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Volumn 330, Issue 1, 2004, Pages 271-283

Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1

Author keywords

Cleavage site; Frameshift; Gag Pol; HIV 1; Maturation; p6*; p6pol; Protease activation; Protease regulation; Transframe protein

Indexed keywords

AMINO ACID; GAG PROTEIN; PEPSINOGEN; PEPTIDE DERIVATIVE; POL PROTEIN;

EID: 7444244966     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2004.09.013     Document Type: Article
Times cited : (23)

References (58)
  • 3
    • 0030880945 scopus 로고    scopus 로고
    • In vivo HIV-1 frameshifting efficiency is directly related to the stability of the stem-loop stimulatory signal
    • L. Bidou, G. Stahl, B. Grima, H. Liu, M. Cassan, and J.P. Rousset In vivo HIV-1 frameshifting efficiency is directly related to the stability of the stem-loop stimulatory signal RNA 3 1997 1153 1158
    • (1997) RNA , vol.3 , pp. 1153-1158
    • Bidou, L.1    Stahl, G.2    Grima, B.3    Liu, H.4    Cassan, M.5    Rousset, J.P.6
  • 4
    • 1842843162 scopus 로고    scopus 로고
    • The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14-I31) is dispensable for the virus in vitro
    • G. Bleiber, S. Peters, R. Martinez, D. Cmarko, P. Meylan, and A. Telenti The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14-I31) is dispensable for the virus in vitro J. Gen. Virol. 85 2004 921 927
    • (2004) J. Gen. Virol. , vol.85 , pp. 921-927
    • Bleiber, G.1    Peters, S.2    Martinez, R.3    Cmarko, D.4    Meylan, P.5    Telenti, A.6
  • 5
    • 0029091681 scopus 로고
    • Ribosomal frameshifting viral RNAs
    • I. Brierley Ribosomal frameshifting viral RNAs J. Gen. Virol. 76 1995 1885 1892
    • (1995) J. Gen. Virol. , vol.76 , pp. 1885-1892
    • Brierley, I.1
  • 6
    • 0028031976 scopus 로고
    • Translational frameshifting at the gag-pol junction of human immunodeficiency virus type 1 is not increased in infected T-lymphoid cells
    • M. Cassan, N. Delaunay, C. Vaquero, and J. Rousset Translational frameshifting at the gag-pol junction of human immunodeficiency virus type 1 is not increased in infected T-lymphoid cells J. Virol. 68 1994 1501 1508
    • (1994) J. Virol. , vol.68 , pp. 1501-1508
    • Cassan, M.1    Delaunay, N.2    Vaquero, C.3    Rousset, J.4
  • 7
    • 0035112594 scopus 로고    scopus 로고
    • Extended nucleocapsid protein is cleaved from the Gag-Pol precursor of human immunodeficiency virus type 1
    • N. Chen, A. Morag, N. Almog, I. Blumenzweig, O. Dreazin, and M. Kotler Extended nucleocapsid protein is cleaved from the Gag-Pol precursor of human immunodeficiency virus type 1 J. Gen. Virol. 82 2001 581 590
    • (2001) J. Gen. Virol. , vol.82 , pp. 581-590
    • Chen, N.1    Morag, A.2    Almog, N.3    Blumenzweig, I.4    Dreazin, O.5    Kotler, M.6
  • 8
    • 0028345852 scopus 로고
    • Proteolytic processing mechanisms of a miniprecursor of the aspartic protease of human immunodeficiency virus type 1
    • E. Co, G. Koelsch, Y. Lin, E. Ido, J.A. Hartsuck, and J. Tang Proteolytic processing mechanisms of a miniprecursor of the aspartic protease of human immunodeficiency virus type 1 Biochemistry 33 1994 1248 1254
    • (1994) Biochemistry , vol.33 , pp. 1248-1254
    • Co, E.1    Koelsch, G.2    Lin, Y.3    Ido, E.4    Hartsuck, J.A.5    Tang, J.6
  • 9
    • 2342569731 scopus 로고    scopus 로고
    • Nef binds p6* in GagPol during replication of human immunodeficiency virus type 1
    • L.J. Costa, Y.-H. Zeng, J. Sabotic, J. Mak, O.T. Fackler, and B.M. Peterlin Nef binds p6* in GagPol during replication of human immunodeficiency virus type 1 J. Virol. 78 2004 5311 5323
    • (2004) J. Virol. , vol.78 , pp. 5311-5323
    • Costa, L.J.1    Zeng, Y.-H.2    Sabotic, J.3    Mak, J.4    Fackler, O.T.5    Peterlin, B.M.6
  • 10
    • 0002929101 scopus 로고
    • A model for evolutionary change in proteins
    • M.O. Dayhoff Natl. Biomed. Res. Found Washington, DC
    • M.O. Dayhoff, R. von Eck, and C.M. Park A model for evolutionary change in proteins M.O. Dayhoff Atlas of Protein Sequence and Structure vol. 5 1972 Natl. Biomed. Res. Found Washington, DC 89 99
    • (1972) Atlas of Protein Sequence and Structure , vol.5 , pp. 89-99
    • Dayhoff, M.O.1    Von Eck, R.2    Park, C.M.3
  • 11
    • 0033060752 scopus 로고    scopus 로고
    • Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins
    • M. Dettenhofer, and X.F. Yu Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins J. Virol. 73 1999 4696 4704
    • (1999) J. Virol. , vol.73 , pp. 4696-4704
    • Dettenhofer, M.1    Yu, X.F.2
  • 12
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • E.O. Freed HIV-1 gag proteins: diverse functions in the virus life cycle Virology 251 1998 1 15
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 14
    • 0022460420 scopus 로고
    • Regulation of human interleukin-2 gene: Functional DNA sequences in the 5′ flanking region for the gene expression in activated T-lymphocytes
    • T. Fujita, H. Shibuya, T. Ohashi, K. Yamanishi, and T. Taniguchi Regulation of human interleukin-2 gene: functional DNA sequences in the 5′ flanking region for the gene expression in activated T-lymphocytes Cell 46 1986 401 405
    • (1986) Cell , vol.46 , pp. 401-405
    • Fujita, T.1    Shibuya, H.2    Ohashi, T.3    Yamanishi, K.4    Taniguchi, T.5
  • 15
    • 84862448860 scopus 로고    scopus 로고
    • HIV-1 Gag: A molecular machine driving viral particle assembly and release
    • Göttlinger, H., 2001. HIV-1 Gag: a molecular machine driving viral particle assembly and release, HIV Database Review Articles.
    • (2001) HIV Database Review Articles
    • Göttlinger, H.1
  • 16
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • F.L. Graham, and A.J. van der Eb A new technique for the assay of infectivity of human adenovirus 5 DNA Virology 52 1973 456 467
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 17
    • 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
    • L.E. Henderson, M.A. Bowers, R.C. Sowder, S.A. Serabyn, D.G. Johnson, J.W. Bess, L.O. Arthur, D.K. Bryant, and C. Fenselau 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 1992 1856 1865
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder, R.C.3    Serabyn, S.A.4    Johnson, D.G.5    Bess, J.W.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 19
    • 0029146144 scopus 로고
    • RNA signals for translation frameshift: Influence of stem size and slippery sequence
    • A. Honda, T. Nakamura, and S. Nishimura RNA signals for translation frameshift: influence of stem size and slippery sequence Biochem. Biophys. Res. Commun. 213 1995 575 582
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 575-582
    • Honda, A.1    Nakamura, T.2    Nishimura, S.3
  • 20
    • 0023870815 scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • T. Jacks, M.D. Power, F.R. Masiarz, P.A. Luciw, P.J. Barr, and H.E. Varmus Characterization of ribosomal frameshifting in HIV-1 gag-pol expression Nature 331 1988 280 283
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3    Luciw, P.A.4    Barr, P.J.5    Varmus, H.E.6
  • 21
    • 0025828543 scopus 로고
    • Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments
    • A.H. Kaplan, and R. Swanstrom Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments Proc. Natl. Acad. Sci. U.S.A. 88 1991 4528 4532
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4528-4532
    • Kaplan, A.H.1    Swanstrom, R.2
  • 22
    • 0024594612 scopus 로고
    • Retrovirus protease characterized as a dimeric aspartic proteinase
    • I. Katoh, Y. Ikawa, and Y. Yoshinaka Retrovirus protease characterized as a dimeric aspartic proteinase J. Virol. 63 1989 2226 2232
    • (1989) J. Virol. , vol.63 , pp. 2226-2232
    • Katoh, I.1    Ikawa, Y.2    Yoshinaka, Y.3
  • 24
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene
    • J. Kimpton, and M. Emerman Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene J. Virol. 66 1992 2232 2239
    • (1992) J. Virol. , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 25
    • 0027941188 scopus 로고
    • The sequences of and distance between two cis-acting signals determine the efficiency of ribosomal frameshifting in human immunodeficiency virus type 1 and human T-cell leukemia virus type II in vivo
    • H. Kollmus, A. Honigman, A. Panet, and H. Hauser The sequences of and distance between two cis-acting signals determine the efficiency of ribosomal frameshifting in human immunodeficiency virus type 1 and human T-cell leukemia virus type II in vivo J. Virol. 68 1994 6087 6091
    • (1994) J. Virol. , vol.68 , pp. 6087-6091
    • Kollmus, H.1    Honigman, A.2    Panet, A.3    Hauser, H.4
  • 26
    • 0026757343 scopus 로고
    • Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active
    • M. Kotler, G. Arad, and S.H. Hughes Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active J. Virol. 66 1992 6781 6783
    • (1992) J. Virol. , vol.66 , pp. 6781-6783
    • Kotler, M.1    Arad, G.2    Hughes, S.H.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0029417217 scopus 로고
    • gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes
    • gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes Virology 214 1995 624 627
    • (1995) Virology , vol.214 , pp. 624-627
    • Lindhofer, H.1    Von Der Helm, K.2    Nitschko, H.3
  • 29
    • 0027936212 scopus 로고
    • Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein
    • J.M. Louis, N.T. Nashed, K.D. Parris, A.R. Kimmel, and D.M. Jerina Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein Proc. Natl. Acad. Sci. U.S.A. 91 1994 7970 7974
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7970-7974
    • Louis, J.M.1    Nashed, N.T.2    Parris, K.D.3    Kimmel, A.R.4    Jerina, D.M.5
  • 30
    • 0032562202 scopus 로고    scopus 로고
    • Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease
    • J.M. Louis, F. Dyda, N.T. Nashed, A.R. Kimmel, and D.R. Davies Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease Biochemistry 37 1998 2105 2110
    • (1998) Biochemistry , vol.37 , pp. 2105-2110
    • Louis, J.M.1    Dyda, F.2    Nashed, N.T.3    Kimmel, A.R.4    Davies, D.R.5
  • 31
    • 17444392445 scopus 로고    scopus 로고
    • Autoprocessing of HIV-1 protease is tightly coupled to protein folding
    • J.M. Louis, G.M. Clore, and A.M. Gronenborn Autoprocessing of HIV-1 protease is tightly coupled to protein folding Nat. Struct. Biol. 6 1999 868 875
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 868-875
    • Louis, J.M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 32
  • 34
    • 0030407681 scopus 로고    scopus 로고
    • Comparative morphology and structural classification of retroviruses
    • M.V. Nermut, and D.J. Hockley Comparative morphology and structural classification of retroviruses Curr. Top. Microbiol. Immunol. 214 1996 1 24
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 1-24
    • Nermut, M.V.1    Hockley, D.J.2
  • 35
    • 0033956191 scopus 로고    scopus 로고
    • Functional association between the nef gene product and gag-pol region of HIV-1
    • T. Ono, Y. Iwatani, A. Nishimura, A. Ishimoto, and H. Sakai Functional association between the nef gene product and gag-pol region of HIV-1 FEBS Lett. 466 2000 233 238
    • (2000) FEBS Lett. , vol.466 , pp. 233-238
    • Ono, T.1    Iwatani, Y.2    Nishimura, A.3    Ishimoto, A.4    Sakai, H.5
  • 36
    • 0026717107 scopus 로고
    • Human immunodeficiency virus type 1 gag-pol frameshifting is dependent on downstream mRNA secondary structure: Demonstration by expression in vivo
    • N.T. Parkin, M. Chamorro, and H.E. Varmus Human immunodeficiency virus type 1 gag-pol frameshifting is dependent on downstream mRNA secondary structure: demonstration by expression in vivo J. Virol. 66 1992 5147 5151
    • (1992) J. Virol. , vol.66 , pp. 5147-5151
    • Parkin, N.T.1    Chamorro, M.2    Varmus, H.E.3
  • 37
    • 0025728270 scopus 로고
    • Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1
    • K. Partin, G. Zybarth, L. Ehrlich, M. DeCrombrugghe, E. Wimmer, and C. Carter Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1 Proc. Natl. Acad. Sci. U.S.A. 88 1991 4776 4780
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4776-4780
    • Partin, K.1    Zybarth, G.2    Ehrlich, L.3    Decrombrugghe, M.4    Wimmer, E.5    Carter, C.6
  • 38
    • 0033618280 scopus 로고    scopus 로고
    • Competitive inhibition of immunodeficiency virus type-1 protease by the Gag-Pol transframe protein*
    • C. Paulus, S. Hellebrand, U. Tessmer, H. Wolf, H.-G. Kräusslich, and R. Wagner Competitive inhibition of immunodeficiency virus type-1 protease by the Gag-Pol transframe protein* J. Biol. Chem. 274 1999 21539 21543
    • (1999) J. Biol. Chem. , vol.274 , pp. 21539-21543
    • Paulus, C.1    Hellebrand, S.2    Tessmer, U.3    Wolf, H.4    Kräusslich, H.-G.5    Wagner, R.6
  • 39
    • 0037213627 scopus 로고    scopus 로고
    • The dimer interface of protease and extra-protease domains influence the activation of protease and the specificity of Gag-Pol cleavage
    • S.C. Pettit, S. Gulnik, L. Everitt, and A.H. Kaplan The dimer interface of protease and extra-protease domains influence the activation of protease and the specificity of Gag-Pol cleavage J. Virol. 77 2003 366 374
    • (2003) J. Virol. , vol.77 , pp. 366-374
    • Pettit, S.C.1    Gulnik, S.2    Everitt, L.3    Kaplan, A.H.4
  • 40
    • 0026620457 scopus 로고
    • Intrinsic activity of precursor forms of HIV-1 proteinase
    • L.H. Phylip, J.S. Mills, B.F. Parten, B.M. Dunn, and J. Kay Intrinsic activity of precursor forms of HIV-1 proteinase FEBS Lett. 314 1992 449 454
    • (1992) FEBS Lett. , vol.314 , pp. 449-454
    • Phylip, L.H.1    Mills, J.S.2    Parten, B.F.3    Dunn, B.M.4    Kay, J.5
  • 42
    • 0025105912 scopus 로고
    • Test system for determination of HIV-1 frameshifting efficiency in animal cells
    • H. Reil, and H. Hauser Test system for determination of HIV-1 frameshifting efficiency in animal cells Biochim. Biophys. Acta 1050 1990 288 292
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 288-292
    • Reil, H.1    Hauser, H.2
  • 43
    • 0027176380 scopus 로고
    • A heptanucleotide sequence mediates ribosomal frameshifting in mammalian cells
    • H. Reil, H. Kollmus, U.H. Weidle, and H. Hauser A heptanucleotide sequence mediates ribosomal frameshifting in mammalian cells J. Virol. 67 1993 5579 5584
    • (1993) J. Virol. , vol.67 , pp. 5579-5584
    • Reil, H.1    Kollmus, H.2    Weidle, U.H.3    Hauser, H.4
  • 44
    • 0028969065 scopus 로고
    • Defining the level of human immunodeficiency virus type 1 (HIV-1) protease activity required for HIV-1 particle maturation and infectivity
    • J.R. Rosé, L.M. Babé, and C.S. Craik Defining the level of human immunodeficiency virus type 1 (HIV-1) protease activity required for HIV-1 particle maturation and infectivity J. Virol. 69 1995 2751 2758
    • (1995) J. Virol. , vol.69 , pp. 2751-2758
    • Rosé, J.R.1    Babé, L.M.2    Craik, C.S.3
  • 45
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schägger, and G. von Jagow Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 46
    • 0014211618 scopus 로고
    • On the size of the active site in proteases: I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases: I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 48
    • 0036314316 scopus 로고    scopus 로고
    • Analysis of natural variants of the human immunodeficiency virus type 1 gag pol frameshift stem loop structure
    • A. Telenti, R. Martinez, M. Munoz, G. Bleiber, G. Greub, D. Sanglard, and S. Peters Analysis of natural variants of the human immunodeficiency virus type 1 gag pol frameshift stem loop structure J. Virol. 76 2002 7868 7873
    • (2002) J. Virol. , vol.76 , pp. 7868-7873
    • Telenti, A.1    Martinez, R.2    Munoz, M.3    Bleiber, G.4    Greub, G.5    Sanglard, D.6    Peters, S.7
  • 49
    • 2642680072 scopus 로고    scopus 로고
    • Cleavage of human immunodeficiency virus type 1 proteinase from the N terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity
    • U. Tessmer, and H.-G. Kräusslich Cleavage of human immunodeficiency virus type 1 proteinase from the N terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity J. Virol. 72 1998 3459 3463
    • (1998) J. Virol. , vol.72 , pp. 3459-3463
    • Tessmer, U.1    Kräusslich, H.-G.2
  • 50
    • 36849159719 scopus 로고
    • Retroviral protease like sequence in the yeast transposon Ty 1
    • H. Toh, M. Ono, K. Saigo, and T. Miyata Retroviral protease like sequence in the yeast transposon Ty 1 Nature 315 1985 691 692
    • (1985) Nature , vol.315 , pp. 691-692
    • Toh, H.1    Ono, M.2    Saigo, K.3    Miyata, T.4
  • 52
    • 0030419901 scopus 로고    scopus 로고
    • Proteolytic processing and particle maturation
    • V.M. Vogt Proteolytic processing and particle maturation Curr. Top. Microbiol. Immunol. 214 1996 95 131
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 95-131
    • Vogt, V.M.1
  • 53
    • 0024230701 scopus 로고
    • HIV expression strategies: Ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems
    • W. Wilson, M. Braddock, S.E. Adams, P.D. Rathjen, S.M. Kingsman, and A.J. Kingsman HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems Cell 55 1988 1159 1169
    • (1988) Cell , vol.55 , pp. 1159-1169
    • Wilson, W.1    Braddock, M.2    Adams, S.E.3    Rathjen, P.D.4    Kingsman, S.M.5    Kingsman, A.J.6
  • 54
    • 0025264973 scopus 로고
    • Production, mapping and biological characterization of monoclonal antibodies against core protein (p24) of the human immunodeficiency virus
    • H. Wolf, S. Modrow, E. Soutschek, M. Motz, R. Grunow, H. Döbl, and R. von Baehr Production, mapping and biological characterization of monoclonal antibodies against core protein (p24) of the human immunodeficiency virus AIDS-Forsch. 1 1990 16 18
    • (1990) AIDS-Forsch. , vol.1 , pp. 16-18
    • Wolf, H.1    Modrow, S.2    Soutschek, E.3    Motz, M.4    Grunow, R.5    Döbl, H.6    Von Baehr, R.7
  • 55
    • 0030066643 scopus 로고    scopus 로고
    • A transient precursor of the HIV 1 protease. Isolation, characterization, and kinetics of maturation
    • E.M. Wondrak, N.T. Nashed, M.T. Haber, D.M. Jerina, and J.M. Louis A transient precursor of the HIV 1 protease. Isolation, characterization, and kinetics of maturation J. Biol. Chem. 271 1996 4477 4481
    • (1996) J. Biol. Chem. , vol.271 , pp. 4477-4481
    • Wondrak, E.M.1    Nashed, N.T.2    Haber, M.T.3    Jerina, D.M.4    Louis, J.M.5
  • 57
    • 0029013602 scopus 로고
    • Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag Pol influence PR autoprocessing
    • G. Zybarth, and C. Carter Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag Pol influence PR autoprocessing J. Virol. 69 1995 3878 3884
    • (1995) J. Virol. , vol.69 , pp. 3878-3884
    • Zybarth, G.1    Carter, C.2
  • 58
    • 0027957918 scopus 로고
    • Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain
    • G. Zybarth, H.-G. Kräusslich, K. Partin, and C. Carter Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain J. Virol. 68 1994 240 250
    • (1994) J. Virol. , vol.68 , pp. 240-250
    • Zybarth, G.1    Kräusslich, H.-G.2    Partin, K.3    Carter, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.