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Volumn 15, Issue 5, 2006, Pages 465-478

Progress in identifying peptides and small-molecule inhibitors targeted to gp41 of HIV-1

Author keywords

C terminal heptad repeat; Fusion; gp41; Heptad repeats; HIV 1 inhibitor; N terminal heptad repeat; Prefusion

Indexed keywords

ADS J 1; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIRETROVIRUS AGENT; DARUNAVIR; DP 107; DP 180; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; LOPINAVIR PLUS RITONAVIR; NB 2; NB 64; NICOBOXIL; PEPTIDE DERIVATIVE; RITONAVIR; SJ 2176; T 1249; THEAFLAVIN 3,3' DIGALLATE; TIPRANAVIR; UNCLASSIFIED DRUG; ZIDOVUDINE;

EID: 33646459953     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.15.5.465     Document Type: Review
Times cited : (17)

References (58)
  • 1
    • 0345097633 scopus 로고    scopus 로고
    • The discovery of HIV as the cause of AIDS
    • GALLO RC, MONTAGNIER L: The discovery of HIV as the cause of AIDS. N. Engl. J. Med. (2003) 349:2283-2285.
    • (2003) N. Engl. J. Med. , vol.349 , pp. 2283-2285
    • Gallo, R.C.1    Montagnier, L.2
  • 3
    • 11844302187 scopus 로고    scopus 로고
    • Chemokine receptors as new molecular targets for antiviral therapy
    • SANTORO F, VASSENA L, LUSSO P: Chemokine receptors as new molecular targets for antiviral therapy. New Microbiol. (2004) 27:17-29.
    • (2004) New Microbiol. , vol.27 , pp. 17-29
    • Santoro, F.1    Vassena, L.2    Lusso, P.3
  • 4
    • 2442511737 scopus 로고    scopus 로고
    • High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques
    • LIU S, JIANG S: High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: theories and techniques. Curr. Pharm. Des. (2004) 10:1827-1843.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1827-1843
    • Liu, S.1    Jiang, S.2
  • 5
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • ROOT MJ, STEGER HK: HIV-1 gp41 as a target for viral entry inhibition. Curr. Pharm. Des. (2004) 10:1805-1825.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1805-1825
    • Root, M.J.1    Steger, H.K.2
  • 7
    • 0042924181 scopus 로고    scopus 로고
    • Virus entry as a target for anti-HIV intervention
    • ESTE JA: Virus entry as a target for anti-HIV intervention. Curr. Med. Chem. (2003) 10:1617-1632.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1617-1632
    • Este, J.A.1
  • 8
    • 0037130296 scopus 로고    scopus 로고
    • New developments in anti-HIV chemotherapy
    • DE CLERCQ E: New developments in anti-HIV chemotherapy. Biochim. Biophys. Acta (2002) 1587:258-275.
    • (2002) Biochim. Biophys. Acta , vol.1587 , pp. 258-275
    • de Clercq, E.1
  • 9
    • 0034708369 scopus 로고    scopus 로고
    • Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41
    • JIANG S, DEBNATH AK: Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41. Biochem. Biophys. Res. Commun. (2000) 269:641-646.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 641-646
    • Jiang, S.1    Debnath, A.K.2
  • 10
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • JIANG S, ZHAO Q, DEBNATH AK: Peptide and non-peptide HIV fusion inhibitors. Curr. Pharm. Des. (2002) 8:563-580.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 11
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • ECKERT DM, KIM PS: Mechanisms of viral membrane fusion and its inhibition. Ann. Rev. Biochem. (2001) 70:777-810.
    • (2001) Ann. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 12
    • 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, MATTHEWS T: A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA (1992) 89:10537-10541.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 13
    • 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, DUBAY JW, GREENWELL T et al.: 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 (1994) 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3
  • 15
    • 0027203897 scopus 로고
    • Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41
    • JIANG S, LIN K, STRICK N, NEURATH AR: Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41. Biochem. Biophys. Res. Commun. (1993) 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
  • 16
    • 0029411484 scopus 로고
    • Effect of amino acid replacements, additions and deletions on the antiviral activity of a peptide derived from the HIV-1 GP41 sequence
    • JIANG S, LIN K: Effect of amino acid replacements, additions and deletions on the antiviral activity of a peptide derived from the HIV-1 GP41 sequence. Pept. Res. (1995) 8:345-348.
    • (1995) Pept. Res. , vol.8 , pp. 345-348
    • Jiang, S.1    Lin, K.2
  • 17
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • WILD C, GREENWELL T, MATTHEWS T: A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retrov. (1993) 9:1051-1053.
    • (1993) AIDS Res. Hum. Retrov. , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 18
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • KILBY JM, HOPKINS S, VENETTA TM et al.: Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat. Med. (1998) 4:1302-1307.
    • (1998) Nat. Med. , vol.4 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3
  • 19
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults
    • KILBY JM, LALEZARI JP, ERON JJ et al.: The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults. AIDS Res. Hum. Retrov. (2002) 18:685-693.
    • (2002) AIDS Res. Hum. Retrov. , vol.18 , pp. 685-693
    • Kilby, J.M.1    Lalezari, J.P.2    Eron, J.J.3
  • 20
    • 0035313589 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion
    • NAGASHIMA KA, THOMPSON DA, ROSENFIELD SI, MADDON PJ, DRAGIC T, OLSON WC: Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion. J. Infect. Dis. (2001) 183:1121-1125.
    • (2001) J. Infect. Dis. , vol.183 , pp. 1121-1125
    • Nagashima, K.A.1    Thompson, D.A.2    Rosenfield, S.I.3    Maddon, P.J.4    Dragic, T.5    Olson, W.C.6
  • 22
    • 0036232981 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro
    • TREMBLAY CL, GIGUEL F, KOLLMANN C et al.: Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro. Antimicrob. Agents Chemother. (2002) 46:1336-1339.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1336-1339
    • Tremblay, C.L.1    Giguel, F.2    Kollmann, C.3
  • 24
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • LU M, BLACKLOW SC, KIM PS: A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. (1995) 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 25
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • LU M, KIM PS: A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. (1997) 15:465-471.
    • (1997) J. Biomol. Struct. Dyn. , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 26
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • TAN K, LIU J, WANG J, SHEN S, LU M: Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA (1997) 94:12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 27
    • 0034701058 scopus 로고    scopus 로고
    • Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
    • SHU W, LIU J, JI H, RADIGEN L, JIANG S, LU M: Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides. Biochemistry (2000) 39:1634-1642.
    • (2000) Biochemistry , vol.39 , pp. 1634-1642
    • Shu, W.1    Liu, J.2    Ji, H.3    Radigen, L.4    Jiang, S.5    Lu, M.6
  • 28
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • CHAN DC, CHUTKOWSKI CT, KIM PS: Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA (1998) 95:15613-15617.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 29
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • HERSKOWITZ I: Functional inactivation of genes by dominant negative mutations. Nature (1987) 329:219-222.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 30
    • 0037119022 scopus 로고    scopus 로고
    • Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells
    • OTAKA A, NAKAMURA M, NAMEKI D et al.: Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells. Angew. Chem. Int. Ed. Engl. (2002) 41:2937-2940.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2937-2940
    • Otaka, A.1    Nakamura, M.2    Nameki, D.3
  • 31
    • 17444378287 scopus 로고    scopus 로고
    • Differential inhibition of HIV-1 and SIV envelope-mediated cell fusion by C34 peptides derived from the C-terminal heptad repeat of gp41 from diverse strains of HIV-1, HIV-2, and SIV
    • GUSTCHINA E, HUMMER G, BEWLEY CA, CLORE GM: Differential inhibition of HIV-1 and SIV envelope-mediated cell fusion by C34 peptides derived from the C-terminal heptad repeat of gp41 from diverse strains of HIV-1, HIV-2, and SIV. J. Med. Chem. (2005) 48:3036-3044.
    • (2005) J. Med. Chem. , vol.48 , pp. 3036-3044
    • Gustchina, E.1    Hummer, G.2    Bewley, C.A.3    Clore, G.M.4
  • 33
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implications for the viral fusion mechanism
    • JUDICE JK, TOM JY, HUANG W et al.: Inhibition of HIV type 1 infectivity by constrained α-helical peptides: implications for the viral fusion mechanism. Proc. Natl. Acad. Sci. USA (1997) 94:13426-13430.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13426-13430
    • Judice, J.K.1    Tom, J.Y.2    Huang, W.3
  • 34
    • 0034693932 scopus 로고    scopus 로고
    • Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1
    • JIN BS, RYU JR, AHN K, YU YG: Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retrov. (2000) 16:1797-1804.
    • (2000) AIDS Res. Hum. Retrov. , vol.16 , pp. 1797-1804
    • Jin, B.S.1    Ryu, J.R.2    Ahn, K.3    Yu, Y.G.4
  • 35
    • 27744529111 scopus 로고    scopus 로고
    • Stronger anti-HIV-1 activity of C-peptide derived from HIV-189.6 gp41 C-terminal heptad repeated sequence
    • SEO JK, KIM HK, LEE TY, HAHM KS, KIM KL, LEE MK: Stronger anti-HIV-1 activity of C-peptide derived from HIV-189.6 gp41 C-terminal heptad repeated sequence. Peptides (2005) 26:2175-2181.
    • (2005) Peptides , vol.26 , pp. 2175-2181
    • Seo, J.K.1    Kim, H.K.2    Lee, T.Y.3    Hahm, K.S.4    Kim, K.L.5    Lee, M.K.6
  • 36
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • ECKERT DM, KIM PS: Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc. Natl. Acad. Sci. USA (2001) 98:11187-11192.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 37
    • 0032509096 scopus 로고    scopus 로고
    • Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues
    • ECKERT DM, MALASHKEVICH VN, KIM PS: Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues. J. Mol. Biol. (1998) 284:859-865.
    • (1998) J. Mol. Biol. , vol.284 , pp. 859-865
    • Eckert, D.M.1    Malashkevich, V.N.2    Kim, P.S.3
  • 38
    • 0031793228 scopus 로고    scopus 로고
    • An isoleucine zipper peptide forms a native-like triple stranded coiled coil in solution
    • SUZUKI K, HIROAKI H, KOHDA D, TANAKA T. An isoleucine zipper peptide forms a native-like triple stranded coiled coil in solution. Protein Eng. (1998) 11:1051-1055.
    • (1998) Protein Eng. , vol.11 , pp. 1051-1055
    • Suzuki, K.1    Hiroaki, H.2    Kohda, D.3    Tanaka, T.4
  • 39
    • 24644449058 scopus 로고    scopus 로고
    • Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection
    • BIANCHI E, FINOTTO M, INGALLINELLA P et al.: Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection. Proc. Natl. Acad. Sci. USA (2005) 102:12903-12908.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12903-12908
    • Bianchi, E.1    Finotto, M.2    Ingallinella, P.3
  • 40
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • BEWLEY CA, LOUIS JM, GHIRLANDO R, CLORE GM: Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. (2002) 277:14238-14245.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 41
    • 0037490139 scopus 로고    scopus 로고
    • Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion
    • LOUIS JM, NESHEIWAT I, CHANG L, CLORE GM, BEWLEY CA: Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion. J Biol. Chem. (2003) 278:20278-20285.
    • (2003) J Biol. Chem. , vol.278 , pp. 20278-20285
    • Louis, J.M.1    Nesheiwat, I.2    Chang, L.3    Clore, G.M.4    Bewley, C.A.5
  • 42
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV entry inhibitor
    • ROOT MJ, KAY MS, KIM PS: Protein design of an HIV entry inhibitor. Science (2001) 291:884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 43
    • 19744363341 scopus 로고    scopus 로고
    • Rational design of highly potent HIV-1 fusion inhibitory proteins: Implication for developing antiviral therapeutics
    • NI L, GAO GF, TIEN P: Rational design of highly potent HIV-1 fusion inhibitory proteins: implication for developing antiviral therapeutics. Biochem. Biophys. Res. Commun. (2005) 332:831-836.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 831-836
    • Ni, L.1    Gao, G.F.2    Tien, P.3
  • 44
    • 0035800816 scopus 로고    scopus 로고
    • CCG-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • CCG-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J. Biol. Chem. (2001) 276:29485-29489.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 45
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • CHAN DC, FASS D, BERGER JM, KIM PS: Core structure of gp41 from the HIV envelope glycoprotein. Cell (1997) 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
  • 46
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • ECKERT DM, MALASHKEVICH VN, HONG LH, CARR PA, KIM PS: Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell (1999) 99:103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 47
    • 0032876381 scopus 로고    scopus 로고
    • Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elements
    • FERRER M, KAPOOR TM, STRASSMAIER T et al.: Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elements. Nat. Struct. Biol. (1999) 6:953-960.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 953-960
    • Ferrer, M.1    Kapoor, T.M.2    Strassmaier, T.3
  • 48
    • 17944384967 scopus 로고    scopus 로고
    • The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core
    • ZHOU G, FERRER M, CHOPRA R et al: The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core. Bioorg. Med. Chem. (2000) 8:2219-2227.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 2219-2227
    • Zhou, G.1    Ferrer, M.2    Chopra, R.3
  • 49
    • 0034595078 scopus 로고    scopus 로고
    • A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity
    • JIANG S, DEBNATH AK: A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity. Biochem. Biophys. Res. Commun. (2000) 270:153-157.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 153-157
    • Jiang, S.1    Debnath, A.K.2
  • 50
    • 7244253012 scopus 로고    scopus 로고
    • N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion
    • JIANG S, LU H, LIU S, ZHAO Q, HE Y, DEBNATH AK: N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion. Antimicrob. Agents Chemother. (2004) 48:4349-4359.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4349-4359
    • Jiang, S.1    Lu, H.2    Liu, S.3    Zhao, Q.4    He, Y.5    Debnath, A.K.6
  • 51
    • 0037126834 scopus 로고    scopus 로고
    • Design of a protein surface antagonist based on α-helix mimicry: Inhibition of gp41 assembly and viral fusion
    • ERNST JT, KUTZKI O, DEBNATH AK, JIANG S, LU H, HAMILTON AD: Design of a protein surface antagonist based on α-helix mimicry: inhibition of gp41 assembly and viral fusion. Angew. Chem. Int. Ed. Engl. (2002) 41:278-281.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 278-281
    • Ernst, J.T.1    Kutzki, O.2    Debnath, A.K.3    Jiang, S.4    Lu, H.5    Hamilton, A.D.6
  • 52
    • 0033607028 scopus 로고    scopus 로고
    • Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodeficiency virus type 1
    • DEBNATH AK, RADIGAN L, JIANG S: Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodeficiency virus type 1. J. Med. Chem. (1999) 42:3203-3209.
    • (1999) J. Med. Chem. , vol.42 , pp. 3203-3209
    • Debnath, A.K.1    Radigan, L.2    Jiang, S.3
  • 53
    • 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, LIN K, ZHANG L, DEBNATH AK: A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods (1999) 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
  • 54
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • LIPINSKI CA: Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods (2000) 44:235-249.
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 55
    • 0036392065 scopus 로고    scopus 로고
    • XTT formazan widely used to detect cell viability inhibits HIV type 1 infection in vitro by targeting gp41
    • ZHAO Q, ERNST JT, HAMILTON AD, DEBNATH AK, JIANG S: XTT formazan widely used to detect cell viability inhibits HIV type 1 infection in vitro by targeting gp41. AIDS Res. Hum. Retrov. (2002) 18:989-997.
    • (2002) AIDS Res. Hum. Retrov. , vol.18 , pp. 989-997
    • Zhao, Q.1    Ernst, J.T.2    Hamilton, A.D.3    Debnath, A.K.4    Jiang, S.5
  • 58
    • 19744379597 scopus 로고    scopus 로고
    • Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41
    • LIU S, LU H, ZHAO Q et al.: Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41. Biochim. Biophys. Acta (2005) 1723:270-181.
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 181-270
    • Liu, S.1    Lu, H.2    Zhao, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.