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Volumn 71, Issue 10, 1997, Pages 7180-7186

The ectodomain of the human T-cell leukemia virus type 1 TM glycoprotein is involved in postfusion events

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

EID: 0030801229     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.10.7180-7186.1997     Document Type: Article
Times cited : (29)

References (73)
  • 2
    • 0026415343 scopus 로고
    • Coronavirus motif
    • Britton, P. 1991. Coronavirus motif. Nature 353:394.
    • (1991) Nature , vol.353 , pp. 394
    • Britton, P.1
  • 3
    • 0026742288 scopus 로고
    • Mutations within the env gene of Mason-Pfizer monkey virus: Ettects on protein transport and SU-TM association
    • Brody, B. A., and E. Hunter. 1992. Mutations within the env gene of Mason-Pfizer monkey virus: ettects on protein transport and SU-TM association. J. Virol. 66:3466-3475.
    • (1992) J. Virol. , vol.66 , pp. 3466-3475
    • Brody, B.A.1    Hunter, E.2
  • 4
    • 0028106370 scopus 로고
    • Mutations within the transmembrane glycoprotein of Mason-Pfizer monkey virus: Loss of SU-TM association and effects on infectivity
    • Brody, B. A., M. G. Kimball, and E. Hunter. 1994. Mutations within the transmembrane glycoprotein of Mason-Pfizer monkey virus: loss of SU-TM association and effects on infectivity. Virology 202:673-683.
    • (1994) Virology , vol.202 , pp. 673-683
    • Brody, B.A.1    Kimball, M.G.2    Hunter, E.3
  • 5
    • 0024968289 scopus 로고
    • Leucine zipper motif extends
    • Buckland, R., and F. Wild. 1989. Leucine ziPPer motif extends. Nature 338:547.
    • (1989) Nature , vol.338 , pp. 547
    • Buckland, R.1    Wild, F.2
  • 6
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0028932068 scopus 로고
    • Mutations within a putative cysteine loop of the transmembrane protein of an attenuated immunodeficiency-inducing feline leukemia virus variant inhibit envelope protein processing
    • Burns, C. C., M. L. Poss, E. Thomas, and J. Overbaugh. 1995. Mutations within a putative cysteine loop of the transmembrane protein of an attenuated immunodeficiency-inducing feline leukemia virus variant inhibit envelope protein processing. J. Virol. 69:2126-2132.
    • (1995) J. Virol. , vol.69 , pp. 2126-2132
    • Burns, C.C.1    Poss, M.L.2    Thomas, E.3    Overbaugh, J.4
  • 8
    • 0025153242 scopus 로고
    • The prevalence of antibody to HTLV-I/II in United States plasma donors and in United States and French hemophiliacs
    • Canavaggio, M., G. Leckie, J. P. Allain, J. W. Steaffens, Y. Laurian, D. Brettler, and H. Lee. 1990. The prevalence of antibody to HTLV-I/II in United States plasma donors and in United States and French hemophiliacs. Transfusion 30:780-782.
    • (1990) Transfusion , vol.30 , pp. 780-782
    • Canavaggio, M.1    Leckie, G.2    Allain, J.P.3    Steaffens, J.W.4    Laurian, Y.5    Brettler, D.6    Lee, H.7
  • 9
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., L. Bergeron, E. Helseth, M. Thali, H. Repke, and J. Sodroski. 1993. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67:2747-2755.
    • (1993) J. Virol. , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 10
    • 0028300968 scopus 로고
    • Changes in the cytopathic effects of human immunodeficiency virus type 1 associated with a single amino acid alteration in the ectodomain of the gp41 transmembrane glycoprotein
    • Cao, J., B. Vasir, and J. G. Sodroski. 1994. Changes in the cytopathic effects of human immunodeficiency virus type 1 associated with a single amino acid alteration in the ectodomain of the gp41 transmembrane glycoprotein. J. Virol. 68:4662-4668.
    • (1994) J. Virol. , vol.68 , pp. 4662-4668
    • Cao, J.1    Vasir, B.2    Sodroski, J.G.3
  • 11
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 12
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 14
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C. H., T. J. Matthews, C. B. McDanal, D. P. Bolognesi, and M. L. Greenberg. 1995. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:3771-3777.
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 15
    • 0028107566 scopus 로고
    • Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41
    • Chen, S. S.-L. 1994. Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 68: 2002-2010.
    • (1994) J. Virol. , vol.68 , pp. 2002-2010
    • Chen, S.S.-L.1
  • 16
    • 0027266886 scopus 로고
    • Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein
    • Chen, S. S.-L., C.-N. Lee, W.-R. Lee, K. McIntosh, and T.-H. Lee. 1993. Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J. Virol. 67: 3615-3619.
    • (1993) J. Virol. , vol.67 , pp. 3615-3619
    • Chen, S.S.-L.1    Lee, C.-N.2    Lee, W.-R.3    McIntosh, K.4    Lee, T.-H.5
  • 17
    • 0022408821 scopus 로고
    • Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins
    • Cianciolo, G. J., T. D. Copeland, S. Oroszlan, and R. Snyderman. 1985. Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins. Science 230:453-455.
    • (1985) Science , vol.230 , pp. 453-455
    • Cianciolo, G.J.1    Copeland, T.D.2    Oroszlan, S.3    Snyderman, R.4
  • 18
    • 0026515141 scopus 로고
    • Complex splicing in the human T-cell leukemia virus (HTLV) family of retroviruses: Novel mRNAs and proteins produced by HTLV type I
    • Ciminale, V., G. N. Pavlakis, D. Derse, C. P. Cunningham, and B. K. Felber. 1992. Complex splicing in the human T-cell leukemia virus (HTLV) family of retroviruses: novel mRNAs and proteins produced by HTLV type I. J. Virol. 66:1737-1745.
    • (1992) J. Virol. , vol.66 , pp. 1737-1745
    • Ciminale, V.1    Pavlakis, G.N.2    Derse, D.3    Cunningham, C.P.4    Felber, B.K.5
  • 19
    • 0021071021 scopus 로고
    • Productive infection and cell-free transmission of human T-cell leukemia virus in a nonlymphoid cell line
    • Clapham, P., K. Nagy, R. Cheingsong-Popov, M. Exley, and R. A. Weiss. 1983. Productive infection and cell-free transmission of human T-cell leukemia virus in a nonlymphoid cell line. Science 222:1125-1127.
    • (1983) Science , vol.222 , pp. 1125-1127
    • Clapham, P.1    Nagy, K.2    Cheingsong-Popov, R.3    Exley, M.4    Weiss, R.A.5
  • 20
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen, B. R. 1987. Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol. 152:684-704.
    • (1987) Methods Enzymol. , vol.152 , pp. 684-704
    • Cullen, B.R.1
  • 21
    • 0026546746 scopus 로고
    • Conserved cysteine residues in the human immunodeficiency virus type 1 transmembrane envelope protein are essential for precursor envelope cleavage
    • Dedera, D., R. Gu, and L. Ratner. 1992. Conserved cysteine residues in the human immunodeficiency virus type 1 transmembrane envelope protein are essential for precursor envelope cleavage. J. Virol. 66:1207-1209.
    • (1992) J. Virol. , vol.66 , pp. 1207-1209
    • Dedera, D.1    Gu, R.2    Ratner, L.3
  • 22
    • 0028263918 scopus 로고
    • Identification of functional regions in the human T-cell leukemia virus type 1 SU glycoprotein
    • Delamarre, L., C. Pique, D. Pham, T. Tursz, and M.-C. Dokhélar. 1994. Identification of functional regions in the human T-cell leukemia virus type 1 SU glycoprotein, J. Virol. 68:3544-3549.
    • (1994) J. Virol. , vol.68 , pp. 3544-3549
    • Delamarre, L.1    Pique, C.2    Pham, D.3    Tursz, T.4    Dokhélar, M.-C.5
  • 24
    • 0031060136 scopus 로고    scopus 로고
    • A novel human T-leukemia virus type 1 cell-to-cell transmission assay permits definition of SU glycoprotein amino acids important for infectivity
    • Delamarre, L., A. R. Rosenberg, C. Pique, D. Pham, and M.-C. Dokhélar. 1997. A novel human T-leukemia virus type 1 cell-to-cell transmission assay permits definition of SU glycoprotein amino acids important for infectivity. J. Virol. 71:259-266.
    • (1997) J. Virol. , vol.71 , pp. 259-266
    • Delamarre, L.1    Rosenberg, A.R.2    Pique, C.3    Pham, D.4    Dokhélar, M.-C.5
  • 25
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat
    • Delwart, E. L., G. Mosialos, and T. Gilmore. 1990. Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat. AIDS Res. Hum. Retroviruses 6:703-706.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 26
    • 0029010763 scopus 로고
    • Influence of transmembrane domains on the fusogenic abilities of human and murine leukemia retrovirus envelopes
    • Denesvre, C., P. Sonigo, A. Corbin, H. Ellerbrok, and M. Sitbon. 1995. Influence of transmembrane domains on the fusogenic abilities of human and murine leukemia retrovirus envelopes. J. Virol. 69:4149-4157.
    • (1995) J. Virol. , vol.69 , pp. 4149-4157
    • Denesvre, C.1    Sonigo, P.2    Corbin, A.3    Ellerbrok, H.4    Sitbon, M.5
  • 27
    • 0028816439 scopus 로고
    • Virions released from cells transfected with a molecular clone of human T-cell leukemia virus type 1 give rise to primary and secondary infections of T cells
    • Derse, D., J. Mikovits, M. Polianova, B. K. Felber, and F. Ruscetti. 1995. Virions released from cells transfected with a molecular clone of human T-cell leukemia virus type 1 give rise to primary and secondary infections of T cells. J. Virol. 69:1907-1912.
    • (1995) J. Virol. , vol.69 , pp. 1907-1912
    • Derse, D.1    Mikovits, J.2    Polianova, M.3    Felber, B.K.4    Ruscetti, F.5
  • 28
    • 0028220152 scopus 로고
    • Identification of novel neutralization-inducing regions of the human T cell lymphotropic virus type I envelope glycoproteins with human HTLV-I-seropositive sera
    • Desgranges, C., S. Souche, J.-C. Vernant, D. Smadja, A. Vahlne, and P. Horal. 1994. Identification of novel neutralization-inducing regions of the human T cell lymphotropic virus type I envelope glycoproteins with human HTLV-I-seropositive sera. AIDS Res. Hum. Retroviruses 10:163-173.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 163-173
    • Desgranges, C.1    Souche, S.2    Vernant, J.-C.3    Smadja, D.4    Vahlne, A.5    Horal, P.6
  • 29
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., R. A. Lamb, J. K. Rose, and A. Helenius. 1993. Folding and assembly of viral membrane proteins. Virology 193:545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 31
    • 0026654559 scopus 로고
    • Complementation of murine cells for human immunodeficiency virus envelope/CD4-mediated fusion in human/murinc heterokaryons
    • Dragic, T., P. Charneau, F. Clavel, and M. Alizon. 1992. Complementation of murine cells for human immunodeficiency virus envelope/CD4-mediated fusion in human/murinc heterokaryons. J. Virol. 66:4794-4802.
    • (1992) J. Virol. , vol.66 , pp. 4794-4802
    • Dragic, T.1    Charneau, P.2    Clavel, F.3    Alizon, M.4
  • 32
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., S. J. Roberts, B. Brody, and E. Hunter. 1992. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:4748-4756.
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 33
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
    • Dubay, J. W., S. J. Roberts, B. H. Hahn, and E. Hunter. 1992. Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity. J. Virol. 66:6616-6625.
    • (1992) J. Virol. , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 34
    • 0026600904 scopus 로고
    • Infection of peripheral blood mononuclear cells and cell lines by cell-free human T-cell lymphoma/leukemia virus type I
    • Fan, N., J. Gavalchin, B. Paul, K. H. Wells, M. J. Lane, and B. J. Poiesz. 1992. Infection of peripheral blood mononuclear cells and cell lines by cell-free human T-cell lymphoma/leukemia virus type I. J. Clin. Microbiol. 30:905-910.
    • (1992) J. Clin. Microbiol. , vol.30 , pp. 905-910
    • Fan, N.1    Gavalchin, J.2    Paul, B.3    Wells, K.H.4    Lane, M.J.5    Poiesz, B.J.6
  • 35
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Å resolution
    • Fass, D., S. C. Harrison, and P. S. Kim. 1996. Retrovirus envelope domain at 1.7 Å resolution. Nat. Struct. Biol. 3:465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 36
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E. O., D. J. Myers, and R. Risser. 1990. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl. Acad. Sci. USA 87:4650-4654.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 37
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda, D. H., A. Lever, E. Terwilliger, and J. Sodroski. 1992. Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 66:3306-3315.
    • (1992) J. Virol. , vol.66 , pp. 3306-3315
    • Gabuzda, D.H.1    Lever, A.2    Terwilliger, E.3    Sodroski, J.4
  • 39
    • 0021995980 scopus 로고
    • Antibodies to human T-lymphotropic virus type-I in patients with tropical spastic paraparesis
    • Gessain, A., F. Barin, J. C. Vernant, O. Gout, L. Maurs, A. Calender, and G. de Thé. 1985. Antibodies to human T-lymphotropic virus type-I in patients with tropical spastic paraparesis. Lancet ii:407-410.
    • (1985) Lancet , vol.2 , pp. 407-410
    • Gessain, A.1    Barin, F.2    Vernant, J.C.3    Gout, O.4    Maurs, L.5    Calender, A.6    De Thé, G.7
  • 40
    • 0019351935 scopus 로고
    • SV40-transformed simian cells support the replication of early SV40 mutants
    • Gluzman, Y. 1981. SV40-transformed simian cells support the replication of early SV40 mutants. Cell 23:175-182.
    • (1981) Cell , vol.23 , pp. 175-182
    • Gluzman, Y.1
  • 41
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P. B., T. Zhang, P. S. Kim, and T. Alber. 1993. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 42
    • 0025268873 scopus 로고
    • Rapid complementation assays measuring replicative potential of human immunodeficiency virus type 1 envelope glycoprotein mutants
    • Helseth, E., M. Kowalski, D. Gabuzda, U. Olshevsky, W. Haseltine, and J. Sodroski, 1990. Rapid complementation assays measuring replicative potential of human immunodeficiency virus type 1 envelope glycoprotein mutants. J. Virol. 64:2416-2420.
    • (1990) J. Virol. , vol.64 , pp. 2416-2420
    • Helseth, E.1    Kowalski, M.2    Gabuzda, D.3    Olshevsky, U.4    Haseltine, W.5    Sodroski, J.6
  • 43
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth, E., U. Olshevsky, C. Furman, and J. Sodroski. 1991. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65:2119-2123.
    • (1991) J. Virol. , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 45
    • 0025864155 scopus 로고
    • The N-terminal 31 amino acids of human immunodeficiency virus type 1 envelope protein gp120 contain a potential gp41 contact site
    • Ivey-Hoyle, M., R. K. Clark, and M. Rosenberg. 1991. The N-terminal 31 amino acids of human immunodeficiency virus type 1 envelope protein gp120 contain a potential gp41 contact site. J. Virol. 65:2682-2685.
    • (1991) J. Virol. , vol.65 , pp. 2682-2685
    • Ivey-Hoyle, M.1    Clark, R.K.2    Rosenberg, M.3
  • 47
    • 0027203897 scopus 로고
    • Inhibition of HIV-l infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein gp41
    • Jiang, S., K. Lin, N. Strick, and A. R. Neurath. 1993. Inhibition of HIV-l infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein gp41. Biochem. Biophys. Res. Commun. 195:533-538.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 533-538
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 48
    • 0343174876 scopus 로고
    • Envelope proteins of human T-cell leukemia virus: Expression in Escherichia coli and its application to studies of env gene functions
    • Kiyokawa, T., H. Yoshikura, S. Hattori, M. Seiki, and M. Yoshida. 1984. Envelope proteins of human T-cell leukemia virus: expression in Escherichia coli and its application to studies of env gene functions. Proc. Natl. Acad. Sci. USA 81:6202-6206.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6202-6206
    • Kiyokawa, T.1    Yoshikura, H.2    Hattori, S.3    Seiki, M.4    Yoshida, M.5
  • 49
    • 0025958921 scopus 로고
    • Attenuation of human immunodeficiency virus type 1 cytopathic effect by a mutation affecting the transmembrane envelope glycoprotein
    • Kowalski, M., L. Bergeron, T. Dorfman, W. Haseltine, and J. Sodroski. 1991. Attenuation of human immunodeficiency virus type 1 cytopathic effect by a mutation affecting the transmembrane envelope glycoprotein. J. Virol. 65: 281-291.
    • (1991) J. Virol. , vol.65 , pp. 281-291
    • Kowalski, M.1    Bergeron, L.2    Dorfman, T.3    Haseltine, W.4    Sodroski, J.5
  • 51
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 52
    • 0025957564 scopus 로고
    • Pseudotyping with human T-cell leukemia virus type 1 broadens the human immunodeficiency virus host range
    • Landau, N. R., K. A. Page, and D. R. Littman. 1991. Pseudotyping with human T-cell leukemia virus type 1 broadens the human immunodeficiency virus host range. J. Virol. 65:162-169.
    • (1991) J. Virol. , vol.65 , pp. 162-169
    • Landau, N.R.1    Page, K.A.2    Littman, D.R.3
  • 54
    • 0028168944 scopus 로고
    • Structural rearrangements in the transmembrane glycoprotein after receptor binding
    • Matthews, T. J., C. Wild, C.-H. Chen, D. P. Bolognesi, and M. L. Greenberg. 1994. Structural rearrangements in the transmembrane glycoprotein after receptor binding. Immunol. Rev. 140:93-104.
    • (1994) Immunol. Rev. , vol.140 , pp. 93-104
    • Matthews, T.J.1    Wild, C.2    Chen, C.-H.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 55
    • 0021206551 scopus 로고
    • A retrospective study on transmission of adult T cell leukemia virus by blood transfusion: Seroconversion in recipients
    • Okochi, K., H. Sato, and Y. Hinuma. 1984. A retrospective study on transmission of adult T cell leukemia virus by blood transfusion: seroconversion in recipients. Vox Sang. 46:245-253.
    • (1984) Vox Sang. , vol.46 , pp. 245-253
    • Okochi, K.1    Sato, H.2    Hinuma, Y.3
  • 57
    • 0028903355 scopus 로고
    • Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein
    • Pancino, G., L. Camoin, and P. Sonigo. 1995. Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein. J. Virol. 69:2110-2118.
    • (1995) J. Virol. , vol.69 , pp. 2110-2118
    • Pancino, G.1    Camoin, L.2    Sonigo, P.3
  • 58
    • 0021756566 scopus 로고
    • Similarities among retrovirus proteins
    • Patarca, R., and W. A. Haseltine. 1984. Similarities among retrovirus proteins. Nature 312:496.
    • (1984) Nature , vol.312 , pp. 496
    • Patarca, R.1    Haseltine, W.A.2
  • 59
    • 0027402614 scopus 로고
    • The cytoplasmic domain of the human T-cell leukemia virus type 1 envelope can modulate envelope functions in a cell type-dependent manner
    • Pique, C., D. Pham, T. Tursz, and M.-C. Dokhélar. 1993. The cytoplasmic domain of the human T-cell leukemia virus type 1 envelope can modulate envelope functions in a cell type-dependent manner. J. Virol. 67:557-561.
    • (1993) J. Virol. , vol.67 , pp. 557-561
    • Pique, C.1    Pham, D.2    Tursz, T.3    Dokhélar, M.-C.4
  • 60
    • 0026542792 scopus 로고
    • Human T-cell leukemia virus type 1 envelope protein maturation process: Requirements for syncytium formation
    • Pique, C., D. Pham, T. Tursz, and M.-C. Dokhélar. 1992. Human T-cell leukemia virus type 1 envelope protein maturation process: requirements for syncytium formation. J. Virol. 66:906-913.
    • (1992) J. Virol. , vol.66 , pp. 906-913
    • Pique, C.1    Pham, D.2    Tursz, T.3    Dokhélar, M.-C.4
  • 61
    • 0025608577 scopus 로고
    • Mutations introduced along the HTLV-I envelope gene result in a non-functional protein: A basis for envelope conservation?
    • Pique, C., T. Tursz, and M.-C. Dokhélar. 1990. Mutations introduced along the HTLV-I envelope gene result in a non-functional protein: a basis for envelope conservation? EMBO J. 9:4243-4248.
    • (1990) EMBO J. , vol.9 , pp. 4243-4248
    • Pique, C.1    Tursz, T.2    Dokhélar, M.-C.3
  • 62
    • 0019254359 scopus 로고
    • Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma
    • Poiesz, B. J., F. W. Ruscetti, A. F. Gazdar, P. A. Bunn, J. D. Minna, and R. C. Gallo. 1980. Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma. Proc. Natl. Acad. Sci. USA 77:7415-7419.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7415-7419
    • Poiesz, B.J.1    Ruscetti, F.W.2    Gazdar, A.F.3    Bunn, P.A.4    Minna, J.D.5    Gallo, R.C.6
  • 64
    • 0026739609 scopus 로고
    • Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?
    • Schulz, T. F., B. A. Jameson, L. Lopalco, A. G. Siccardi, R. A. Weiss, and J. P. Moore. 1992. Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins? AIDS Res. Hum. Retroviruses 8:1571-1580.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 1571-1580
    • Schulz, T.F.1    Jameson, B.A.2    Lopalco, L.3    Siccardi, A.G.4    Weiss, R.A.5    Moore, J.P.6
  • 65
    • 1542686422 scopus 로고
    • Human adult T-cell leukemia virus: Complete nucleotide sequence of the provirus genome integrated in leukemia cell DMA
    • Seiki, M., S. Hattori, Y. Hirayama, and M. Yoshida. 1983. Human adult T-cell leukemia virus: complete nucleotide sequence of the provirus genome integrated in leukemia cell DMA. Proc. Natl. Acad. Sci. USA 80:3618-3622.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3618-3622
    • Seiki, M.1    Hattori, S.2    Hirayama, Y.3    Yoshida, M.4
  • 66
    • 0026735967 scopus 로고
    • Role of the fusogenic peptide sequence in syncytium induction and infectivity of human immunodeficiency virus type 2
    • Steffy, K. R., G. Kraus, D. J. Looney, and F. Wong-Staal. 1992. Role of the fusogenic peptide sequence in syncytium induction and infectivity of human immunodeficiency virus type 2. J. Virol. 66:4532-4535.
    • (1992) J. Virol. , vol.66 , pp. 4532-4535
    • Steffy, K.R.1    Kraus, G.2    Looney, D.J.3    Wong-Staal, F.4
  • 67
    • 0025996335 scopus 로고
    • Role of conserved gp41 cysteine residues in the processing of human immunodeficiency virus envelope precursor and viral infectivity
    • Syu, W.-J., W.-R. Lee, B. Du, Q.-C. Yu, M. Essex, and T.-H. Lee. 1991. Role of conserved gp41 cysteine residues in the processing of human immunodeficiency virus envelope precursor and viral infectivity. J. Virol. 65:6349-6352.
    • (1991) J. Virol. , vol.65 , pp. 6349-6352
    • Syu, W.-J.1    Lee, W.-R.2    Du, B.3    Yu, Q.-C.4    Essex, M.5    Lee, T.-H.6
  • 69
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., J. W. Dubay, T. Greenwell, T. Baird, Jr., T. G. Oas, C. McDaual, E. Hunter, and T. Matthews. 1994. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDaual, C.6    Hunter, E.7    Matthews, T.8
  • 70
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure
    • Wild, C., T. Greenwell, D. Shugars, L. Rimsky-Clarke, and T. Matthews. 1995. The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Retroviruses 11:323-325.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 71
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 72
    • 0020000678 scopus 로고
    • Transformation of human leukocytes by cocultivation with an adult T cell leukemia virus producer cell line
    • Yamamoto, N., M. Okada, Y. Koyanagi, M. Kannagi, and Y. Hinuma. 1982. Transformation of human leukocytes by cocultivation with an adult T cell leukemia virus producer cell line. Science 217:737-739.
    • (1982) Science , vol.217 , pp. 737-739
    • Yamamoto, N.1    Okada, M.2    Koyanagi, Y.3    Kannagi, M.4    Hinuma, Y.5
  • 73
    • 0000904435 scopus 로고
    • Isolation and characterization of retrovirus from cell lines of human adult T-cell leukemia and its implication in the disease
    • Yoshida, M., I. Miyoshi, and Y. Hinuma. 1982. Isolation and characterization of retrovirus from cell lines of human adult T-cell leukemia and its implication in the disease. Proc. Natl. Acad. Sci. USA 79:2031-2035.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2031-2035
    • Yoshida, M.1    Miyoshi, I.2    Hinuma, Y.3


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