메뉴 건너뛰기




Volumn 8, Issue 6, 1998, Pages 717-723

Development of an in vitro Assay System for Screening of gp41 Inhibitory Compounds

Author keywords

gp41; HIV; In vitro Assay; Inhibitor

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; GLUTATHIONE TRANSFERASE; GLYCOPROTEIN GP 41; HYBRID PROTEIN; PEPTIDE FRAGMENT; THIOREDOXIN;

EID: 0032585364     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (13)

References (25)
  • 1
    • 0026434572 scopus 로고
    • Receptor-mediated activation of immunodeficiency viruses in viral fusion
    • Allan, J. S. (1991) Receptor-mediated activation of immunodeficiency viruses in viral fusion. Science 252, 1322-1323.
    • (1991) Science , vol.252 , pp. 1322-1323
    • Allan, J.S.1
  • 2
    • 0028023726 scopus 로고
    • The structure of influenza hemagglutinine at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994) The structure of influenza hemagglutinine 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
  • 3
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (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
  • 4
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a "leucine zipper "-like repeat
    • Delwart, E. L., Mosialos, G., and Gilmore, T. (1990) Retroviral envelope glycoproteins contain a "leucine zipper "-like repeat. AIDS Res. Hum. Ret. 6, 703-706.
    • (1990) AIDS Res. Hum. Ret. , vol.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 5
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, D., Broder, C. C., Kennedy, P. E., and Berger, E. A. (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 72, 872-877.
    • (1996) Science , vol.72 , pp. 872-877
    • Feng, D.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 6
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120
    • Hart, K. T., Kirsch, R., Ellens, H., Sweet, R. W., Lambert, D. M., Petteway, S. R. Jr., Learly, J., and Bugelski, P. J. (1991) Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120. Proc. Natl. Acad. Sci. USA 88, 2189-2193.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2189-2193
    • Hart, K.T.1    Kirsch, R.2    Ellens, H.3    Sweet, R.W.4    Lambert, D.M.5    Petteway Jr., S.R.6    Learly, J.7    Bugelski, P.J.8
  • 7
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 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
  • 8
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implication for the viral fusion mechanism
    • Judice, J. C., Tom, J. Y. K., Huang, W., Wrin, T., Vennari, J., Petropoulos, C. J., and McDowell, R. S. (1997) Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implication for the viral fusion mechanism. Proc. Natl. Acad. Sci. USA 94, 13426-13430.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13426-13430
    • Judice, J.C.1    Tom, J.Y.K.2    Huang, W.3    Wrin, T.4    Vennari, J.5    Petropoulos, C.J.6    McDowell, R.S.7
  • 9
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid peptide synthesis
    • King, D. S., Field, C. G., and Field, G. B. (1990) A cleavage method which minimizes side reactions following Fmoc solid peptide synthesis. Int. J. Peptide Protein Res. 36, 255-266.
    • (1990) Int. J. Peptide Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Field, C.G.2    Field, G.B.3
  • 10
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J., and Hendrickson, W. A. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 11
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41
    • Lawless, M. K., Barney, S., Guthrie, K. I., Bucy, T. B., Petteway, S. R., and Merutka, G. (1996) HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41. Biochemistry 35, 13697-13708.
    • (1996) Biochemistry , vol.35 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway, S.R.5    Merutka, G.6
  • 12
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C., and Kim, P. S. (1995) A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Structural Biology 2, 1075-1082.
    • (1995) Nature Structural Biology , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 13
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon, P. J., Dalgleish, A. G., McDougal, J. S., Clapham, P. R., Weiss, R. A., and Axel, R. (1986) The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 47, 333-348.
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.G.2    McDougal, J.S.3    Clapham, P.R.4    Weiss, R.A.5    Axel, R.6
  • 14
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 induced by soluble CD4
    • Moore, J. P., McKeating, J. A., Weiss, R., and Sattentau, Q. J. (1990) Dissociation of gp120 from HIV-1 induced by soluble CD4. Science 250, 1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.3    Sattentau, Q.J.4
  • 15
    • 0028129959 scopus 로고
    • Fusogenic mechanisms of the enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation
    • Nussbaum, O., Broder, C. C., and Berger, E. A. (1994) Fusogenic mechanisms of the enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68, 5411-5422.
    • (1994) J. Virol. , vol.68 , pp. 5411-5422
    • Nussbaum, O.1    Broder, C.C.2    Berger, E.A.3
  • 16
    • 0031058386 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoprotein oligomerization requires the gp41 amphipathic α-helical/leucine zipper-like sequence
    • Poumbourios, P., Wilson, K. A., Center, R. J., Ahmar, W. L., and Kemp, B. (1997) Human immunodeficiency virus type 1 envelope glycoprotein oligomerization requires the gp41 amphipathic α-helical/leucine zipper-like sequence. J. Virol. 71, 2041-2049.
    • (1997) J. Virol. , vol.71 , pp. 2041-2049
    • Poumbourios, P.1    Wilson, K.A.2    Center, R.J.3    Ahmar, W.L.4    Kemp, B.5
  • 17
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein, M. and Shin, Y.-K. (1995) A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 34, 13390-13397.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.-K.2
  • 18
    • 0021717961 scopus 로고
    • Molecular characterization of human T-cell leukemia (lymphotropic) virus type III in the acquired immune deficiency syndrome
    • Shaw, G. M., Hahn, B. H., Arya, S. K., Groopman, J. E., Gallo, R. C., and Wong-Staal, F. (1984) Molecular characterization of human T-cell leukemia (lymphotropic) virus type III in the acquired immune deficiency syndrome. Science 226, 1165-1171.
    • (1984) Science , vol.226 , pp. 1165-1171
    • Shaw, G.M.1    Hahn, B.H.2    Arya, S.K.3    Groopman, J.E.4    Gallo, R.C.5    Wong-Staal, F.6
  • 19
    • 0029964418 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • Shugars, D. C., Wild, C. T., Greenwell, T. K., and Matthews, T. J. (1996) Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 70, 2982-2991.
    • (1996) J. Virol. , vol.70 , pp. 2982-2991
    • Shugars, D.C.1    Wild, C.T.2    Greenwell, T.K.3    Matthews, T.J.4
  • 22
    • 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., Greenwell, T., Shugars, D., Rimsky-Clarke, L., Mathews, T. (1995) The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Ret. 11, 323-325.
    • (1995) AIDS Res. Hum. Ret. , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Mathews, T.5
  • 23
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., Oas, T., McDanal, C., Bolognesi, D., and Matthews, T. (1992) A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89, 10537-10641.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10641
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 24
    • 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., Shugars, D. C., Greenwell, T. K., McDanal, C. B., and Matthews, T (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.5
  • 25
    • 0002386888 scopus 로고    scopus 로고
    • Inhibition of gp120-CD4 interaction by various plant extracts
    • Woo, E.-R., Yoon, S. H., Kwak, J. H., Kim, H. J., and Park, H. (1997) Inhibition of gp120-CD4 interaction by various plant extracts. Phytomedicine 4, 53-58.
    • (1997) Phytomedicine , vol.4 , pp. 53-58
    • Woo, E.-R.1    Yoon, S.H.2    Kwak, J.H.3    Kim, H.J.4    Park, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.