메뉴 건너뛰기




Volumn 57, Issue 12, 2014, Pages 5270-5281

Structure-activity relationship studies of indole-based compounds as small molecule HIV-1 fusion inhibitors targeting glycoprotein 41

Author keywords

[No Author keywords available]

Indexed keywords

3 [[ 1 [(3 METHOXYCARBONYLPHENYL)METHYL]INDOL 6 YL]INDOL 1 YL]METHYL]BENZOIC ACID; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; INDOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84903540200     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm500344y     Document Type: Article
Times cited : (30)

References (57)
  • 1
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B.; Markosyan, R. M.; Hemmati, H.; Delmedico, M. K.; Lambert, D. M.; Cohen, F. S. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion J. Cell Biol. 2000, 151, 413-423
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 2
    • 84903551027 scopus 로고    scopus 로고
    • Comment is in J. Cell. Biol. 2000, 151 (2), F9-F14.
    • (2000) J. Cell. Biol. , vol.151 , Issue.2
  • 3
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo, S. A.; Puri, A.; Blumenthal, R. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process Biochemistry (Moscow) 2001, 40, 12231-12236
    • (2001) Biochemistry (Moscow) , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 4
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • Steger, H. K.; Root, M. J. Kinetic dependence to HIV-1 entry inhibition J. Biol. Chem. 2006, 281, 25813-25821
    • (2006) J. Biol. Chem. , vol.281 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 5
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M.; Kim, P. S. Mechanisms of viral membrane fusion and its inhibition Annu. Rev. Biochem. 2001, 70, 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 7
    • 24944493173 scopus 로고    scopus 로고
    • Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation
    • Dimitrov, A. S.; Louis, J. M.; Bewley, C. A.; Clore, G. M.; Blumenthal, R. Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation Biochemistry (Moscow) 2005, 44, 12471-12479
    • (2005) Biochemistry (Moscow) , vol.44 , pp. 12471-12479
    • Dimitrov, A.S.1    Louis, J.M.2    Bewley, C.A.3    Clore, G.M.4    Blumenthal, R.5
  • 9
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • Greenberg, M. L.; Cammack, N. Resistance to enfuvirtide, the first HIV fusion inhibitor J. Antimicrob. Chemother. 2004, 54, 333-340
    • (2004) J. Antimicrob. Chemother. , vol.54 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 11
    • 27144451245 scopus 로고    scopus 로고
    • Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41
    • Louis, J. M.; Bewley, C. A.; Gustchina, E.; Aniana, A.; Clore, G. M. Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41 J. Mol. Biol. 2005, 353, 945-951
    • (2005) J. Mol. Biol. , vol.353 , pp. 945-951
    • Louis, J.M.1    Bewley, C.A.2    Gustchina, E.3    Aniana, A.4    Clore, G.M.5
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C.; Fass, D.; Berger, J. M.; Kim, P. S. 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
  • 14
    • 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, D. C.; Chutkowski, C. T.; Kim, P. S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 15613-15617
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 15
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of d -peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D. M.; Malashkevich, V. N.; Hong, L. H.; Carr, P. A.; Kim, P. S. 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
  • 16
    • 76649145391 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of indole compounds as novel inhibitors targeting Gp41
    • Zhou, G.; Wu, D.; Hermel, E.; Balogh, E.; Gochin, M. Design, synthesis, and evaluation of indole compounds as novel inhibitors targeting Gp41 Bioorg. Med. Chem. Lett. 2010, 20, 1500-1503
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1500-1503
    • Zhou, G.1    Wu, D.2    Hermel, E.3    Balogh, E.4    Gochin, M.5
  • 17
    • 84859442418 scopus 로고    scopus 로고
    • Discovery of HIV fusion inhibitors targeting gp41 using a comprehensive alpha-helix mimetic library
    • Whitby, L. R.; Boyle, K. E.; Cai, L.; Yu, X.; Gochin, M.; Boger, D. L. Discovery of HIV fusion inhibitors targeting gp41 using a comprehensive alpha-helix mimetic library Bioorg. Med. Chem. Lett. 2012, 22, 2861-2865
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 2861-2865
    • Whitby, L.R.1    Boyle, K.E.2    Cai, L.3    Yu, X.4    Gochin, M.5    Boger, D.L.6
  • 18
    • 58149090406 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of N -carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41
    • Liu, K.; Lu, H.; Hou, L.; Qi, Z.; Teixeira, C.; Barbault, F.; Fan, B. T.; Liu, S.; Jiang, S.; Xie, L. Design, synthesis, and biological evaluation of N -carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41 J. Med. Chem. 2008, 51, 7843-7854
    • (2008) J. Med. Chem. , vol.51 , pp. 7843-7854
    • Liu, K.1    Lu, H.2    Hou, L.3    Qi, Z.4    Teixeira, C.5    Barbault, F.6    Fan, B.T.7    Liu, S.8    Jiang, S.9    Xie, L.10
  • 19
    • 78751657690 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of novel 5-((arylfuran/1 H -pyrrol-2-yl)methylene)-2-thioxo-3-(3-(trifluoromethyl)phenyl) thiazolidin-4-ones as HIV-1 fusion inhibitors targeting gp41
    • Jiang, S.; Tala, S. R.; Lu, H.; Abo-Dya, N. E.; Avan, I.; Gyanda, K.; Lu, L.; Katritzky, A. R.; Debnath, A. K. Design, synthesis, and biological activity of novel 5-((arylfuran/1 H -pyrrol-2-yl)methylene)-2-thioxo-3-(3- (trifluoromethyl)phenyl)thiazolidin-4-ones as HIV-1 fusion inhibitors targeting gp41 J. Med. Chem. 2011, 54, 572-579
    • (2011) J. Med. Chem. , vol.54 , pp. 572-579
    • Jiang, S.1    Tala, S.R.2    Lu, H.3    Abo-Dya, N.E.4    Avan, I.5    Gyanda, K.6    Lu, L.7    Katritzky, A.R.8    Debnath, A.K.9
  • 20
    • 84886950938 scopus 로고    scopus 로고
    • Small molecule fusion inhibitors: Design, synthesis and biological evaluation of (Z)-3-(5-(3-benzyl-4-oxo-2-thioxothiazolidinylidene)methyl)- N -(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrroles and related derivatives targeting HIV-1 gp41
    • He, X. Y.; Lu, L.; Qiu, J.; Zou, P.; Yu, F.; Jiang, X. K.; Li, L.; Jiang, S.; Liu, S.; Xie, L. Small molecule fusion inhibitors: design, synthesis and biological evaluation of (Z)-3-(5-(3-benzyl-4-oxo-2-thioxothiazolidinylidene) methyl)- N -(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrroles and related derivatives targeting HIV-1 gp41 Bioorg. Med. Chem. 2013, 21, 7539-7548
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 7539-7548
    • He, X.Y.1    Lu, L.2    Qiu, J.3    Zou, P.4    Yu, F.5    Jiang, X.K.6    Li, L.7    Jiang, S.8    Liu, S.9    Xie, L.10
  • 21
    • 72249122328 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors
    • Katritzky, A. R.; Tala, S. R.; Lu, H.; Vakulenko, A. V.; Chen, Q. Y.; Sivapackiam, J.; Pandya, K.; Jiang, S.; Debnath, A. K. Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3- phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors J. Med. Chem. 2009, 52, 7631-7639
    • (2009) J. Med. Chem. , vol.52 , pp. 7631-7639
    • Katritzky, A.R.1    Tala, S.R.2    Lu, H.3    Vakulenko, A.V.4    Chen, Q.Y.5    Sivapackiam, J.6    Pandya, K.7    Jiang, S.8    Debnath, A.K.9
  • 22
    • 80052395837 scopus 로고    scopus 로고
    • Cell-to-cell spread of HIV permits ongoing replication despite antiretroviral therapy
    • Sigal, A.; Kim, J. T.; Balazs, A. B.; Dekel, E.; Mayo, A.; Milo, R.; Baltimore, D. Cell-to-cell spread of HIV permits ongoing replication despite antiretroviral therapy Nature 2011, 477, 95-98
    • (2011) Nature , vol.477 , pp. 95-98
    • Sigal, A.1    Kim, J.T.2    Balazs, A.B.3    Dekel, E.4    Mayo, A.5    Milo, R.6    Baltimore, D.7
  • 23
    • 80054910151 scopus 로고    scopus 로고
    • Development of indole compounds as small molecule inhibitors of HIV-1 gp41
    • Zhou, G.; Wu, D.; Snyder, B.; Ptak, R. G.; Kaur, H.; Gochin, M. Development of indole compounds as small molecule inhibitors of HIV-1 gp41 J. Med. Chem. 2011, 54, 7220-7231
    • (2011) J. Med. Chem. , vol.54 , pp. 7220-7231
    • Zhou, G.1    Wu, D.2    Snyder, B.3    Ptak, R.G.4    Kaur, H.5    Gochin, M.6
  • 25
    • 84872836027 scopus 로고    scopus 로고
    • Suzuki-Miyaura cross-coupling in acylation reactions, scope and recent developments
    • Blangetti, M.; Rosso, H.; Prandi, C.; Deagostino, A.; Venturello, P. Suzuki-Miyaura cross-coupling in acylation reactions, scope and recent developments Molecules 2013, 18, 1188-1213
    • (2013) Molecules , vol.18 , pp. 1188-1213
    • Blangetti, M.1    Rosso, H.2    Prandi, C.3    Deagostino, A.4    Venturello, P.5
  • 26
    • 2042507954 scopus 로고
    • Palladium-catalyzed cross-coupling reactions of organoboron compounds
    • Miyaura, N.; Suzuki, A. Palladium-catalyzed cross-coupling reactions of organoboron compounds Chem. Rev. 1995, 95, 2457-2483
    • (1995) Chem. Rev. , vol.95 , pp. 2457-2483
    • Miyaura, N.1    Suzuki, A.2
  • 28
    • 67650745033 scopus 로고    scopus 로고
    • The role of amphiphilicity and negative charge in glycoprotein 41 interactions in the hydrophobic pocket
    • Gochin, M.; Cai, L. The role of amphiphilicity and negative charge in glycoprotein 41 interactions in the hydrophobic pocket J. Med. Chem. 2009, 52, 4338-4344
    • (2009) J. Med. Chem. , vol.52 , pp. 4338-4344
    • Gochin, M.1    Cai, L.2
  • 29
    • 77951986384 scopus 로고    scopus 로고
    • Conformer generation with OMEGA: Algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database
    • Hawkins, P. C.; Skillman, A. G.; Warren, G. L.; Ellingson, B. A.; Stahl, M. T. Conformer generation with OMEGA: algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database J. Chem. Inf. Model. 2010, 50, 572-584
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 572-584
    • Hawkins, P.C.1    Skillman, A.G.2    Warren, G.L.3    Ellingson, B.A.4    Stahl, M.T.5
  • 30
    • 84869987609 scopus 로고    scopus 로고
    • Conformer generation with OMEGA: Learning from the data set and the analysis of failures
    • Hawkins, P. C.; Nicholls, A. Conformer generation with OMEGA: learning from the data set and the analysis of failures J. Chem. Inf. Model. 2012, 52, 2919-2936
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2919-2936
    • Hawkins, P.C.1    Nicholls, A.2
  • 31
    • 0024801485 scopus 로고
    • Efficient conversion of nitriles to amides with basic hydrogen peroxide in dimethyl sulfoxide
    • Katritzky, A. R.; Pilarski, B.; Urogdi, L. Efficient conversion of nitriles to amides with basic hydrogen peroxide in dimethyl sulfoxide Synthesis 1989, 12, 949-950
    • (1989) Synthesis , vol.12 , pp. 949-950
    • Katritzky, A.R.1    Pilarski, B.2    Urogdi, L.3
  • 32
    • 84875659806 scopus 로고    scopus 로고
    • Conjugation of cholesterol to HIV-1 fusion inhibitor C34 increases peptide-membrane interactions potentiating its action
    • Hollmann, A.; Matos, P. M.; Augusto, M. T.; Castanho, M. A.; Santos, N. C. Conjugation of cholesterol to HIV-1 fusion inhibitor C34 increases peptide-membrane interactions potentiating its action PLoS One 2013, 8, e60302
    • (2013) PLoS One , vol.8 , pp. 60302
    • Hollmann, A.1    Matos, P.M.2    Augusto, M.T.3    Castanho, M.A.4    Santos, N.C.5
  • 33
    • 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, A. K. 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
  • 34
    • 34548481743 scopus 로고    scopus 로고
    • Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry
    • He, Y.; Liu, S.; Jing, W.; Lu, H.; Cai, D.; Chin, D. J.; Debnath, A. K.; Kirchhoff, F.; Jiang, S. Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry J. Biol. Chem. 2007, 282, 25631-25639
    • (2007) J. Biol. Chem. , vol.282 , pp. 25631-25639
    • He, Y.1    Liu, S.2    Jing, W.3    Lu, H.4    Cai, D.5    Chin, D.J.6    Debnath, A.K.7    Kirchhoff, F.8    Jiang, S.9
  • 35
    • 84882263100 scopus 로고    scopus 로고
    • NMR-assisted computational studies of peptidomimetic inhibitors bound in the hydrophobic pocket of HIV-1 glycoprotein 41
    • Gochin, M.; Whitby, L. R.; Phillips, A. H.; Boger, D. L. NMR-assisted computational studies of peptidomimetic inhibitors bound in the hydrophobic pocket of HIV-1 glycoprotein 41 J. Comput.-Aided Mol. Des. 2013, 27, 569-582
    • (2013) J. Comput.-Aided Mol. Des. , vol.27 , pp. 569-582
    • Gochin, M.1    Whitby, L.R.2    Phillips, A.H.3    Boger, D.L.4
  • 36
    • 84899877600 scopus 로고    scopus 로고
    • Computer-aided approaches for targeting HIVgp41
    • Allen, W. J.; Rizzo, R. C. Computer-aided approaches for targeting HIVgp41 Biology 2012, 1, 311-338
    • (2012) Biology , vol.1 , pp. 311-338
    • Allen, W.J.1    Rizzo, R.C.2
  • 38
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge, M. D.; Murray, C. W.; Auton, T. R.; Paolini, G. V.; Mee, R. P. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes J. Comput.-Aided Mol. Des. 1997, 11, 425-445
    • (1997) J. Comput.-Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 39
    • 34447260888 scopus 로고    scopus 로고
    • A novel fluorescence intensity screening assay identifies new low molecular weight inhibitors of the gp41 coiled coil domain of HIV-1
    • Cai, L.; Gochin, M. A novel fluorescence intensity screening assay identifies new low molecular weight inhibitors of the gp41 coiled coil domain of HIV-1 Antimicrob. Agents Chemother. 2007, 51, 2388-2395
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2388-2395
    • Cai, L.1    Gochin, M.2
  • 40
    • 84867253840 scopus 로고    scopus 로고
    • A suite of modular fluorescence assays interrogate the human immunodeficiency virus glycoprotein-41 coiled coil and assist in determining binding mechanism of low molecular weight fusion inhibitors
    • Gochin, M. A suite of modular fluorescence assays interrogate the human immunodeficiency virus glycoprotein-41 coiled coil and assist in determining binding mechanism of low molecular weight fusion inhibitors Assay Drug Dev. Technol. 2012, 10, 407-416
    • (2012) Assay Drug Dev. Technol. , vol.10 , pp. 407-416
    • Gochin, M.1
  • 41
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt, E. J.; Wehrly, K.; Kuhmann, S. E.; Chesebro, B.; Kabat, D. Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1 J. Virol. 1998, 72, 2855-2864
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 46
    • 0021707158 scopus 로고
    • T4 positive human neoplastic cell lines susceptible to and permissive for HTLV-III
    • Popovic, M.; Read-Connole, E.; Gallo, R. C. T4 positive human neoplastic cell lines susceptible to and permissive for HTLV-III Lancet 1984, 2, 1472-1473
    • (1984) Lancet , vol.2 , pp. 1472-1473
    • Popovic, M.1    Read-Connole, E.2    Gallo, R.C.3
  • 48
    • 0030899871 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection
    • Chackerian, B.; Long, E. M.; Luciw, P. A.; Overbaugh, J. Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection J. Virol. 1997, 71, 3932-3939
    • (1997) J. Virol. , vol.71 , pp. 3932-3939
    • Chackerian, B.1    Long, E.M.2    Luciw, P.A.3    Overbaugh, J.4
  • 51
    • 0025810128 scopus 로고
    • Characterization of an HIV-1 isolate displaying an apparent absence of virion-associated reverse transcriptase activity
    • Buckheit, R. W., Jr.; Swanstrom, R. Characterization of an HIV-1 isolate displaying an apparent absence of virion-associated reverse transcriptase activity AIDS Res. Hum. Retroviruses 1991, 7, 295-302
    • (1991) AIDS Res. Hum. Retroviruses , vol.7 , pp. 295-302
    • Buckheit Jr., R.W.1    Swanstrom, R.2
  • 52
    • 0028077123 scopus 로고
    • Genetic variation of HIV type 1 in four World Health Organization- sponsored vaccine evaluation sites: Generation of functional envelope (glycoprotein 160) clones representative of sequence subtypes A, B, C, and E. WHO Network for HIV Isolation and Characterization
    • Gao, F.; Yue, L.; Craig, S.; Thornton, C. L.; Robertson, D. L.; McCutchan, F. E.; Bradac, J. A.; Sharp, P. M.; Hahn, B. H. Genetic variation of HIV type 1 in four World Health Organization-sponsored vaccine evaluation sites: generation of functional envelope (glycoprotein 160) clones representative of sequence subtypes A, B, C, and E. WHO Network for HIV Isolation and Characterization AIDS Res. Hum. Retroviruses 1994, 10, 1359-1368
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 1359-1368
    • Gao, F.1    Yue, L.2    Craig, S.3    Thornton, C.L.4    Robertson, D.L.5    McCutchan, F.E.6    Bradac, J.A.7    Sharp, P.M.8    Hahn, B.H.9
  • 53
    • 20944444788 scopus 로고    scopus 로고
    • Biologic and genetic characterization of a panel of 60 human immunodeficiency virus type 1 isolates, representing clades A, B, C, D, CRF01-AE, and CRF02-AG, for the development and assessment of candidate vaccines
    • Brown, B. K.; Darden, J. M.; Tovanabutra, S.; Oblander, T.; Frost, J.; Sanders-Buell, E.; de Souza, M. S.; Birx, D. L.; McCutchan, F. E.; Polonis, V. R. Biologic and genetic characterization of a panel of 60 human immunodeficiency virus type 1 isolates, representing clades A, B, C, D, CRF01-AE, and CRF02-AG, for the development and assessment of candidate vaccines J. Virol. 2005, 79, 6089-6101
    • (2005) J. Virol. , vol.79 , pp. 6089-6101
    • Brown, B.K.1    Darden, J.M.2    Tovanabutra, S.3    Oblander, T.4    Frost, J.5    Sanders-Buell, E.6    De Souza, M.S.7    Birx, D.L.8    McCutchan, F.E.9    Polonis, V.R.10
  • 54
    • 0034005970 scopus 로고    scopus 로고
    • Use of calibrated viral load standards for group M subtypes of human immunodeficiency virus type 1 to assess the performance of viral RNA quantitation tests
    • Jagodzinski, L. L.; Wiggins, D. L.; McManis, J. L.; Emery, S.; Overbaugh, J.; Robb, M.; Bodrug, S.; Michael, N. L. Use of calibrated viral load standards for group M subtypes of human immunodeficiency virus type 1 to assess the performance of viral RNA quantitation tests J. Clin. Microbiol. 2000, 38, 1247-1249
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 1247-1249
    • Jagodzinski, L.L.1    Wiggins, D.L.2    McManis, J.L.3    Emery, S.4    Overbaugh, J.5    Robb, M.6    Bodrug, S.7    Michael, N.L.8
  • 55
    • 0001109246 scopus 로고    scopus 로고
    • A fast method of molecular shape comparison: A simple application of a Gaussian description of molecular shape
    • Grant, J. A.; Gallardo, M. A.; Pickup, B. T. A fast method of molecular shape comparison: a simple application of a Gaussian description of molecular shape J. Comput. Chem. 1996, 17, 1653-1666
    • (1996) J. Comput. Chem. , vol.17 , pp. 1653-1666
    • Grant, J.A.1    Gallardo, M.A.2    Pickup, B.T.3
  • 57
    • 79952262090 scopus 로고    scopus 로고
    • FRED pose prediction and virtual screening accuracy
    • McGann, M. FRED pose prediction and virtual screening accuracy J. Chem. Inf. Model. 2011, 51, 578-596
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 578-596
    • McGann, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.