메뉴 건너뛰기




Volumn 77, Issue 23, 2003, Pages 12592-12602

Human Immunodeficiency Virus Type 1 N-Terminal Capsid Mutants Containing Cores with Abnormally High Levels of Capsid Protein and Virtually No Reverse Transcriptase

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CAPSID PROTEIN; CORE PROTEIN; CYCLOPHILIN A; RNA DIRECTED DNA POLYMERASE; VIRUS DNA;

EID: 0242409380     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.23.12592-12602.2003     Document Type: Article
Times cited : (47)

References (73)
  • 2
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol. , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 3
    • 0030878798 scopus 로고    scopus 로고
    • Cyclophilin A-induced alterations of human immunodeficiency virus type 1 CA protein in vitro
    • Agresta, B. E., and C. A. Carter. 1997. Cyclophilin A-induced alterations of human immunodeficiency virus type 1 CA protein in vitro. J. Virol. 71:6921-6927.
    • (1997) J. Virol. , vol.71 , pp. 6921-6927
    • Agresta, B.E.1    Carter, C.A.2
  • 4
    • 0030835321 scopus 로고    scopus 로고
    • Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A
    • Aiken, C. 1997. Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A. J. Virol. 71:5871-5877.
    • (1997) J. Virol. , vol.71 , pp. 5871-5877
    • Aiken, C.1
  • 5
    • 0030586691 scopus 로고    scopus 로고
    • Amino acid substitutions in the CA protein of Moloney murine leukemia virus that block early events in infection
    • Alin, K., and S. P. Goff. 1996. Amino acid substitutions in the CA protein of Moloney murine leukemia virus that block early events in infection. Virology 222:339-351.
    • (1996) Virology , vol.222 , pp. 339-351
    • Alin, K.1    Goff, S.P.2
  • 7
    • 0034954578 scopus 로고    scopus 로고
    • Second-site suppressors of Rous sarcoma virus CA mutations: Evidence for interdomain interactions
    • Bowzard, J. B., J. W. Wills, and R. C. Craven. 2001. Second-site suppressors of Rous sarcoma virus CA mutations: evidence for interdomain interactions. J. Virol. 75:6850-6856.
    • (2001) J. Virol. , vol.75 , pp. 6850-6856
    • Bowzard, J.B.1    Wills, J.W.2    Craven, R.C.3
  • 8
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten, D., E. K. Franke, and J. Luban. 1996. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70:3551-3560.
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 9
    • 0027199982 scopus 로고
    • Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection
    • Bukrinsky, M. I., N. Sharova, T. L. McDonald, T. Pushkarskaya, W. G. Tarpley, and M. Stevenson. 1993. Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection. Proc. Natl. Acad. Sci. USA 90:6125-6129.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6125-6129
    • Bukrinsky, M.I.1    Sharova, N.2    McDonald, T.L.3    Pushkarskaya, T.4    Tarpley, W.G.5    Stevenson, M.6
  • 10
    • 0034751087 scopus 로고    scopus 로고
    • Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants
    • Cairns, T. M., and R. C. Craven. 2001. Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants. J. Virol. 75:242-250.
    • (2001) J. Virol. , vol.75 , pp. 242-250
    • Cairns, T.M.1    Craven, R.C.2
  • 11
    • 0036779196 scopus 로고    scopus 로고
    • Effects of gag mutations on human immunodeficiency virus type 1 particle assembly, processing, and cyclophilin A incorporation
    • Chiu, H.-C., F.-D. Wang, S.-Y. Yao, and C.-T. Wang. 2002. Effects of gag mutations on human immunodeficiency virus type 1 particle assembly, processing, and cyclophilin A incorporation. J. Med. Virol. 68:156-163.
    • (2002) J. Med. Virol. , vol.68 , pp. 156-163
    • Chiu, H.-C.1    Wang, F.-D.2    Yao, S.-Y.3    Wang, C.-T.4
  • 12
    • 0036635446 scopus 로고    scopus 로고
    • Assembling the human immunodeficiency virus type 1
    • Cimarelli, A., and J.-L Darlix. 2002. Assembling the human immunodeficiency virus type 1. Cell. Mol. Life Sci. 59:1166-1184.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1166-1184
    • Cimarelli, A.1    Darlix, J.-L.2
  • 13
    • 0035027292 scopus 로고    scopus 로고
    • Structural consequences of cyclophilin A binding on maturational refolding in human immunodeficiency virus type 1 capsid protein
    • Dietrich, L., L. S. Ehrlich, T. J. LaGrassa, D. Ebbets-Reed, and C. Carter. 2001. Structural consequences of cyclophilin A binding on maturational refolding in human immunodeficiency virus type 1 capsid protein. J. Virol. 75:4721-4733.
    • (2001) J. Virol. , vol.75 , pp. 4721-4733
    • Dietrich, L.1    Ehrlich, L.S.2    LaGrassa, T.J.3    Ebbets-Reed, D.4    Carter, C.5
  • 14
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman, T., A. Bukovsky, Å. Öhagen, S. Höglund, and H. G. Göttlinger. 1994. Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68:8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Öhagen, Å.3    Höglund, S.4    Göttlinger, H.G.5
  • 15
    • 0025968854 scopus 로고
    • Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex
    • Farnet, C. M., and W. A. Haseltine. 1991. Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex. J. Virol. 65:1910-1915.
    • (1991) J. Virol. , vol.65 , pp. 1910-1915
    • Farnet, C.M.1    Haseltine, W.A.2
  • 16
    • 0035078745 scopus 로고    scopus 로고
    • Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1
    • Fassati, A., and S. P. Goff. 2001. Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. J. Virol. 75:3626-3635.
    • (2001) J. Virol. , vol.75 , pp. 3626-3635
    • Fassati, A.1    Goff, S.P.2
  • 17
    • 0034653538 scopus 로고    scopus 로고
    • Proline residues in the HIV-1 NH2-terminal capsid domain: Structure determinants for proper core assembly and subsequent steps of early replication
    • Fitzon, T., B. Leschonsky, K. Bieler, C. Paulus, J. Schröder, H. Wolf, and R. Wagner. 2000. Proline residues in the HIV-1 NH2-terminal capsid domain: structure determinants for proper core assembly and subsequent steps of early replication. Virology 268:294-307.
    • (2000) Virology , vol.268 , pp. 294-307
    • Fitzon, T.1    Leschonsky, B.2    Bieler, K.3    Paulus, C.4    Schröder, J.5    Wolf, H.6    Wagner, R.7
  • 18
    • 0037378462 scopus 로고    scopus 로고
    • Disassembly of human immunodeficiency vius type 1 cores in vitro reveals association of Nef with the subviral ribonucleoprotein complex
    • Forshey, B. M., and C. Aiken. 2003. Disassembly of human immunodeficiency vius type 1 cores in vitro reveals association of Nef with the subviral ribonucleoprotein complex. J. Virol. 77:4409-4414.
    • (2003) J. Virol. , vol.77 , pp. 4409-4414
    • Forshey, B.M.1    Aiken, C.2
  • 19
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey, B. M., U. von Schwedler, W. I. Sundquist, and C. Aiken. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76:5667-5677.
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 20
    • 0030219974 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by cyclosporine A or related compounds correlates with the ability to disrupt the Gag-cyclophilin A interaction
    • Franke, E. K., and J. Luban. 1996. Inhibition of HIV-1 replication by cyclosporine A or related compounds correlates with the ability to disrupt the Gag-cyclophilin A interaction. Virology 222:279-282.
    • (1996) Virology , vol.222 , pp. 279-282
    • Franke, E.K.1    Luban, J.2
  • 21
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E. K., H. E. H. Yuan, and J. Luban. 1994. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372:359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 22
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 23
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., E. L. Delwart, G. L. Buchschacher, Jr., and A. T. Panganiban. 1992. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl. Acad. Sci. USA 89:70-74.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher Jr., G.L.3    Panganiban, A.T.4
  • 24
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed, E. O., G. Englund, and M. A. Martin. 1995. Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. J. Virol. 69:3949-3954.
    • (1995) J. Virol. , vol.69 , pp. 3949-3954
    • Freed, E.O.1    Englund, G.2    Martin, M.A.3
  • 25
    • 0028209824 scopus 로고
    • Evidence for a functional interaction between the V1/V2 and C4 domains of human immunodeficiency virus type 1 envelope glycoprotein gp120
    • Freed, E. O., and M. A. Martin. 1994. Evidence for a functional interaction between the V1/V2 and C4 domains of human immunodeficiency virus type 1 envelope glycoprotein gp120. J. Virol. 68:2503-2512.
    • (1994) J. Virol. , vol.68 , pp. 2503-2512
    • Freed, E.O.1    Martin, M.A.2
  • 26
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
    • Freed, E. O., and M. A. Martin. 1995. Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix. J. Virol. 69:1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 27
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R., F. F. Vajdos, S. Yoo, D. K. Worthylake, M. Houseweart, W. I. Sundquist, and C. P. Hill. 1996. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87:1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 29
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser, B. K., S. Li, V. Y. Klishko, J. T. Finch, and W. I. Sundquist. 1999. Assembly and analysis of conical models for the HIV-1 core. Science 283:80-83.
    • (1999) Science , vol.283 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 30
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom, H. R. 1991. Assembly and morphology of HIV: potential effect of structure on viral function. AIDS 5:617-637.
    • (1991) AIDS , vol.5 , pp. 617-637
    • Gelderblom, H.R.1
  • 31
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti, R. K., B. M. Lee, J. Walker, M. F. Summers, S. Yoo, and W. L. Sundquist. 1996. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 273:231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.L.6
  • 32
    • 0041925439 scopus 로고    scopus 로고
    • In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A
    • Grättinger, M., H. Hohenberg, D. Thomas, T. Wilk, B. Müller, and H.-G. Kräusslich. 1999. In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A. Virology 257:247-260.
    • (1999) Virology , vol.257 , pp. 247-260
    • Grättinger, M.1    Hohenberg, H.2    Thomas, D.3    Wilk, T.4    Müller, B.5    Kräusslich, H.-G.6
  • 34
    • 0031954466 scopus 로고    scopus 로고
    • N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross, I., H. Hohenberg, C. Huckhagel, and H.-G. Kräusslich. 1998. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Kräusslich, H.-G.4
  • 36
    • 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. Sowder II, 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 II, R.C.3    Serabyn, S.A.4    Johnson, D.G.5    Bess Jr., J.W.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 38
    • 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
  • 39
    • 0027738867 scopus 로고
    • Characterization of HIV replication complexes early after cell-to-cell infection
    • Karageorgos, L., P. Li, and C. Burrell. 1993. Characterization of HIV replication complexes early after cell-to-cell infection. AIDS Res. Hum. Retrovir. 9:817-823.
    • (1993) AIDS Res. Hum. Retrovir. , vol.9 , pp. 817-823
    • Karageorgos, L.1    Li, P.2    Burrell, C.3
  • 40
    • 0037379214 scopus 로고    scopus 로고
    • Treatment of human immunodeficiency virus type 1 virions depleted of cyclophilin A by natural endogenous reverse transcription restores infectivity
    • Khan, M., M. Garcia-Barrio, and M. D. Powell. 2003. Treatment of human immunodeficiency virus type 1 virions depleted of cyclophilin A by natural endogenous reverse transcription restores infectivity. J. Virol. 77:4431-4434.
    • (2003) J. Virol. , vol.77 , pp. 4431-4434
    • Khan, M.1    Garcia-Barrio, M.2    Powell, M.D.3
  • 41
    • 0034899286 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA
    • Khan, M. A., C. Aberham, S. Kao, H. Akari, R. Gorelick, S. Bour, and K. Strebel. 2001. Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J. Virol. 75:7252-7265.
    • (2001) J. Virol. , vol.75 , pp. 7252-7265
    • Khan, M.A.1    Aberham, C.2    Kao, S.3    Akari, H.4    Gorelick, R.5    Bour, S.6    Strebel, K.7
  • 42
    • 0036788987 scopus 로고    scopus 로고
    • Characterization of a human immunodeficiency virus type 1 pre-integration complex in which the majority of the cDNA is resistant to DNase I digestion
    • Khiytani, D. K., and N. J. Dimmock. 2002. Characterization of a human immunodeficiency virus type 1 pre-integration complex in which the majority of the cDNA is resistant to DNase I digestion. J. Gen. Virol. 83:2523-2532.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2523-2532
    • Khiytani, D.K.1    Dimmock, N.J.2
  • 43
    • 0033035418 scopus 로고    scopus 로고
    • Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity
    • Kiernan, R. E., A. Ono, and E. O. Freed. 1999. Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity. J. Virol. 73:4728-4737.
    • (1999) J. Virol. , vol.73 , pp. 4728-4737
    • Kiernan, R.E.1    Ono, A.2    Freed, E.O.3
  • 44
    • 0031837693 scopus 로고    scopus 로고
    • Generation of HIV-1/HIV-2 cross-reactive peptide antisera by small sequence changes in HIV-1 reverse transcriptase and integrase immunizing peptides
    • Klutch, M., A. M. Woerner, C. J. Marcus-Sekura, and J. G. Levin. 1998. Generation of HIV-1/HIV-2 cross-reactive peptide antisera by small sequence changes in HIV-1 reverse transcriptase and integrase immunizing peptides. J. Biomed. Sci. 5:192-202.
    • (1998) J. Biomed. Sci. , vol.5 , pp. 192-202
    • Klutch, M.1    Woerner, A.M.2    Marcus-Sekura, C.J.3    Levin, J.G.4
  • 45
    • 0032863144 scopus 로고    scopus 로고
    • Association of Nef with the human immunodeficiency virus type 1 core
    • Kotov, A., J. Zhou, P. Flicker, and C. Aiken. 1999. Association of Nef with the human immunodeficiency virus type 1 core. J. Virol. 73:8824-8830.
    • (1999) J. Virol. , vol.73 , pp. 8824-8830
    • Kotov, A.1    Zhou, J.2    Flicker, P.3    Aiken, C.4
  • 46
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structues
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structues. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 0037462921 scopus 로고    scopus 로고
    • Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry
    • Lanman, J., T. T. Lam, S. Barnes, M. Sakalian, M. R. Emmett, A. G. Marshall, and P. E. Prevelige, Jr. 2003. Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry. J. Mol. Biol. 325:759-772.
    • (2003) J. Mol. Biol. , vol.325 , pp. 759-772
    • Lanman, J.1    Lam, T.T.2    Barnes, S.3    Sakalian, M.4    Emmett, M.R.5    Marshall, A.G.6    Prevelige Jr., P.E.7
  • 48
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li, S., C. P. Hill, W. I. Sundquist, and J. T. Finch. 2000. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407:409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 49
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., K. L. Bossolt, E. K. Franke, G. V. Kalpana, and S. P. Goff. 1993. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73:1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 51
    • 0023755462 scopus 로고
    • The gag gene products of human immunodeficiency virus type 1: Alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors
    • Mervis, R. J., N. Ahmad, E. P. Lillehoj, M. G. Raum, F. H. R. Salazar, H. W. Chan, and S. Venkatesan. 1988. The gag gene products of human immunodeficiency virus type 1: alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors. J. Virol. 62:3993-4002.
    • (1988) J. Virol. , vol.62 , pp. 3993-4002
    • Mervis, R.J.1    Ahmad, N.2    Lillehoj, E.P.3    Raum, M.G.4    Salazar, F.H.R.5    Chan, H.W.6    Venkatesan, S.7
  • 52
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: Studies of organization and composition
    • Miller, M. D., C. M. Farnet, and F. D. Bushman. 1997. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Virol. 71:5382-5390.
    • (1997) J. Virol. , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 54
    • 0029151733 scopus 로고
    • Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain
    • Ott, D. E., L. V. Coren, D. G. Johnson, R. C. Sowder II, L. O. Arthur, and L. E. Henderson. 1995. Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain. AIDS Res. Hum. Retrovir. 11:1003-1006.
    • (1995) AIDS Res. Hum. Retrovir. , vol.11 , pp. 1003-1006
    • Ott, D.E.1    Coren, L.V.2    Johnson, D.G.3    Sowder II, R.C.4    Arthur, L.O.5    Henderson, L.E.6
  • 55
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle
    • Reicin, A. S., A. Ohagen, L. Yin, S. Hoglund, and S. P. Goff. 1996. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle. J. Virol. 70:8645-8652.
    • (1996) J. Virol. , vol.70 , pp. 8645-8652
    • Reicin, A.S.1    Ohagen, A.2    Yin, L.3    Hoglund, S.4    Goff, S.P.5
  • 56
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: Effects on virion particle assembly, release, and infectivity
    • Reicin, A. S., S. Paik, R. D. Berkowitz, J. Luban, I. Lowy, and S. P. Goff. 1995. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity. J. Virol. 69:642-650.
    • (1995) J. Virol. , vol.69 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Goff, S.P.6
  • 57
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Swanstrom, R., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 59
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang, C., Y. Ndassa, and M. F. Summers. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9:537-543.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 60
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang, S., T. Murakami, B. E. Agresta, S. Campbell, E. O. Freed, and J. G. Levin. 2001. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J. Virol. 75:9357-9366.
    • (2001) J. Virol. , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 62
    • 0033534386 scopus 로고    scopus 로고
    • Structural biology of HIV
    • Turner, B. G., and M. F. Summers. 1999. Structural biology of HIV. J. Mol. Biol. 285:1-32.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1-32
    • Turner, B.G.1    Summers, M.F.2
  • 63
    • 0003151659 scopus 로고    scopus 로고
    • Retroviral virions and genomes
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Vogt, V. M. 1997. Retroviral virions and genomes, p. 27-69. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) Retroviruses , pp. 27-69
    • Vogt, V.M.1
  • 65
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler, U. K., K. M. Stray, J. E. Garrus, and W. I. Sundquist. 2003. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77:5439-5450.
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • Von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 66
    • 0027160015 scopus 로고
    • Assembly, processing, and infectivity of human immunodeficiency virus type 1 Gag mutants
    • Wang, C.-T., and E. Barklis. 1993. Assembly, processing, and infectivity of human immunodeficiency virus type 1 Gag mutants. J. Virol. 67:4264-4273.
    • (1993) J. Virol. , vol.67 , pp. 4264-4273
    • Wang, C.-T.1    Barklis, E.2
  • 67
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker, R., H. Hohenberg, U. Tessmer, C. Huckhagel, and H.-G. Kräusslich. 2000. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74:1168-1177.
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Kräusslich, H.-G.5
  • 68
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers, K., G. Rutter, H. Kottler, U. Tessmer, H. Hohenberg, and H.-G. Kräusslich. 1998. Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72:2846-2854.
    • (1998) J. Virol. , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Kräusslich, H.-G.6
  • 69
    • 0033602561 scopus 로고    scopus 로고
    • Cyclophilin A incorporation is not required for human immunodeficiency virus type 1 particle maturation and does not destabilize the mature capsid
    • Wiegers, K., G. Rutter, U. Schubert, M. Grättinger, and H.-G. Kräusslich. 1999. Cyclophilin A incorporation is not required for human immunodeficiency virus type 1 particle maturation and does not destabilize the mature capsid. Virology 257:261-274.
    • (1999) Virology , vol.257 , pp. 261-274
    • Wiegers, K.1    Rutter, G.2    Schubert, U.3    Grättinger, M.4    Kräusslich, H.-G.5
  • 70
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • Willey, R. L., J. S. Bonifacino, B. J. Potts, M. A. Martin, and R. D. Klausner. 1988. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. Proc. Natl. Acad. Sci. USA 85:9580-9584.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 71
    • 0025813326 scopus 로고
    • Mutations within the human immunodeficiency virus type 1 gp160 envelope glycoprotein alter its intracellular transport and processing
    • Willey, R. L., T. Klimkait, D. M. Frucht, J. S. Bonifacino, and M. A. Martin. 1991. Mutations within the human immunodeficiency virus type 1 gp160 envelope glycoprotein alter its intracellular transport and processing. Virology 184:319-329.
    • (1991) Virology , vol.184 , pp. 319-329
    • Willey, R.L.1    Klimkait, T.2    Frucht, D.M.3    Bonifacino, J.S.4    Martin, M.A.5
  • 72
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral Gag proteins
    • Wills, J. W., and R. C. Craven. 1991. Form, function, and use of retroviral Gag proteins. AIDS 5:639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.