메뉴 건너뛰기




Volumn 84, Issue 18, 2010, Pages 9359-9368

Identification of a gp41 core-binding molecule with homologous sequence of human TNNI3K-like protein as a novel human immunodeficiency virus type 1 entry inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; COMPLEMENTARY DNA; ENFUVIRTIDE; GLYCOPROTEIN GP 41; P 20; TROPONIN I TYPE 3 INTERACTING KINASE LIKE PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; GP41 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; PEPTIDE; PROTEIN BINDING; TNNI3K PROTEIN, HUMAN;

EID: 77956021159     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00644-10     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 34147170129 scopus 로고    scopus 로고
    • Targeting the sticky fingers of HIV-1
    • Blumenthal, R., and D. S. Dimitrov. 2007. Targeting the sticky fingers of HIV-1. Cell 129:243-245.
    • (2007) Cell , vol.129 , pp. 243-245
    • Blumenthal, R.1    Dimitrov, D.S.2
  • 3
    • 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
  • 4
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 5
    • 0033046030 scopus 로고    scopus 로고
    • Efficacy and safety analyses of a recombinant human immunodeficiency virus type 1 derived vector system
    • Chang, L. J., V. Urlacher, T. Iwakuma, Y. Cui, and J. Zucali. 1999. Efficacy and safety analyses of a recombinant human immunodeficiency virus type 1 derived vector system. Gene Ther. 6:715-728.
    • (1999) Gene Ther. , vol.6 , pp. 715-728
    • Chang, L.J.1    Urlacher, V.2    Iwakuma, T.3    Cui, Y.4    Zucali, J.5
  • 6
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou, T. C., and P. Talalay. 1984. Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv. Enzyme Regul. 22:27-55.
    • (1984) Adv. Enzyme Regul. , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 7
    • 0019321271 scopus 로고
    • Concentration-dependent effects of sodium-butyrate in Chinese-hamster cells-cell-cycle progression, inner-histone acetylation, histone H-1 dephosphorylation, and induction of an H1-like protein
    • D'Anna, J. A., R. A. Tobey, and L. R. Gurley. 1980. Concentration- dependent effects of sodium-butyrate in Chinese-hamster cells-cell-cycle progression, inner-histone acetylation, histone H-1 dephosphorylation, and induction of an H1-like protein. Biochemistry 19:2656-2671.
    • (1980) Biochemistry , vol.19 , pp. 2656-2671
    • D'Anna, J.A.1    Tobey, R.A.2    Gurley, L.R.3
  • 8
    • 0031470456 scopus 로고    scopus 로고
    • How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity
    • Dimitrov, D. S. 1997. How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity. Cell 91:721-730.
    • (1997) Cell , vol.91 , pp. 721-730
    • Dimitrov, D.S.1
  • 11
    • 33646078264 scopus 로고    scopus 로고
    • Interaction kinetic characterization of HIV-1 reverse transcriptase non-nucleoside inhibitor resistance
    • Geitmann, M., T. Unge, and U. H. Danielson. 2006. Interaction kinetic characterization of HIV-1 reverse transcriptase non-nucleoside inhibitor resistance. J. Med. Chem. 49:2375-2387.
    • (2006) J. Med. Chem. , vol.49 , pp. 2375-2387
    • Geitmann, M.1    Unge, T.2    Danielson, U.H.3
  • 12
    • 48949118733 scopus 로고    scopus 로고
    • HIV-I Vif, APOBEC, and intrinsic immunity
    • Goila-Gaur, R., and K. Strebel. 2008. HIV-I Vif, APOBEC, and intrinsic immunity. Retrovirology 5:51.
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 14
    • 0034046091 scopus 로고    scopus 로고
    • Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41
    • Gorny, M. K., and S. Zolla-Pazner. 2000. Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41. J. Virol. 74:6186-6192.
    • (2000) J. Virol. , vol.74 , pp. 6186-6192
    • Gorny, M.K.1    Zolla-Pazner, S.2
  • 15
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • Greenberg, M. L., and N. Cammack. 2004. Resistance to enfuvirtide, the first HIV fusion inhibitor. J. Antimicrob. Chemother. 54:333-340.
    • (2004) J. Antimicrob. Chemother. , vol.54 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 17
    • 33748185656 scopus 로고    scopus 로고
    • Identification of the HIV-1 gp41 core-binding motif-HXXNPF
    • Huang, J. H., Z. Q. Liu, S. Liu, S. Jiang, and Y. H. Chen. 2006. Identification of the HIV-1 gp41 core-binding motif-HXXNPF. FEBS Lett. 580:4807-4814.
    • (2006) FEBS Lett. , vol.580 , pp. 4807-4814
    • Huang, J.H.1    Liu, Z.Q.2    Liu, S.3    Jiang, S.4    Chen, Y.H.5
  • 18
    • 47249098487 scopus 로고    scopus 로고
    • Interaction of HIV-1 gp41 core with NPF motif in Epsin-implication in endocytosis of HIV
    • Huang, J. H., Z. Qi, F. Wu, L. Kotula, S. B. Jiang, and Y. H. Chen. 2008. Interaction of HIV-1 gp41 core with NPF motif in Epsin-implication in endocytosis of HIV. J. Biol. Chem. 283:14994-15002.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14994-15002
    • Huang, J.H.1    Qi, Z.2    Wu, F.3    Kotula, L.4    Jiang, S.B.5    Chen, Y.H.6
  • 19
    • 34247859078 scopus 로고    scopus 로고
    • The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation
    • Huang, J. H., H. W. Yang, S. Liu, J. Li, S. Jiang, and Y. H. Chen. 2007. The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation. Biochem. J. 403:565-571.
    • (2007) Biochem. J. , vol.403 , pp. 565-571
    • Huang, J.H.1    Yang, H.W.2    Liu, S.3    Li, J.4    Jiang, S.5    Chen, Y.H.6
  • 20
    • 0034708369 scopus 로고    scopus 로고
    • Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41
    • Jiang, S., and A. K. Debnath. 2000. Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41. Biochem. Biophys. Res. Commun. 269:641-646.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 641-646
    • Jiang, S.1    Debnath, A.K.2
  • 21
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang, S., K. Lin, and M. Lu. 1998. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 72:10213-10217.
    • (1998) J. Virol. , vol.72 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 23
    • 0027203897 scopus 로고
    • Inhibition of HIV-1 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-1 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
  • 24
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang, S., K. Lin, L. Zhang, and A. K. Debnath. 1999. A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 80:85-96.
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 25
    • 0025719310 scopus 로고
    • Enhancement of human immunodeficiency virus type 1 infection by antisera to peptides from the envelope glycoproteins gp120/gp41
    • Jiang, S. B., K. Lin, and A. R. Neurath. 1991. Enhancement of human immunodeficiency virus type 1 infection by antisera to peptides from the envelope glycoproteins gp120/gp41. J. Exp. Med. 174:1557-1563.
    • (1991) J. Exp. Med. , vol.174 , pp. 1557-1563
    • Jiang, S.B.1    Lin, K.2    Neurath, A.R.3
  • 26
    • 0038187684 scopus 로고    scopus 로고
    • Novel therapies based on mechanisms of HIV-1 cell entry
    • Kilby, J. M., and J. J. Eron. 2003. Novel therapies based on mechanisms of HIV-1 cell entry. N. Engl. J. Med. 348:2228-2238.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2228-2238
    • Kilby, J.M.1    Eron, J.J.2
  • 29
    • 0027163762 scopus 로고
    • Identification of mutations in p53 that affect its binding to SV40 large T antigen by using the yeast two-hybrid system
    • Li, B., and S. Fields. 1993. Identification of mutations in P53 that affect its binding to SV40 large T-antigen by using the yeast 2-hybrid system. FASEB J. 7:957-963. (Pubitemid 23225555)
    • (1993) FASEB Journal , vol.7 , Issue.10 , pp. 957-963
    • Li, B.1    Fields, S.2
  • 30
    • 58149522849 scopus 로고    scopus 로고
    • Identification of critical antibody-binding sites in the HIV-1 gp41 six-helix bundle core as potential targets for HIV-1 fusion inhibitors
    • Li, J., X. Chen, J. Huang, S. Jiang, and Y. H. Chen. 2009. Identification of critical antibody-binding sites in the HIV-1 gp41 six-helix bundle core as potential targets for HIV-1 fusion inhibitors. Immunobiology 214:51-60.
    • (2009) Immunobiology , vol.214 , pp. 51-60
    • Li, J.1    Chen, X.2    Huang, J.3    Jiang, S.4    Chen, Y.H.5
  • 31
    • 77951216905 scopus 로고    scopus 로고
    • 3-Hydroxyphthalic anhydride-modified chicken ovalbumin exhibits potent and broad anti-HIV-1 activity: A potential microbicide for preventing sexual transmission of HIV-1. Antimicrob
    • Li, L., L. He, S. Tan, X. Guo, H. Lu, Z. Qi, C. Pan, X. An, S. Jiang, and S. Liu. 2010. 3-Hydroxyphthalic anhydride-modified chicken ovalbumin exhibits potent and broad anti-HIV-1 activity: a potential microbicide for preventing sexual transmission of HIV-1. Antimicrob. Agents Chemother. 54:1700-1711.
    • (2010) Agents Chemother. , vol.54 , pp. 1700-1711
    • Li, L.1    He, L.2    Tan, S.3    Guo, X.4    Lu, H.5    Qi, Z.6    Pan, C.7    An, X.8    Jiang, S.9    Liu, S.10
  • 32
    • 33846173312 scopus 로고    scopus 로고
    • HIV entry inhibitors targeting gp41: From polypeptides to small-molecule compounds
    • Liu, S., S. Wu, and S. Jiang. 2007. HIV entry inhibitors targeting gp41: from polypeptides to small-molecule compounds. Curr. Pharm. Des. 13:143-162.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 143-162
    • Liu, S.1    Wu, S.2    Jiang, S.3
  • 33
    • 15744393651 scopus 로고    scopus 로고
    • Different from the HIV fusion inhibitor C34, the anti-HIV drug fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120
    • Liu, S. W., H. Lu, J. Niu, Y. J. Xu, S. G. Wu, and S. B. Jiang. 2005. Different from the HIV fusion inhibitor C34, the anti-HIV drug fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120. J. Biol. Chem. 280:11259-11273.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11259-11273
    • Liu, S.W.1    Lu, H.2    Niu, J.3    Xu, Y.J.4    Wu, S.G.5    Jiang, S.B.6
  • 34
    • 0346729750 scopus 로고    scopus 로고
    • Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: Applicable for identification of HIV-1 fusion inhibitors
    • Liu, S. W., Q. Zhao, and S. B. Jiang. 2003. Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: applicable for identification of HIV-1 fusion inhibitors. Peptides 24:1303-1313.
    • (2003) Peptides , vol.24 , pp. 1303-1313
    • Liu, S.W.1    Zhao, Q.2    Jiang, S.B.3
  • 35
    • 0442292287 scopus 로고    scopus 로고
    • Design and construction of a recombinant epitope-peptide gene as a universal epitope-vaccine strategy
    • Liu, Z., and Y. H. Chen. 2004. Design and construction of a recombinant epitope-peptide gene as a universal epitope-vaccine strategy. J. Immunol. Methods 285:93-97.
    • (2004) J. Immunol. Methods , vol.285 , pp. 93-97
    • Liu, Z.1    Chen, Y.H.2
  • 37
    • 47749086305 scopus 로고    scopus 로고
    • Surface exposure of the HIV-1 Env cytoplasmic tail LLP2 domain during the membrane fusion process-interaction with gp41 fusion core
    • Lu, L., Y. Zhu, J. H. Huang, X. Chen, H. W. Yang, S. B. Jiang, and Y. H. Chen. 2008. Surface exposure of the HIV-1 Env cytoplasmic tail LLP2 domain during the membrane fusion process-interaction with gp41 fusion core. J. Biol. Chem. 283:16723-16731.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16723-16731
    • Lu, L.1    Zhu, Y.2    Huang, J.H.3    Chen, X.4    Yang, H.W.5    Jiang, S.B.6    Chen, Y.H.7
  • 38
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 39
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi, K., Y. Kim, O. Latinovic, V. Morozov, and G. B. Melikyan. 2009. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137:433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 40
    • 2942622122 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of cellulose acetate phthalate: Synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles
    • Neurath, A. R., N. Strick, S. Jiang, Y. Y. Li, and A. K. Debnath. 2002. Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles. BMC Infect. Dis. 2:6.
    • (2002) BMC Infect. Dis. , vol.2 , pp. 6
    • Neurath, A.R.1    Strick, N.2    Jiang, S.3    Li, Y.Y.4    Debnath, A.K.5
  • 41
    • 20744446731 scopus 로고    scopus 로고
    • Design, expression, and immunogenicity of a soluble HIV trimeric envelope fragment adopting a prefusion gp41 configuration
    • Qiao, Z. S., M. Kim, B. Reinhold, D. Montefiori, J. H. Wang, and E. L. Reinherz. 2005. Design, expression, and immunogenicity of a soluble HIV trimeric envelope fragment adopting a prefusion gp41 configuration. J. Biol. Chem. 280:23138-23146.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23138-23146
    • Qiao, Z.S.1    Kim, M.2    Reinhold, B.3    Montefiori, D.4    Wang, J.H.5    Reinherz, E.L.6
  • 42
    • 37549010341 scopus 로고    scopus 로고
    • Survey of the year 2006 commercial optical biosensor literature
    • Rich, R. L., and D. G. Myszka. 2007. Survey of the year 2006 commercial optical biosensor literature. J. Mol. Recognit. 20:300-366.
    • (2007) J. Mol. Recognit. , vol.20 , pp. 300-366
    • Rich, R.L.1    Myszka, D.G.2
  • 43
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 44
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., M. S. Kay, and P. S. Kim. 2001. Protein design of an HIV-1 entry inhibitor. Science 291:884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 47
  • 48
    • 34447317534 scopus 로고    scopus 로고
    • The control of viral infection by tripartite motif proteins and cyclophilin A
    • Towers, G. J. 2007. The control of viral infection by tripartite motif proteins and cyclophilin A. Retrovirology 4:40.
    • (2007) Retrovirology , vol.4 , pp. 40
    • Towers, G.J.1
  • 52
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild, C., T. Greenwell, and T. Matthews. 1993. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retrovir. 9:1051-1053.
    • (1993) AIDS Res. Hum. Retrovir. , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 53
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-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 alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 54
    • 0026055421 scopus 로고
    • Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies
    • Xu, J. Y., M. K. Gorny, T. Palker, S. Karwowska, and S. Zolla-Pazner. 1991. Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies. J. Virol. 65:4832-4838.
    • (1991) J. Virol. , vol.65 , pp. 4832-4838
    • Xu, J.Y.1    Gorny, M.K.2    Palker, T.3    Karwowska, S.4    Zolla-Pazner, S.5
  • 55
    • 0037119027 scopus 로고    scopus 로고
    • Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients
    • DOI 10.1097/00002030-200208160-00016
    • Xu, L., S. Hue, S. Taylor, D. Ratcliffe, J. A. Workman, S. Jackson, P. A. Cane, and D. Pillay. 2002. Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients. AIDS 16:1684-1686. (Pubitemid 34921116)
    • (2002) AIDS , vol.16 , Issue.12 , pp. 1684-1686
    • Xu, L.1    Hue, S.2    Taylor, S.3    Ratcliffe, D.4    Workman, J.A.5    Jackson, S.6    Cane, P.A.7    Pillay, D.8
  • 56
    • 67749148923 scopus 로고    scopus 로고
    • A genome-wide short hairpin RNA screening of Jurkat T-cells for human proteins contributing to productive HIV-1 replication
    • Yeung, M. L., L. Houzet, V. S. R. K. Yedavalli, and K. T. Jeang. 2009. A genome-wide short hairpin RNA screening of Jurkat T-cells for human proteins contributing to productive HIV-1 replication. J. Biol. Chem. 284: 19463-19473.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19463-19473
    • Yeung, M.L.1    Houzet, L.2    Yedavalli, V.S.R.K.3    Jeang, K.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.