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Volumn 55, Issue 9, 2012, Pages 4382-4396

Structure-based design, synthesis, and characterization of dual hotspot small-molecule HIV-1 Entry Inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR;

EID: 84861048825     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm300265j     Document Type: Article
Times cited : (85)

References (97)
  • 1
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • Barre-Sinoussi, F.; Chermann, J. C.; Rey, F.; Nugeyre, M. T.; Chamaret, S.; Gruest, J.; Dauguet, C.; Axler-Blin, C.; Vezinet-Brun, F.; Rouzioux, C.; Rozenbaum, W.; Montagnier, L. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS) Science 1983, 220, 868-871 (Pubitemid 13080157)
    • (1983) Science , vol.220 , Issue.4599 , pp. 868-871
    • Barre Sinoussi, F.1    Chermann, J.C.2    Rey, F.3
  • 2
    • 0021261510 scopus 로고
    • Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS
    • Gallo, R. C.; Salahuddin, S. Z.; Popovic, M.; Shearer, G. M.; Kaplan, M.; Haynes, B. F.; Palker, T. J.; Redfield, R.; Oleske, J.; Safai, B. Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS Science 1984, 224, 500-503 (Pubitemid 14134741)
    • (1984) Science , vol.224 , Issue.4648 , pp. 500-503
    • Gallo, R.C.1    Salahuddin, S.Z.2    Popovic, M.3
  • 3
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • DOI 10.1038/312763a0
    • Dalgleish, A. G.; Beverley, P. C.; Clapham, P. R.; Crawford, D. H.; Greaves, M. F.; Weiss, R. A. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus Nature 1984, 312, 763-767 (Pubitemid 15195924)
    • (1984) Nature , vol.312 , Issue.5996 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.L.2    Clapham, P.R.3
  • 4
    • 0022587282 scopus 로고
    • Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110K viral protein and the T4 molecule
    • McDougal, J. S.; Kennedy, M. S.; Sligh, J. M.; Cort, S. P.; Mawle, A.; Nicholson, J. K. Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110K viral protein and the T4 molecule Science 1986, 231
    • (1986) Science , pp. 231
    • McDougal, J.S.1    Kennedy, M.S.2    Sligh, J.M.3    Cort, S.P.4    Mawle, A.5    Nicholson, J.K.6
  • 5
    • 0021720872 scopus 로고
    • T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
    • DOI 10.1038/312767a0
    • Klatzmann, D.; Champagne, E.; Chamaret, S.; Gruest, J.; Guetard, D.; Hercend, T.; Gluckman, J. C.; Montagnier, L. T-Lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV Nature 1984, 314, 767-768 (Pubitemid 15195925)
    • (1984) Nature , vol.312 , Issue.5996 , pp. 767-768
    • Klatzmann, D.1    Champagne, E.2    Chamaret, S.3
  • 6
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • DOI 10.1126/science.280.5371.1884
    • Wyatt, R.; Sodroski, J. The HIV-1 envelope glycoproteins fusogens antigens and immunogens Science 1998, 280, 1884-1888 (Pubitemid 28299385)
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 8
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow, S. C.; Lu, M.; Kim, P. S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein Biochemistry 1995, 34, 14955-14962
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 9
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M.; Blacklow, S. C.; Kim, P. S. 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
  • 10
    • 0023217711 scopus 로고
    • Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1
    • Kowalski, M.; Potz, J.; Basiripour, L.; Dorfman, T.; Goh, W. C.; Terwilliger, E.; Dayton, A.; Rosen, C.; Haseltine, W.; Sodroski, J. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1 Science 1987, 237, 1351-1355 (Pubitemid 17134619)
    • (1987) Science , vol.237 , Issue.4820 , pp. 1351-1355
    • Kowalski, M.1    Potz, J.2    Basiripour, L.3
  • 11
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, Q. J.; Moore, J. P. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding J. Exp. Med. 1991, 174, 407-415
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 12
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau, Q. J.; Moore, J. P.; Vignaux, F.; Traincard, F.; Poignard, P. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding J. Virol. 1993, 67, 7383-7393 (Pubitemid 23343866)
    • (1993) Journal of Virology , vol.67 , Issue.12 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 17
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • DOI 10.1016/S0092-8674(00)81314-8
    • Doranz, B. J.; Rucker, J.; Yi, Y.; Smyth, R. J.; Samson, M.; Peiper, S. C.; Parmentier, M.; Collman, R. G.; Doms, R. W. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors Cell 1996, 85, 1149-1158 (Pubitemid 26235280)
    • (1996) Cell , vol.85 , Issue.7 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmentier, M.7    Collman, R.G.8    Doms, R.W.9
  • 20
    • 0025223471 scopus 로고
    • Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion
    • Helseth, E.; Olshevsky, U.; Gabuzda, D.; Ardman, B.; Haseltine, W.; Sodroski, J. Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion J. Virol. 1990, 64, 6314-6318
    • (1990) J. Virol. , vol.64 , pp. 6314-6318
    • Helseth, E.1    Olshevsky, U.2    Gabuzda, D.3    Ardman, B.4    Haseltine, W.5    Sodroski, J.6
  • 23
    • 79952282671 scopus 로고    scopus 로고
    • Viral surface glycoproteins, gp120 and gp41, as potential drug targets against HIV-1: Brief overview one quarter of a century past the approval of zidovudine, the first anti-retroviral drug
    • Teixeira, C.; Gomes, J. R.; Gomes, P.; Maurel, F.; Barbault, F. Viral surface glycoproteins, gp120 and gp41, as potential drug targets against HIV-1: brief overview one quarter of a century past the approval of zidovudine, the first anti-retroviral drug Eur. J. Med. Chem. 2011, 46, 979-992
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 979-992
    • Teixeira, C.1    Gomes, J.R.2    Gomes, P.3    Maurel, F.4    Barbault, F.5
  • 24
    • 77957931762 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: A promising avenue of anti-HIV drug discovery
    • Zhan, P.; Li, W.; Chen, H.; Liu, X. Targeting protein-protein interactions: a promising avenue of anti-HIV drug discovery Curr. Med. Chem. 2010, 17, 3393-3409
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3393-3409
    • Zhan, P.1    Li, W.2    Chen, H.3    Liu, X.4
  • 25
    • 33747622811 scopus 로고    scopus 로고
    • Small-molecule HIV-1 gp120 inhibitors to prevent HIV-1 entry: An emerging opportunity for drug development
    • Kadow, J.; Wang, H. G.; Lin, P. F. Small-molecule HIV-1 gp120 inhibitors to prevent HIV-1 entry: an emerging opportunity for drug development Curr. Opin. Invest. Drugs 2006, 7, 721-726 (Pubitemid 44263176)
    • (2006) Current Opinion in Investigational Drugs , vol.7 , Issue.8 , pp. 721-726
    • Kadow, J.1    Hwei-Gene, H.W.2    Pin-Fang, L.3
  • 28
    • 77951939875 scopus 로고    scopus 로고
    • Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity
    • Diskin, R.; Marcovecchio, P. M.; Bjorkman, P. J. Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity Nat. Struct. Mol. Biol. 2010, 17, 608-613
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 608-613
    • Diskin, R.1    Marcovecchio, P.M.2    Bjorkman, P.J.3
  • 31
    • 0034482696 scopus 로고    scopus 로고
    • Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    • DOI 10.1016/S0969-2126(00)00547-5, PII S0969212600005475
    • Kwong, P. D.; Wyatt, R.; Majeed, S.; Robinson, J.; Sweet, R. W.; Sodroski, J.; Hendrickson, W. A. Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates Structure (London) 2000, 8, 1329-1339 (Pubitemid 32149759)
    • (2000) Structure , vol.8 , Issue.12 , pp. 1329-1339
    • Kwong, P.D.1    Wyatt, R.2    Majeed, S.3    Robinson, J.4    Sweet, R.W.5    Sodroski, J.6    Hendrickson, W.A.7
  • 32
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong, P. D.; Wyatt, R.; Robinson, J.; Sweet, R. W.; Sodroski, J.; Hendrickson, W. A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody Nature 1998, 393, 648-659 (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 35
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • DOI 10.1038/nature03327
    • Chen, B.; Vogan, E. M.; Gong, H.; Skehel, J. J.; Wiley, D. C.; Harrison, S. C. Structure of an unliganded simian immunodeficiency virus gp120 core Nature 2005, 433, 834-841 (Pubitemid 40314887)
    • (2005) Nature , vol.433 , Issue.7028 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 37
    • 0022459886 scopus 로고
    • Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS
    • Starcich, B. R.; Hahn, B. H.; Shaw, G. S.; McNeely, P. D.; Modrow, S.; Wolf, H.; Parks, E. S.; Parks, W. P.; Josephs, S. F.; Gallo, R. C.; Wong-Staal, F. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS Cell 1986, 5, 637-648 (Pubitemid 16063128)
    • (1986) Cell , vol.45 , Issue.5 , pp. 637-648
    • Starcich, B.R.1    Hahn, B.H.2    Shaw, G.M.3
  • 38
    • 0026650992 scopus 로고
    • The human immunodeficiency virus gp120 binding site on CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure
    • Moebius, U.; Clayton, L. K.; Abraham, S.; Harrison, S. C.; Reinherz, E. L. The human immunodeficiency virus gp120 binding site on CD4: delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure J. Exp. Med. 1992, 176, 507-517
    • (1992) J. Exp. Med. , vol.176 , pp. 507-517
    • Moebius, U.1    Clayton, L.K.2    Abraham, S.3    Harrison, S.C.4    Reinherz, E.L.5
  • 39
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells, J. A.; McClendon, C. L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 2007, 450, 1001-1009 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 40
    • 47349109056 scopus 로고    scopus 로고
    • Drug-like inhibitors of protein-protein interactions: A structural examination of effective protein mimicry
    • DOI 10.2174/138920308784533989
    • Fry, D. C. Drug-like inhibitors of protein-protein interactions: a structural examination of effective protein mimicry Curr. Protein Pept. Sci. 2008, 9, 240-247 (Pubitemid 351997840)
    • (2008) Current Protein and Peptide Science , vol.9 , Issue.3 , pp. 240-247
    • Fry, D.C.1
  • 41
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • Morelli, X.; Bourgeas, R.; Roche, P. Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I) Curr. Opin. Chem. Biol. 2011, 15, 475-481
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Roche, P.3
  • 43
    • 23844440296 scopus 로고    scopus 로고
    • Identification of N-phenyl-N′-(2,2,6,6-tetramethyl-piperidin-4-yl)- oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4
    • DOI 10.1016/j.virol.2005.06.008, PII S0042682205003363
    • Zhao, Q.; Ma, L.; Jiang, S.; Lu, H.; Liu, S.; He, Y.; Strick, N.; Neamati, N.; Debnath, A. K. Identification of N -phenyl- N ′-(2,2,6,6- tetramethyl-piperidin-4-yl)-oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4 Virology 2005, 339, 213-225 (Pubitemid 41169789)
    • (2005) Virology , vol.339 , Issue.2 , pp. 213-225
    • Zhao, Q.1    Ma, L.2    Jiang, S.3    Lu, H.4    Liu, S.5    He, Y.6    Strick, N.7    Neamati, N.8    Debnath, A.K.9
  • 47
    • 34249827906 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: Antigenicity, biophysics, and immunogenicity
    • DOI 10.1128/JVI.02500-06
    • Dey, B.; Pancera, M.; Svehla, K.; Shu, Y.; Xiang, S. H.; Vainshtein, J.; Li, Y.; Sodroski, J.; Kwong, P. D.; Mascola, J. R.; Wyatt, R. Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity J. Virol. 2007, 81, 5579-5593 (Pubitemid 46846998)
    • (2007) Journal of Virology , vol.81 , Issue.11 , pp. 5579-5593
    • Dey, B.1    Pancera, M.2    Svehla, K.3    Shu, Y.4    Xiang, S.-H.5    Vainshtein, J.6    Li, Y.7    Sodroski, J.8    Kwong, P.D.9    Mascola, J.R.10    Wyatt, R.11
  • 49
    • 33748491260 scopus 로고    scopus 로고
    • Thermodynamics of binding of a low-molecular-weight CD4 mimetic to HIV-1 gp120
    • DOI 10.1021/bi061193r
    • Schön, A.; Madani, N.; Klein, J. C.; Hubicki, A.; Ng, D.; Yang, X.; Smith, A. B., 3rd; Sodroski, J.; Freire, E. Thermodynamics of binding of a low-molecular-weight CD4 mimetic to HIV-1 gp120 Biochemistry 2006, 45, 10973-10980 (Pubitemid 44360167)
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 10973-10980
    • Schon, A.1    Madani, N.2    Klein, J.C.3    Hubicki, A.4    Ng, D.5    Yang, X.6    Smith III, A.B.7    Sodroski, J.8    Freire, E.9
  • 53
    • 84861070554 scopus 로고    scopus 로고
    • Nonspecificity has been observed (data not shown) for compounds with weak anti-viral activity belonging to the NBD chemotype.
    • Nonspecificity has been observed (data not shown) for compounds with weak anti-viral activity belonging to the NBD chemotype.
  • 57
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 1997, 267, 727-748 (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 59
    • 84861045455 scopus 로고    scopus 로고
    • OpenEye Scientific Software, Inc. (3600 Cerrillos Road, Suite 1107, Santa Fe, NM 87507).
    • ROCS; OpenEye Scientific Software, Inc. (3600 Cerrillos Road, Suite 1107, Santa Fe, NM 87507), 2008; www.eyesopen.com.
    • (2008) ROCS
  • 60
    • 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. A fast method of molecular shape comparison. A simple application of a Gaussian description of molecular shape J. Comput. Chem. 1996, 17, 1653-1666 (Pubitemid 126535414)
    • (1996) Journal of Computational Chemistry , vol.17 , Issue.14 , pp. 1653-1666
    • Grant, J.A.1    Gallardo, M.A.2    Pickup, B.T.3
  • 61
    • 14944348527 scopus 로고    scopus 로고
    • A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction
    • DOI 10.1021/jm040163o
    • Rush, T. S., 3rd; Grant, J. A.; Mosyak, L.; Nicholls, A. A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction J. Med. Chem. 2005, 48, 1489-1495 (Pubitemid 40364556)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.5 , pp. 1489-1495
    • Rush III, T.S.1    Grant, J.A.2    Mosyak, L.3    Nicholls, A.4
  • 62
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - A free database of commercially available compounds for virtual screening
    • DOI 10.1021/ci049714+
    • Irwin, J. J.; Shoichet, B. K. ZINC - a free database of commercially available compounds for virtual screening J. Chem. Inf. Model. 2005, 45, 177-182 (Pubitemid 40736970)
    • (2005) Journal of Chemical Information and Modeling , vol.45 , Issue.1 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 63
    • 84861022085 scopus 로고    scopus 로고
    • version 7; University of California, San Francisco, CA.
    • ZINC, version 7; University of California, San Francisco, CA, 2006; http://zinc.docking.org/.
    • (2006) ZINC
  • 64
    • 84861064296 scopus 로고    scopus 로고
    • Monotropic isolates infect cells expressing CD4 and one of the transmembrane co-receptors, CD4/CCR5 or CD4/CXCR4. Dual-tropic isolates can infect cells expressing CD4 and either transmembrane co-receptor CD4/CCR5 or CD4/CXCR4.
    • Monotropic isolates infect cells expressing CD4 and one of the transmembrane co-receptors, CD4/CCR5 or CD4/CXCR4. Dual-tropic isolates can infect cells expressing CD4 and either transmembrane co-receptor CD4/CCR5 or CD4/CXCR4.
  • 65
    • 33745767712 scopus 로고    scopus 로고
    • Characterization of the multiple conformationai states of free monomeric and trimeric human immunodeficiency virus envelope glycoproteins after fixation by cross-linker
    • DOI 10.1128/JVI.00118-06
    • Yuan, W.; Bazick, J.; Sodroski, J. Characterization of the multiple conformational states of free monomeric and trimeric human immunodeficiency virus envelope glycoproteins after fixation by cross-linker J. Virol. 2006, 80, 6725-6737 (Pubitemid 44025172)
    • (2006) Journal of Virology , vol.80 , Issue.14 , pp. 6725-6737
    • Yuan, W.1    Bazick, J.2    Sodroski, J.3
  • 66
    • 77956819789 scopus 로고    scopus 로고
    • Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange
    • Kong, L.; Huang, C. C.; Coales, S. J.; Molnar, K. S.; Skinner, J.; Hamuro, Y.; Kwong, P. D. Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange J. Virol. 2010, 84, 10311-10321
    • (2010) J. Virol. , vol.84 , pp. 10311-10321
    • Kong, L.1    Huang, C.C.2    Coales, S.J.3    Molnar, K.S.4    Skinner, J.5    Hamuro, Y.6    Kwong, P.D.7
  • 67
    • 17044403086 scopus 로고    scopus 로고
    • Ligand efficiency indices as guideposts for drug discovery
    • Abad-Zapatero, C.; Metz, J. T. Ligand efficiency indices as guideposts for drug discovery Drug Discovery Today 2005, 10, 464-469
    • (2005) Drug Discovery Today , vol.10 , pp. 464-469
    • Abad-Zapatero, C.1    Metz, J.T.2
  • 68
    • 77949743743 scopus 로고    scopus 로고
    • Atomic Analysis of protein-protein interfaces with known inhibitors: The 2P2I database
    • Bourgeas, R. I.; Basse, M.-J.; Morelli, X.; Roche, X. Atomic Analysis of protein-protein interfaces with known inhibitors: the 2P2I database PLoS One 2010, 5 (3) e9598
    • (2010) PLoS One , vol.5 , Issue.3 , pp. 9598
    • Bourgeas, R.I.1    Basse, M.-J.2    Morelli, X.3    Roche, X.4
  • 69
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • DOI 10.1016/S0076-6879(98)95037-6
    • Luque, I.; Freire, E. Structure-based prediction of binding affinities and molecular design of peptide ligands Methods Enzymol. 1998, 295, 100-127 (Pubitemid 29349911)
    • (1998) Methods in Enzymology , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 70
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire, E. Do enthalpy and entropy distinguish first in class from best in class? Drug Discovery Today 2008, 13, 869-874
    • (2008) Drug Discovery Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 71
    • 0036776445 scopus 로고    scopus 로고
    • Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • DOI 10.1128/JVI.76.19.9888-9899.2002
    • Xiang, S. H.; Kwong, P. D.; Gupta, R.; Rizzuto, C. D.; Casper, D. J.; Wyatt, R.; Wang, L.; Hendrickson, W. A.; Doyle, M. L.; Sodroski, J. Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein J. Virol. 2002, 76, 9888-9899 (Pubitemid 35006528)
    • (2002) Journal of Virology , vol.76 , Issue.19 , pp. 9888-9899
    • Xiang, S.-H.1    Kwong, P.D.2    Gupta, R.3    Rizzuto, C.D.4    Casper, D.J.5    Wyatt, R.6    Wang, L.7    Hendrickson, W.A.8    Doyle, M.L.9    Sodroski, J.10
  • 72
    • 84861064300 scopus 로고    scopus 로고
    • We did not obtain X-ray cocrystal structure of antipode (-)- 6 bound to core gp120.
    • We did not obtain X-ray cocrystal structure of antipode (-)- 6 bound to core gp120.
  • 74
    • 5544242529 scopus 로고    scopus 로고
    • MMFF VI. MMFF94s option for energy minimization studies
    • Halgren, T. A. MMFF VI. MMFF94s option for energy minimization studies J. Comput. Chem. 1999, 20, 720-729 (Pubitemid 129652635)
    • (1999) Journal of Computational Chemistry , vol.20 , Issue.7 , pp. 720-729
    • Halgren, T.A.1
  • 75
    • 0001242234 scopus 로고    scopus 로고
    • MMFF MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular- interaction energies and geometries
    • Halgren, T. A. MMFF MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries J. Comput. Chem. 1999, 20, 740-774
    • (1999) J. Comput. Chem. , vol.20 , pp. 740-774
    • Halgren, T.A.1
  • 77
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • DOI 10.1006/jmbi.1998.2401
    • Word, J.; Lovell, S.; Richardson, J.; Richardson, D. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation J. Mol. Biol. 1999, 285, 1735-1747 (Pubitemid 29060467)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 78
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • Jorgensen, W. L.; Maxwell, D. S.; Tirado-Rives, J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids J. Am. Chem. Soc. 1996, 117, 11225-11236 (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 79
    • 0347296066 scopus 로고    scopus 로고
    • Assessing the performance of OMEGA with respect to retrieving bioactive conformations
    • Boström, J.; Greenwood, J. R.; Gottfries, J. Assessing the performance of OMEGA with respect to retrieving bioactive conformations J. Mol. Graphics Modell. 2003, 21
    • (2003) J. Mol. Graphics Modell. , pp. 21
    • Boström, J.1    Greenwood, J.R.2    Gottfries, J.3
  • 80
    • 0030333470 scopus 로고    scopus 로고
    • Three-dimensional hydrogen-bond geometry and probability information from a crystal survey
    • Mills, J. E. J.; Dean, P. M. Three-dimensional hydrogen-bond geometry and probability information from a crystal survey J. Comput.-Aided Mol. Des. 1996, 10, 607
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , pp. 607
    • Mills, J.E.J.1    Dean, P.M.2
  • 81
    • 0035914438 scopus 로고    scopus 로고
    • Ligand binding characteristics of CXCR4 incorporated into paramagnetic proteoliposomes
    • Babcock, G. J.; Mirzabekov, T.; Wojtowicz, W.; Sodroski, J. Ligand binding characteristics of CXCR4 incorporated into paramagnetic proteoliposomes J. Biol. Chem. 2001, 276, 38433-38440
    • (2001) J. Biol. Chem. , vol.276 , pp. 38433-38440
    • Babcock, G.J.1    Mirzabekov, T.2    Wojtowicz, W.3    Sodroski, J.4
  • 83
    • 0019406057 scopus 로고
    • Characterization of the reverse transcriptase from a new retrovirus (HTLV) produced by a human cutaneous T-cell lymphoma cell line
    • DOI 10.1016/0042-6822(81)90642-5
    • Rho, H. M.; Poiesz, B.; Ruscetti, F. W.; Gallo, R. C. Characterization of the reverse transcriptase from a new retrovirus (HTLV) produced by a human cutaneous T-cell lymphoma cell line Virology 1981, 112, 355-360 (Pubitemid 11069788)
    • (1981) Virology , vol.112 , Issue.1 , pp. 355-360
    • Rho, H.M.1    Poiesz, B.2    Ruscetti, F.W.3    Gallo, R.C.4
  • 87
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu, X.; Zhou, T.; O'Dell, S.; Wyatt, R. T.; Kwong, P. D.; Mascola, J. R. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment J. Virol. 2009, 83, 10892-10907
    • (2009) J. Virol. , vol.83 , pp. 10892-10907
    • Wu, X.1    Zhou, T.2    O'Dell, S.3    Wyatt, R.T.4    Kwong, P.D.5    Mascola, J.R.6
  • 88
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. MUSCLE: a multiple sequence alignment method with reduced time and space complexity BMC Bioinf. 2004, 5, 113
    • (2004) BMC Bioinf. , vol.5 , pp. 113
    • Edgar, R.C.1
  • 89
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • Edgar, R. C. MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 2004, 32, 1792-1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 90
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones, D. T.; Taylor, W. R.; Thornton, J. M. The rapid generation of mutation data matrices from protein sequences Comput. Appl. Biosci. 1992, 8, 275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 91
    • 0028177080 scopus 로고
    • A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates
    • Kuhner, M. K.; Felsenstein, J. A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates Mol. Biol. Evol. 1994, 11, 459-468
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 459-468
    • Kuhner, M.K.1    Felsenstein, J.2
  • 93
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 1997, 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 97
    • 84861070555 scopus 로고    scopus 로고
    • DeLano Scientific LLC: South San Francisco, CA; This is an open-source molecular graphics system developed, supported, and maintained by DeLano Scientific LLC (http://www.delanoscientific.com).
    • Delano, W. PyMOL 098; DeLano Scientific LLC: South San Francisco, CA; http://www.pymol.org. This is an open-source molecular graphics system developed, supported, and maintained by DeLano Scientific LLC (http://www.delanoscientific.com).
    • PyMOL 098
    • Delano, W.1


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