메뉴 건너뛰기




Volumn 72, Issue 6, 1998, Pages 4798-4810

N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; GAG PROTEIN;

EID: 0031954466     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.6.4798-4810.1998     Document Type: Article
Times cited : (161)

References (60)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and non-human 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 non-human 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
    • 0028965266 scopus 로고
    • Mode of action of SDZ NIM811. A non immunosuppressive cyclosporin a analog with activity against human immunodeficiency virus (HIV) type 1: Interference with HIV protein-cyclophilin a interactions
    • Billich, A., F. Hammerschmid, P. Peichl, R. Wenger, G. Zenke, V. Queshian, and B. Rosenwirth. 1995. Mode of action of SDZ NIM811. a non immunosuppressive cyclosporin A analog with activity against human immunodeficiency virus (HIV) type 1: interference with HIV protein-cyclophilin A interactions. J. Virol. 69:2451-2461.
    • (1995) J. Virol. , vol.69 , pp. 2451-2461
    • Billich, A.1    Hammerschmid, F.2    Peichl, P.3    Wenger, R.4    Zenke, G.5    Queshian, V.6    Rosenwirth, B.7
  • 4
    • 2642636368 scopus 로고    scopus 로고
    • Personal communication
    • Boulanger, P. Personal communication.
    • Boulanger, P.1
  • 5
    • 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 iniziation 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 iniziation 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
  • 6
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant, M., and L. Ratner. 1990. Myristoylation-dependent 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
  • 7
    • 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
  • 8
    • 0030947591 scopus 로고    scopus 로고
    • In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: Identification of the p10 domain as a morphological determinant in the formation of spherical particles
    • Campbell, S., and V. M. Vogt. 1997. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J. Virol. 71:4425-4435.
    • (1997) J. Virol. , vol.71 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.2
  • 11
    • 0027177935 scopus 로고
    • A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects particle assembly from the plasma membrane to the endoplasmic reticulum
    • Fäcke, M., A. Janetzko, R. L. Shoeman, and H.-G. Kräusslich. 1993. A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects particle assembly from the plasma membrane to the endoplasmic reticulum. J. Virol. 67:4972-4980.
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Fäcke, M.1    Janetzko, A.2    Shoeman, R.L.3    Kräusslich, H.-G.4
  • 12
    • 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
  • 13
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV particle
    • Fuller, S. D., T. Wilk, B. E. Gowen, H.-G. Kräusslich, and V. M. Vogt. 1997. Cryo-electron microscopy reveals ordered domains in the immature HIV particle. Curr. Biol. 7:729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Kräusslich, H.-G.4    Vogt, V.M.5
  • 14
    • 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
  • 16
    • 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 5:617-638.
    • (1991) AIDS , vol.5 , pp. 617-638
    • Gelderblom, H.R.1
  • 17
    • 0023099283 scopus 로고
    • Fine structure of human immunodeficiency virus (HIV) and immuno-localization of structural proteins
    • Gelderblom, H. R., E. H. S. Hausmann, M. Özel, G. Pauli, and M. A. Koch. 1987. Fine structure of human immunodeficiency virus (HIV) and immuno-localization of structural proteins. Virology 156:171-176.
    • (1987) Virology , vol.156 , pp. 171-176
    • Gelderblom, H.R.1    Hausmann, E.H.S.2    Özel, M.3    Pauli, G.4    Koch, M.A.5
  • 18
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55 gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen, D., E. Jacobs, F. de Foresta, C. Thiriart, M. Francotte, D. Thines, and M. De Wilde. 1989. Assembly and release of HIV-1 precursor Pr55 gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59:103-112.
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 19
    • 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. I. 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.I.6
  • 20
    • 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
  • 21
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation on 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 on infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86:5781-5785.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 22
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross, I., H. Hohenberg, and H.-G. Kräusslich. 1997. In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus. Eur. J. Biochem. 249:592-600.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 592-600
    • Gross, I.1    Hohenberg, H.2    Kräusslich, H.-G.3
  • 23
    • 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
  • 24
    • 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., D. Worthylake, D. P. Bancroft, A. M. Christensen, and W. I. Sundquist. 1996. Crystal structure of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc. Natl. Acad. Sci. USA 93:3099-3104.
    • (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
  • 25
    • 0027995484 scopus 로고
    • Comparative morphology of Gag protein structures produced by mutants of the gag gene of human immunodeficiency virus type 1
    • Hockley, D. J., M. V. Nermut, C. Grief, J. B. M. Jowett, and I. M. Jones. 1994. Comparative morphology of Gag protein structures produced by mutants of the gag gene of human immunodeficiency virus type 1. J. Gen. Virol. 75:2985-2997.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2985-2997
    • Hockley, D.J.1    Nermut, M.V.2    Grief, C.3    Jowett, J.B.M.4    Jones, I.M.5
  • 26
    • 2642591479 scopus 로고    scopus 로고
    • Hohenberg, H., C. Huckhagel. I. Gross, and H.-G. Kräusslich. Unpublished data
    • Hohenberg, H., C. Huckhagel. I. Gross, and H.-G. Kräusslich. Unpublished data.
  • 27
    • 0027982167 scopus 로고
    • High-pressure freezing of cell suspensions in cellulose capillary tubes
    • Hohenberg, H., K. Mannweiler, and M. Müller. 1994. High-pressure freezing of cell suspensions in cellulose capillary tubes. J. Microsc. 175:34-43.
    • (1994) J. Microsc. , vol.175 , pp. 34-43
    • Hohenberg, H.1    Mannweiler, K.2    Müller, M.3
  • 28
    • 0026094405 scopus 로고
    • Role of the gag and pol genes of human immunodeficiency virus in the morphogenesis and maturation of retrovirus-like particles expressed by recombinant vaccinia virus: An ultrastructural study
    • Hoshikawa, N., A. Kojima, A. Yasuda, E. Takayashiki, S. Masuko, J. Chiba, T. Sata, and T. Kurata. 1991. Role of the gag and pol genes of human immunodeficiency virus in the morphogenesis and maturation of retrovirus-like particles expressed by recombinant vaccinia virus: an ultrastructural study. J. Gen. Virol. 72:2509-2517.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2509-2517
    • Hoshikawa, N.1    Kojima, A.2    Yasuda, A.3    Takayashiki, E.4    Masuko, S.5    Chiba, J.6    Sata, T.7    Kurata, T.8
  • 29
    • 0027101766 scopus 로고
    • Distinct signals in human immunodeficiency virus type 1 pr55 necessary for RNA binding and particle formation
    • Jowett, J. B. M., 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.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3079-3086
    • Jowett, J.B.M.1    Hockley, D.J.2    Nermut, M.V.3    Jones, I.M.4
  • 30
    • 0024392730 scopus 로고
    • Human immunodeficiency virus-like particles produced by a vaccinia virus expression system
    • Karacostas, V., K. Najashima, M. A. Gonda, and B. Moss. 1989. Human immunodeficiency virus-like particles produced by a vaccinia virus expression system. Proc. Natl. Acad. Sci. USA 86:8964-8967.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8964-8967
    • Karacostas, V.1    Najashima, K.2    Gonda, M.A.3    Moss, B.4
  • 31
    • 0028811978 scopus 로고
    • Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria
    • Klikova, N., S. S. Rhee, E. Hunter, and T. Ruml. 1995. Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria. J. Virol. 69:1093-1098.
    • (1995) J. Virol. , vol.69 , pp. 1093-1098
    • Klikova, N.1    Rhee, S.S.2    Hunter, E.3    Ruml, T.4
  • 33
    • 0030420089 scopus 로고    scopus 로고
    • Intracellular transport of retroviral capsid components
    • Kräusslich, 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
    • Kräusslich, H.-G.1    Welker, R.2
  • 34
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidometric methods for measuring proteins
    • Layne, E. 1957. Spectrophotometric and turbidometric methods for measuring proteins. Methods Enzymol. 3:447-454.
    • (1957) Methods Enzymol. , vol.3 , pp. 447-454
    • Layne, E.1
  • 35
    • 0028168754 scopus 로고
    • Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal
    • Lee, P. P., and M. Linial. 1994. Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. J. Virol. 68:6644-6654.
    • (1994) J. Virol. , vol.68 , pp. 6644-6654
    • Lee, P.P.1    Linial, M.2
  • 37
    • 0025216877 scopus 로고
    • Cloning, expression, and purification of human cyclophilin a in Escherichia coli and assessment of the catalytic role of cysteins by site-directed mutagenesis
    • Liu, J., M. W. Albers, Q.-M. Chen, S. L. Schreiber, and C. T. Walsh. 1990. Cloning, expression, and purification of human cyclophilin A in Escherichia coli and assessment of the catalytic role of cysteins by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 87:2304-2308.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2304-2308
    • Liu, J.1    Albers, M.W.2    Chen, Q.-M.3    Schreiber, S.L.4    Walsh, C.T.5
  • 38
    • 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 73:1076-1078.
    • (1993) Cell , vol.73 , pp. 1076-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 40
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
    • Mergener, K., M. Fäcke, R. Welker, V. Brinkmann, H. R. Gelderblom, and H.-G. Krâusslich. 1992. Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells. Virology 186:25-39.
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Fäcke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Krâusslich, H.-G.6
  • 41
    • 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. 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.5    Chan, H.W.6    Venkatesan, S.7
  • 43
    • 0029565831 scopus 로고
    • Crystal structure of the SIV matrix antigen and implications for virus assembly
    • Rao, Z., A. S. Balyaev, E. Fry, I. M. Jones, and D. I. Stuart. 1995. Crystal structure of the SIV matrix antigen and implications for virus assembly. Nature 378:743-747.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Balyaev, A.S.2    Fry, E.3    Jones, I.M.4    Stuart, D.I.5
  • 44
    • 0025027813 scopus 로고
    • A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of type C retrovirus
    • Rhee, S. S., and E. Hunter. 1990. A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of type C retrovirus. Cell 63:77-86.
    • (1990) Cell , vol.63 , pp. 77-86
    • Rhee, S.S.1    Hunter, E.2
  • 46
    • 0025744626 scopus 로고
    • Functional domains of HIV-1 gag-polyprotein expressed in baculovirus-infected cells
    • Royer, M., M. Cerutti, B. Gay, S. S. Hong, G. Devauchelle, and P. Boulanger. 1991. Functional domains of HIV-1 gag-polyprotein expressed in baculovirus-infected cells. Virology 184:417-422.
    • (1991) Virology , vol.184 , pp. 417-422
    • Royer, M.1    Cerutti, M.2    Gay, B.3    Hong, S.S.4    Devauchelle, G.5    Boulanger, P.6
  • 47
    • 0029888089 scopus 로고    scopus 로고
    • Synthesis and assembly of retrovirus Gag precursors into immature capsid in vitro
    • Sakalian, M., S. D. Parker, R. A. Weldon, Jr., and E. Hunter. 1996. Synthesis and assembly of retrovirus Gag precursors into immature capsid in vitro. J. Virol. 70:3706-3715.
    • (1996) J. Virol. , vol.70 , pp. 3706-3715
    • Sakalian, M.1    Parker, S.D.2    Weldon Jr., R.A.3    Hunter, E.4
  • 48
    • 0018253747 scopus 로고
    • High frequency of aberrant expression of Moloney leukemia virus in clonal infections
    • Shields, A., O. N. Witte, R. Rothenberg, and D. Baltimore. 1978. High frequency of aberrant expression of Moloney leukemia virus in clonal infections. Cell 14:601-609.
    • (1978) Cell , vol.14 , pp. 601-609
    • Shields, A.1    Witte, O.N.2    Rothenberg, R.3    Baltimore, D.4
  • 49
    • 0025312215 scopus 로고
    • Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV
    • Shioda, T., and H. Shibuta. 1990. Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV. Virology 175:139-148.
    • (1990) Virology , vol.175 , pp. 139-148
    • Shioda, T.1    Shibuta, H.2
  • 50
    • 0025329086 scopus 로고
    • Human immunodeficiency virus type 1 Pr55 gag and Pr160 gag-pol expressed from a simian virus 40 late replacement vector are efficiently processed and assembled into virus-like particles
    • Smith, A. J., M. Cho, M.-L. Hammarskjöld, and D. Rekosh. 1990. Human immunodeficiency virus type 1 Pr55 gag and Pr160 gag-pol expressed from a simian virus 40 late replacement vector are efficiently processed and assembled into virus-like particles. J. Virol. 64:2743-2750.
    • (1990) J. Virol. , vol.64 , pp. 2743-2750
    • Smith, A.J.1    Cho, M.2    Hammarskjöld, M.-L.3    Rekosh, D.4
  • 51
    • 0029821262 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 capsid formation in reticulocyte lysates
    • Spearman, P., and L. Ratner. 1996. Human immunodeficiency virus type 1 capsid formation in reticulocyte lysates. J. Virol. 70:8187-8194.
    • (1996) J. Virol. , vol.70 , pp. 8187-8194
    • Spearman, P.1    Ratner, L.2
  • 52
    • 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. Van der 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    Van Der Heyden, N.3    Ratner, L.4
  • 53
    • 0014603052 scopus 로고
    • The isolation of IgG from mammalian sera with the aid of caprylic acid
    • Steinbuch, M., and R. Andran. 1969. The isolation of IgG from mammalian sera with the aid of caprylic acid. Arch. Biochem. Biophys. 134:279-284.
    • (1969) Arch. Biochem. Biophys. , vol.134 , pp. 279-284
    • Steinbuch, M.1    Andran, R.2
  • 55
    • 0030419901 scopus 로고    scopus 로고
    • Proteolytic processing and particle maturation
    • Vogt, V. M. 1996. Proteolytic processing and particle maturation. Curr. Top. Microbiol. Immunol. 214:95-132.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 95-132
    • Vogt, V.M.1
  • 57
    • 0027487961 scopus 로고
    • Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant
    • Wang, C.-T., Y. Zhang, J. McDermott, and E. Barklis. 1993. Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant. J. Virol. 67:7067-7076.
    • (1993) J. Virol. , vol.67 , pp. 7067-7076
    • Wang, C.-T.1    Zhang, Y.2    McDermott, J.3    Barklis, E.4
  • 58
    • 0030985923 scopus 로고    scopus 로고
    • Plasma membrane targeting of chimeric intracisternal A-type particle polyproteins leads to particle release and specific activation of the viral proteinase
    • Welker, R., A. Janetzko, and H.-G. Kräusslich. 1997. Plasma membrane targeting of chimeric intracisternal A-type particle polyproteins leads to particle release and specific activation of the viral proteinase. J. Virol. 71: 5209-5217.
    • (1997) J. Virol. , vol.71 , pp. 5209-5217
    • Welker, R.1    Janetzko, A.2    Kräusslich, H.-G.3
  • 59
    • 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
  • 60
    • 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.