P. F., Emerman M. Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus. J. Virol. 68:1994;510-516.
    • (1994) J. Virol. , vol.68 , pp. 510-516
    • Lewis, P.F.1    Emerman, M.2
  • 44
    • 0026654682 scopus 로고
    • Human immunodeficiency virus infection of cells arrested in the cell cycle
    • Lewis P., Hensel M., Emerman M. Human immunodeficiency virus infection of cells arrested in the cell cycle. EMBO J. 11:1992;3053-3058.
    • (1992) EMBO J. , vol.11 , pp. 3053-3058
    • Lewis, P.1    Hensel, M.2    Emerman, M.3
  • 45
    • 0025204822 scopus 로고
    • CD4 independent infection by immunodeficiency virus type 1 after phenotypic mixing with human T-cell leukemia viruses
    • Lusso P., Lori F., Gallo R. C. CD4 independent infection by immunodeficiency virus type 1 after phenotypic mixing with human T-cell leukemia viruses. J. Virol. 64:1990a;6341-6344.
    • (1990) J. Virol. , vol.64 , pp. 6341-6344
    • Lusso, P.1    Lori, F.2    Gallo, R.C.3
  • 47
    • 0029037089 scopus 로고
    • Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains
    • Mammano F., Kondo E., Sodroski J., Bukovsky A., Gottlinger H. G. Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains. J. Virol. 69:1995;3824-3830.
    • (1995) J. Virol. , vol.69 , pp. 3824-3830
    • Mammano, F.1    Kondo, E.2    Sodroski, J.3    Bukovsky, A.4    Gottlinger, H.G.5
  • 52
    • 0030035221 scopus 로고    scopus 로고
    • The solution structure of the bovine leukemia virus matrix protein and similarity with lentiviral matrix proteins
    • Matthews S., Mikhailov M., Burny A., Roy P. The solution structure of the bovine leukemia virus matrix protein and similarity with lentiviral matrix proteins. EMBO J. 15:1996;3267-3274.
    • (1996) EMBO J. , vol.15 , pp. 3267-3274
    • Matthews, S.1    Mikhailov, M.2    Burny, A.3    Roy, P.4
  • 54
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral construct in mammalian cells
    • Mergener K., Facke M., Welker R., Brinkmann V., Gelderblom H. R., Krausslich H.-G. Analysis of HIV particle formation using transient expression of subviral construct in mammalian cells. Virology. 186:1992;25-39.
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Facke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Krausslich, H.-G.6
  • 56
    • 0029051459 scopus 로고
    • A molecular determinant of human immunodeficiency virus particle assembly located in the matrix antigen p17
    • Morikawa Y., Kishi T., Zhang W. H., Nermut M. V., Hockley D. J., Jones I. M. A molecular determinant of human immunodeficiency virus particle assembly located in the matrix antigen p17. J. Virol. 69:1995;4519-4523.
    • (1995) J. Virol. , vol.69 , pp. 4519-4523
    • Morikawa, Y.1    Kishi, T.2    Zhang, W.H.3    Nermut, M.V.4    Hockley, D.J.5    Jones, I.M.6
  • 58
    • 0029997457 scopus 로고    scopus 로고
    • A large region within the Rous sarcoma virus matrix protein is dispensable for budding and infectivity
    • Nelle T. D., Wills J. W. A large region within the Rous sarcoma virus matrix protein is dispensable for budding and infectivity. J. Virol. 70:1996;2269-2276.
    • (1996) J. Virol. , vol.70 , pp. 2269-2276
    • Nelle, T.D.1    Wills, J.W.2
  • 59
    • 0028292220 scopus 로고
    • Fullerene-like organization of HIV Gag-protein shell in virus-like particles produced by recombinant baculoviruses
    • Nermut M. V., Hockley D. J., Jowett J. B. M., Jones I. M., Garreau M., Thomas D. Fullerene-like organization of HIV Gag-protein shell in virus-like particles produced by recombinant baculoviruses. Virology. 198:1994;288-296.
    • (1994) Virology , vol.198 , pp. 288-296
    • Nermut, M.V.1    Hockley, D.J.2    Jowett, J.B.M.3    Jones, I.M.4    Garreau, M.5    Thomas, D.6
  • 60
    • 0030926508 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 matrix revertants: Effects on virus assembly, Gag processing, and Env incorporation into virions
    • Ono A., Huang M., Freed E. O. Characterization of human immunodeficiency virus type 1 matrix revertants: Effects on virus assembly, Gag processing, and Env incorporation into virions. J. Virol. 71:1997;4409-4418.
    • (1997) J. Virol. , vol.71 , pp. 4409-4418
    • Ono, A.1    Huang, M.2    Freed, E.O.3
  • 62
    • 0023264436 scopus 로고
    • Mutants of the Rous sarcoma virus envelope glycoprotein that lack of the transmembrane anchor and cytoplasmic domains: Analysis of intracellular transport and assembly into virions
    • Perez L. G., Davis G. L., Hunter E. Mutants of the Rous sarcoma virus envelope glycoprotein that lack of the transmembrane anchor and cytoplasmic domains: Analysis of intracellular transport and assembly into virions. J. Virol. 61:1987;2981-2988.
    • (1987) J. Virol. , vol.61 , pp. 2981-2988
    • Perez, L.G.1    Davis, G.L.2    Hunter, E.3
  • 63
    • 0020623678 scopus 로고
    • Topography of murine leukemia virus envelope proteins: Characterization of transmembrane components
    • Pinter A., Honnen W. J. Topography of murine leukemia virus envelope proteins: characterization of transmembrane components. J. Virol. 46:1983;1056-1060.
    • (1983) J. Virol. , vol.46 , pp. 1056-1060
    • Pinter, A.1    Honnen, W.J.2
  • 64
    • 0028180109 scopus 로고
    • Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry
    • Ragheb J. A., Anderson W. F. Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry. J. Virol. 68:1994;3207-3219.
    • (1994) J. Virol. , vol.68 , pp. 3207-3219
    • Ragheb, J.A.1    Anderson, W.F.2
  • 65
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and its implications for virus assembly
    • Rao Z. H., Beyaev A. S., Fry E., Roy P., Jones I. M., Stuart D. I. Crystal structure of SIV matrix antigen and its implications for virus assembly. Nature. 378:1995;743-747.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.H.1    Beyaev, A.S.2    Fry, E.3    Roy, P.4    Jones, I.M.5    Stuart, D.I.6
  • 66
    • 0023109641 scopus 로고
    • Myristylation is required for intracellular transport but not for assembly of D-type retrovirus capsids
    • Rhee S. R., Hunter E. Myristylation is required for intracellular transport but not for assembly of D-type retrovirus capsids. J. Virol. 61:1987;1045-1053.
    • (1987) J. Virol. , vol.61 , pp. 1045-1053
    • Rhee, S.R.1    Hunter, E.2
  • 67
    • 0025027813 scopus 로고
    • A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus
    • Rhee S. R., Hunter E. A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus. Cell. 63:1990;77-86.
    • (1990) Cell , vol.63 , pp. 77-86
    • Rhee, S.R.1    Hunter, E.2
  • 68
    • 0025976083 scopus 로고
    • Amino acid substitutions within the matrix protein of type D retroviruses affect assembly, transport and membrane association of a capsid
    • Rhee S. R., Hunter E. Amino acid substitutions within the matrix protein of type D retroviruses affect assembly, transport and membrane association of a capsid. EMBO J. 10:1991;535-546.
    • (1991) EMBO J. , vol.10 , pp. 535-546
    • Rhee, S.R.1    Hunter, E.2
  • 69
    • 0025282289 scopus 로고
    • Synthesis and processing of the transmembrane envelope protein of equine infectious anemia virus
    • Rice N. R., Henderson L. E., Sowder R. C., Copeland T. D., Oroszlan S., Edwards J. F. Synthesis and processing of the transmembrane envelope protein of equine infectious anemia virus. J. Virol. 64:1990;3770-3778.
    • (1990) J. Virol. , vol.64 , pp. 3770-3778
    • Rice, N.R.1    Henderson, L.E.2    Sowder, R.C.3    Copeland, T.D.4    Oroszlan, S.5    Edwards, J.F.6
  • 70
    • 0024515364 scopus 로고
    • gagis excluded from virus assembly and maturation events
    • gagis excluded from virus assembly and maturation events. J. Virol. 63:1989;2370-2373.
    • (1989) J. Virol. , vol.63 , pp. 2370-2373
    • Schultz, A.M.1    Rein, A.2
  • 71
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha B., Luo M. Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nature Struct. Biol. 4:1997;239-244.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 72
    • 0030922098 scopus 로고    scopus 로고
    • Mutagenesis analysis of murine leukemia virus matrix protein: Identification of regions important for membrane localization and intracellular transport
    • Soneoka Y., Kingsman S. M., Kingsman A. J. Mutagenesis analysis of murine leukemia virus matrix protein: Identification of regions important for membrane localization and intracellular transport. J. Virol. 71:1997;5549-5559.
    • (1997) J. Virol. , vol.71 , pp. 5549-5559
    • Soneoka, Y.1    Kingsman, S.M.2    Kingsman, A.J.3
  • 73
    • 0022530849 scopus 로고
    • Nucleotide sequence of Mason-Pfizer monkey virus: An immunosuppressive D-type retrovirus
    • Sonigo P., Barker C., Hunter E., Wain-Hobson S. Nucleotide sequence of Mason-Pfizer monkey virus: An immunosuppressive D-type retrovirus. Cell. 45:1986;375-385.
    • (1986) Cell , vol.45 , pp. 375-385
    • Sonigo, P.1    Barker, C.2    Hunter, E.3    Wain-Hobson, S.4
  • 74
    • 0030763024 scopus 로고    scopus 로고
    • Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism
    • Spearman P., Horton R., Ratner L., Kuli-Zade I. Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. J. Virol. 71:1997;6582-6592.
    • (1997) J. Virol. , vol.71 , pp. 6582-6592
    • Spearman, P.1    Horton, R.2    Ratner, L.3    Kuli-Zade, I.4
  • 77
    • 0010501791 scopus 로고    scopus 로고
    • Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection- response
    • Trono D., Gallay P. Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection- response. Cell. 88:1997;173-174.
    • (1997) Cell , vol.88 , pp. 173-174
    • Trono, D.1    Gallay, P.2
  • 78
    • 0029984534 scopus 로고    scopus 로고
    • The membrane-binding domain of the Rous sarcoma virus Gag protein
    • Verderame M. F., Nelle T. D., Wills J. W. The membrane-binding domain of the Rous sarcoma virus Gag protein. J. Virol. 70:1996;2664-2668.
    • (1996) J. Virol. , vol.70 , pp. 2664-2668
    • Verderame, M.F.1    Nelle, T.D.2    Wills, J.W.3
  • 79
    • 0026065009 scopus 로고
    • A murine cell line producing HTLV-1 pseudotype virions carrying a selectable marker gene
    • Vile R. G., Schulz T. F., Danos O. F., Collins M. K. L., Weiss R. A. A murine cell line producing HTLV-1 pseudotype virions carrying a selectable marker gene. Virology. 180:1991;420-424.
    • (1991) Virology , vol.180 , pp. 420-424
    • Vile, R.G.1    Schulz, T.F.2    Danos, O.F.3    Collins, M.K.L.4    Weiss, R.A.5
  • 80
    • 0028234528 scopus 로고
    • The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infectionin macrophages and quiescent T lymphocytes
    • von Schwedler U., Kornbluth R. S., Trono D. The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infectionin macrophages and quiescent T lymphocytes. Proc. Natl. Acad. Sci. USA. 91:1994;6992-6996.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6992-6996
    • Von Schwedler, U.1    Kornbluth, R.S.2    Trono, D.3
  • 81
    • 0025720570 scopus 로고
    • Productive human immunodeficiency virus type 1 (HIV-1) infection of nonproliferating human monocytes
    • Weinberg J. B., Matthews T. J., Cullen B. R., Malim M. H. Productive human immunodeficiency virus type 1 (HIV-1) infection of nonproliferating human monocytes. J. Exp. Med. 174:1991;1477-1482.
    • (1991) J. Exp. Med. , vol.174 , pp. 1477-1482
    • Weinberg, J.B.1    Matthews, T.J.2    Cullen, B.R.3    Malim, M.H.4
  • 82
    • 0026741425 scopus 로고
    • Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product
    • Wilk T., Pfeiffer T., Bosch V. Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product. Virology. 189:1992;167-177.
    • (1992) Virology , vol.189 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3
  • 83
    • 0025728301 scopus 로고
    • Form, function and use of retroviral Gag proteins
    • Wills J. W., Craven R. C. Form, function and use of retroviral Gag proteins. AIDS. 5:1991;639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 85
    • 0024513106 scopus 로고
    • Formation of infectious hybrid virions with gibbon ape leukemia virus and human T-cell leukemia virus retroviral envelope glycoproteins and thegagpol
    • Wilson C., Reitz M. S., Okayama H., Eiden M. V. Formation of infectious hybrid virions with gibbon ape leukemia virus and human T-cell leukemia virus retroviral envelope glycoproteins and thegagpol. J. Virol. 63:1989;2374-2378.
    • (1989) J. Virol. , vol.63 , pp. 2374-2378
    • Wilson, C.1    Reitz, M.S.2    Okayama, H.3    Eiden, M.V.4
  • 86
    • 0026715925 scopus 로고
    • The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein in mature virions
    • Yu X., Yuan X., Matzuda Z., Lee T.-H., Essex M. The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein in mature virions. J. Virol. 66:1992;4966-4971.
    • (1992) J. Virol. , vol.66 , pp. 4966-4971
    • Yu, X.1    Yuan, X.2    Matzuda, Z.3    Lee, T.-H.4    Essex, M.5
  • 87
    • 0027473610 scopus 로고
    • Mutations in the cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein impair the incorporation of Env proteins into mature virions
    • Yu X. F., Yuan X., McLane M. F., Lee T.-H., Essex M. Mutations in the cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein impair the incorporation of Env proteins into mature virions. J. Virol. 67:1993;213-221.
    • (1993) J. Virol. , vol.67 , pp. 213-221
    • Yu, X.F.1    Yuan, X.2    McLane, M.F.3    Lee, T.-H.4    Essex, M.5
  • 88
    • 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 Y., Yu X. F., Lee T.-H., Essex M. Mutations in the N terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor. J. Virol. 67:1993;6387-6394.
    • (1993) J. Virol. , vol.67 , pp. 6387-6394
    • Yuan, Y.1    Yu, X.F.2    Lee, T.-H.3    Essex, M.4
  • 89
    • 0025702622 scopus 로고
    • Efficient incorporation of human CD4 protein into avian leukosis virus particles
    • Young J. A. T., Bates P., Willert K., Varmus H. E. Efficient incorporation of human CD4 protein into avian leukosis virus particles. Science. 250:1990;1421-1423.
    • (1990) Science , vol.250 , pp. 1421-1423
    • Young, J.A.T.1    Bates, P.2    Willert, K.3    Varmus, H.E.4
  • 90
    • 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., Parent L. J., Wills J. W., Resh M. D. 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. 68:1994;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
  • 91
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou W., Resh M. D. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70:1996;8540-8548.
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2
  • 92
    • 0027523446 scopus 로고
    • Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases Env incorporation into particles and fusogenicity and infectivity
    • Zingler K., Littman D. Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases Env incorporation into particles and fusogenicity and infectivity. J. Virol. 67:1993;2824-2831.
    • (1993) J. Virol. , vol.67 , pp. 2824-2831
    • Zingler, K.1    Littman, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.