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Volumn 17, Issue 33, 2011, Pages 3713-3728

Targeting protein-protein and protein-nucleic acid interactions for Anti-HIV therapy

Author keywords

AIDS; Entry; Gp120 CD4; HIV 1; Nucleocapsid protein NCp7; Protein nucleic acid interactions; Protein protein interactions; Reverse transcriptase dimerization

Indexed keywords

1 BENZOYL 4 [(4,7 DIMETHOXY 1H PYRROLO[2,3 C]PYRIDIN 3 YL)OXOACETYL]PIPERAZINE; 4 BENZOYL 1 [(4 METHOXY 1H PYRROLO[2,3 B]PYRIDIN 3 YL)OXOACETYL] 2 METHYLPIPERAZINE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; BMS 663068; CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CICHORIC ACID; DOUBLE STRANDED RNA; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; IBALIZUMAB; MARAVIROC; NBD 556; NBD 557; NCS 651016; NEF PROTEIN; NUCLEOCAPSID PROTEIN; PROTEIN P51; PROTEIN P66; RNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG; ZINTEVIR;

EID: 82055192318     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161211798220972     Document Type: Article
Times cited : (21)

References (152)
  • 1
    • 29144531173 scopus 로고    scopus 로고
    • The druggable genome: An update
    • Russ AP, Lampel S. The druggable genome: an update. Drug Discov Today 2005; 10 (23-24): 1607-10.
    • (2005) Drug Discov Today , vol.10 , Issue.23-24 , pp. 1607-1610
    • Russ, A.P.1    Lampel, S.2
  • 3
    • 0345600892 scopus 로고    scopus 로고
    • Resistance to imatinib (Glivec): Update on clinical mechanisms
    • Weisberg E, Griffin JD. Resistance to imatinib (Glivec): update on clinical mechanisms. Drug Resist. Updat 2003; 6 (5): 231-8.
    • (2003) Drug Resist. Updat. , vol.6 , Issue.5 , pp. 231-238
    • Weisberg, E.1    Griffin, J.D.2
  • 4
    • 70349739265 scopus 로고    scopus 로고
    • The clinical consequences of antimicrobial resistance
    • Rice LB. The clinical consequences of antimicrobial resistance. Curr Opin Microbiol 2009; 12 (5): 476-81.
    • (2009) Curr Opin Microbiol , vol.12 , Issue.5 , pp. 476-481
    • Rice, L.B.1
  • 5
    • 0032080026 scopus 로고    scopus 로고
    • Cisplatin resistance in cyclic AMPdependent protein kinase mutants
    • Cvijic ME, Yang WL, Chin KV. Cisplatin resistance in cyclic AMPdependent protein kinase mutants. Pharmacol Ther 1998, 78 (2): 115-28.
    • (1998) Pharmacol Ther , vol.78 , Issue.2 , pp. 115-128
    • Cvijic, M.E.1    Yang, W.L.2    Chin, K.V.3
  • 6
    • 1542269164 scopus 로고    scopus 로고
    • The impact of the completed human genome sequence on the development of novel therapeutics for human disease
    • Austin CP. The impact of the completed human genome sequence on the development of novel therapeutics for human disease. Annu Rev Med 2004; 55: 1-13.
    • (2004) Annu Rev Med , vol.55 , pp. 1-13
    • Austin, C.P.1
  • 7
    • 70249108523 scopus 로고    scopus 로고
    • Genome sequence data: Management, storage, and visualization
    • Batley J, Edwards D. Genome sequence data: management, storage, and visualization. Biotechniques 2009; 46 (5): 333-4, 336.
    • (2009) Biotechniques , vol.46 , Issue.5 , pp. 336
    • Batley, J.1    Edwards, D.2
  • 8
    • 0033759749 scopus 로고    scopus 로고
    • Decoding the human genome sequence
    • Bentley DR. Decoding the human genome sequence. Hum. Mol Genet 2000; 9 (16): 2353-2358.
    • (2000) Hum. Mol Genet. , vol.9 , Issue.16 , pp. 2353-2358
    • Bentley, D.R.1
  • 9
    • 0035757207 scopus 로고    scopus 로고
    • Significance of the human genome sequence to drug discovery
    • Grenet O. Significance of the human genome sequence to drug discovery. Pharmacogenomics. J 2001; 1 (1): 11-2.
    • (2001) Pharmacogenomics. J. , vol.1 , Issue.1 , pp. 11-12
    • Grenet, O.1
  • 10
    • 38049079362 scopus 로고    scopus 로고
    • Protein-protein interaction networks and biology--what's the connection?
    • Hakes L, Pinney JW, Robertson DL, Lovell SC. Protein-protein interaction networks and biology--what's the connection? Nat Biotechnol 2008; 26 (1): 69-72.
    • (2008) Nat Biotechnol , vol.26 , Issue.1 , pp. 69-72
    • Hakes, L.1    Pinney, J.W.2    Robertson, D.L.3    Lovell, S.C.4
  • 11
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004; 3 (4): 301-17.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 12
    • 23044496736 scopus 로고    scopus 로고
    • Protein-protein interactions in human disease
    • Ryan DP, Matthews JM. Protein-protein interactions in human disease. Curr Opin Struct Biol 2005; 15 (4): 441-6.
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.4 , pp. 441-446
    • Ryan, D.P.1    Matthews, J.M.2
  • 13
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007; 450 (7172): 1001-9.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 15
    • 0030111082 scopus 로고    scopus 로고
    • Specific targeting of protein-DNA complexes by DNA-reactive drugs (+)-CC-1065 and pluramycins
    • Henderson D, Hurley LH. Specific targeting of protein-DNA complexes by DNA-reactive drugs (+)-CC-1065 and pluramycins. J Mol Recognit 1996, 9 (2): 75-87.
    • (1996) J Mol Recognit , vol.9 , Issue.2 , pp. 75-87
    • Henderson, D.1    Hurley, L.H.2
  • 16
    • 0030133930 scopus 로고    scopus 로고
    • Getting into the major groove. Protein- RNA interactions
    • Moras D, Poterszman A. Getting into the major groove. Protein- RNA interactions. Curr Biol 1996, 6 (5): 530-2.
    • (1996) Curr Biol , vol.6 , Issue.5 , pp. 530-532
    • Moras, D.1
  • 17
    • 71849111303 scopus 로고    scopus 로고
    • A structural perspective of the protein-RNA interactions involved in virus-induced RNA silencing and its suppression
    • Yang J, Yuan YA. A structural perspective of the protein-RNA interactions involved in virus-induced RNA silencing and its suppression. Biochim Biophys Acta 2009; 1789 (9-10): 642-52.
    • (2009) Biochim Biophys Acta , vol.1789 , Issue.9-10 , pp. 642-652
    • Yang, J.1    Yuan, Y.A.2
  • 18
    • 8644234910 scopus 로고    scopus 로고
    • Antibody pharmacokinetics and pharmacodynamics
    • Lobo ED, Hansen RJ, Balthasar JP. Antibody pharmacokinetics and pharmacodynamics. J. Pharm Sci 2004; 93 (11): 2645-68.
    • (2004) J. Pharm Sci. , vol.93 , Issue.11 , pp. 2645-2668
    • Lobo, E.D.1    Hansen, R.J.2    Balthasar, J.P.3
  • 19
    • 38749150330 scopus 로고    scopus 로고
    • The emergence of peptides as therapeutic drugs for the inhibition of HIV-1
    • Huther A, Dietrich U. The emergence of peptides as therapeutic drugs for the inhibition of HIV-1. AIDS Rev 2007; 9 (4) 208-17.
    • (2007) AIDS Rev , vol.9 , Issue.4 , pp. 208-217
    • Huther, A.1    Dietrich, U.2
  • 20
    • 22144454687 scopus 로고    scopus 로고
    • Strategies for targeting protein-protein interactions with synthetic agents
    • Yin H, Hamilton AD. Strategies for targeting protein-protein interactions with synthetic agents. Angew. Chem Int Ed Engl 2005; 44 (27): 4130-63.
    • (2005) Angew. Chem Int Ed Engl. , vol.44 , Issue.27 , pp. 4130-4163
    • Yin, H.1    Hamilton, A.D.2
  • 21
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormonereceptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormonereceptor interface. Science 1995, 267 (5196): 383-6.
    • (1995) Science , vol.267 , Issue.5196 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 22
    • 0037388679 scopus 로고    scopus 로고
    • Protein-protein interactions as a target for drugs in proteomics
    • Archakov AI, Govorun VM, Dubanov AV, et al. Protein-protein interactions as a target for drugs in proteomics. Proteomics 2003; 3 (4): 380-91.
    • (2003) Proteomics , vol.3 , Issue.4 , pp. 380-391
    • Archakov, A.I.1    Govorun, V.M.2    Dubanov, A.V.3
  • 23
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • DeLano WL. Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 2002; 12 (1): 14-20.
    • (2002) Curr Opin Struct Biol , vol.12 , Issue.1 , pp. 14-20
    • Delano, W.L.1
  • 24
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996, 93 (1): 13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.1 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 25
    • 41249099723 scopus 로고    scopus 로고
    • Protein-protein interactions as targets for small-molecule therapeutics in cancer
    • White AW, Westwell AD, Brahemi G. Protein-protein interactions as targets for small-molecule therapeutics in cancer. Expert. Rev Mol Med 2008; 10, e8.
    • (2008) Expert. Rev Mol Med. , vol.10
    • White, A.W.1    Westwell, A.D.2    Brahemi, G.3
  • 26
    • 44849112219 scopus 로고    scopus 로고
    • ABT-263: A potent and orally bioavailable Bcl-2 family inhibitor
    • Tse C, Shoemaker AR, Adickes J, et al. ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor. Cancer Res 2008; 68 (9): 3421-8.
    • (2008) Cancer Res , vol.68 , Issue.9 , pp. 3421-3428
    • Tse, C.1    Shoemaker, A.R.2    Adickes, J.3
  • 27
    • 0141569444 scopus 로고    scopus 로고
    • Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenols targeting B-cell lymphocyte/leukemia-2 proteins
    • Kitada S, Leone M, Sareth S, Zhai D, Reed JC, Pellecchia M. Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenols targeting B-cell lymphocyte/leukemia-2 proteins. J Med Chem 2003; 46 (20): 4259-64.
    • (2003) J Med Chem , vol.46 , Issue.20 , pp. 4259-4264
    • Kitada, S.1    Leone, M.2    Sareth, S.3    Zhai, D.4    Reed, J.C.5    Pellecchia, M.6
  • 28
    • 34247276084 scopus 로고    scopus 로고
    • Pyrogallol-based molecules as potent inhibitors of the antiapoptotic Bcl-2 proteins
    • Tang G, Yang CY, Nikolovska-Coleska Z, et al. Pyrogallol-based molecules as potent inhibitors of the antiapoptotic Bcl-2 proteins. J Med Chem 2007; 50 (8): 1723-6.
    • (2007) J Med Chem , vol.50 , Issue.8 , pp. 1723-1726
    • Tang, G.1    Yang, C.Y.2    Nikolovska-Coleska, Z.3
  • 29
    • 41649102468 scopus 로고    scopus 로고
    • Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition
    • Shangary S, Qin D, McEachern D, et al. Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition. Proc Natl Acad Sci USA 2008; 105 (10): 3933-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 30
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004; 303 (5659): 844-8.
    • (2004) Science , vol.303 , Issue.5659 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 31
    • 49649114644 scopus 로고    scopus 로고
    • Fragment docking to S100 proteins reveals a wide diversity of weak interaction sites
    • Arendt Y, Bhaumik A, Del Conte R, Luchinat C, Mori M, Porcu M. Fragment docking to S100 proteins reveals a wide diversity of weak interaction sites. ChemMedChem 2007; 2 (11): 1648-54.
    • (2007) ChemMedChem , vol.2 , Issue.11 , pp. 1648-1654
    • Arendt, Y.1    Bhaumik, A.2    Del Conte, R.3    Luchinat, C.4    Mori, M.5    Porcu, M.6
  • 32
    • 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 (11): 1302-7.
    • (1998) Nat Med , vol.4 , Issue.11 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3
  • 33
  • 34
    • 27644510382 scopus 로고    scopus 로고
    • Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity
    • Dorr P, Westby M, Dobbs S, et al. Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity. Antimicrob. Agents Chemother 2005; 49 (11): 4721-32.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.11 , pp. 4721-4732
    • Dorr, P.1    Westby, M.2    Dobbs, S.3
  • 35
    • 0141515727 scopus 로고    scopus 로고
    • The effect of NNRTIs on HIV reverse transcriptase dimerization
    • Tachedjian G, Goff SP. The effect of NNRTIs on HIV reverse transcriptase dimerization. Curr Opin Investig Drugs 2003; 4 (8): 966-73.
    • (2003) Curr Opin Investig Drugs , vol.4 , Issue.8 , pp. 966-973
    • Tachedjian, G.1    Goff, S.P.2
  • 36
    • 61949425674 scopus 로고    scopus 로고
    • Strategies for inhibiting function of HIV-1 accessory proteins: A necessary route to AIDS therapy?
    • Richter SN, Frasson I, Palu G. Strategies for inhibiting function of HIV-1 accessory proteins: a necessary route to AIDS therapy? Curr Med Chem 2009; 16 (3): 267-86.
    • (2009) Curr Med Chem , vol.16 , Issue.3 , pp. 267-286
    • Richter, S.N.1    Frasson, I.2    Palu, G.3
  • 37
    • 77952781524 scopus 로고    scopus 로고
    • Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G
    • Cen S, Peng ZG, Li XY, et al. Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G. J. Biol Chem 2010; 285 (22): 16546-52.
    • (2010) J. Biol Chem. , vol.285 , Issue.22 , pp. 16546-16552
    • Cen, S.1    Peng, Z.G.2    Li, X.Y.3
  • 38
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • Christ F, Voet A, Marchand A, et al. Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nat Chem Biol 2010; 6 (6): 442-8.
    • (2010) Nat Chem Biol , vol.6 , Issue.6 , pp. 442-448
    • Christ, F.1    Voet, A.2    Marchand, A.3
  • 39
    • 34347378496 scopus 로고    scopus 로고
    • HIV entry inhibitors
    • Este JA, Telenti A. HIV entry inhibitors. Lancet 2007; 370 (9581): 81-8.
    • (2007) Lancet , vol.370 , Issue.9581 , pp. 81-88
    • Este, J.A.1    Telenti, A.2
  • 40
    • 73549092165 scopus 로고    scopus 로고
    • Entry inhibitors in the treatment of HIV-1 infection
    • Tilton JC, Doms RW. Entry inhibitors in the treatment of HIV-1 infection. Antiviral Res 2010; 85 (1): 91-100.
    • (2010) Antiviral Res , vol.85 , Issue.1 , pp. 91-100
    • Tilton, J.C.1    Doms, R.W.2
  • 41
    • 27144534021 scopus 로고    scopus 로고
    • Anti-HIV agents targeting the interaction of gp120 with the cellular CD4 receptor
    • Vermeire K, Schols D. Anti-HIV agents targeting the interaction of gp120 with the cellular CD4 receptor. Expert. Opin Investig Drugs 2005; 14 (10): 1199-212.
    • (2005) Expert. Opin Investig Drugs. , vol.14 , Issue.10 , pp. 1199-1212
    • Vermeire, K.1    Schols, D.2
  • 42
    • 33645982253 scopus 로고    scopus 로고
    • Inhibitors of HIV infection via the cellular CD4 receptor
    • Vermeire K, Schols D, Bell TW. Inhibitors of HIV infection via the cellular CD4 receptor. Curr Med Chem 2006; 13 (7): 731-43.
    • (2006) Curr Med Chem , vol.13 , Issue.7 , pp. 731-743
    • Vermeire, K.1    Schols, D.2    Bell, T.W.3
  • 43
    • 33846173312 scopus 로고    scopus 로고
    • HIV entry inhibitors targeting gp41: From polypeptides to small-molecule compounds
    • Liu S, Wu S, Jiang S. HIV entry inhibitors targeting gp41: from polypeptides to small-molecule compounds. Curr Pharm Des 2007; 13 (2): 143-62.
    • (2007) Curr Pharm Des , vol.13 , Issue.2 , pp. 143-162
    • Liu, S.1    Wu, S.2    Jiang, S.3
  • 44
    • 70350165412 scopus 로고    scopus 로고
    • Novel drug classes: Entry inhibitors[enfuvirtide, chemokine (C-C motif) receptor 5 antagonists]
    • McKinnell JA, Saag MS. Novel drug classes: entry inhibitors[enfuvirtide, chemokine (C-C motif) receptor 5 antagonists]. Curr Opin HIV. AIDS 2009; 4 (6): 513-7.
    • (2009) Curr Opin HIV. AIDS. , vol.4 , Issue.6 , pp. 513-517
    • McKinnell, J.A.1    Saag, M.S.2
  • 46
    • 65549115032 scopus 로고    scopus 로고
    • The fusion inhibitor enfuvirtide in recent antiretroviral strategies
    • Makinson A, Reynes J. The fusion inhibitor enfuvirtide in recent antiretroviral strategies. Curr Opin HIV. AIDS 2009; 4 (2): 150-8.
    • (2009) Curr Opin HIV. AIDS. , vol.4 , Issue.2 , pp. 150-158
    • Makinson, A.1    Reynes, J.2
  • 47
    • 33746929059 scopus 로고    scopus 로고
    • A novel antiretroviral class (fusion inhibitors) in the management of HIV infection. Present features and future perspectives of enfuvirtide (T-20)
    • Manfredi R, Sabbatani S. A novel antiretroviral class (fusion inhibitors) in the management of HIV infection. Present features and future perspectives of enfuvirtide (T-20). Curr Med Chem 2006; 13 (20): 2369-84.
    • (2006) Curr Med Chem , vol.13 , Issue.20 , pp. 2369-2384
    • Manfredi, R.1    Sabbatani, S.2
  • 48
    • 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 HG, Lin PF. Small-molecule HIV-1 gp120 inhibitors to prevent HIV-1 entry: an emerging opportunity for drug development. Curr Opin Investig Drugs 2006; 7 (8): 721-6.
    • (2006) Curr Opin Investig Drugs , vol.7 , Issue.8 , pp. 721-726
    • Kadow, J.1    Wang, H.G.2    Lin, P.F.3
  • 49
    • 0141703204 scopus 로고    scopus 로고
    • A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding
    • Lin PF, Blair W, Wang T, et al. A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding. Proc Natl Acad Sci USA 2003; 100 (19): 11013-18.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.19 , pp. 11013-11018
    • Lin, P.F.1    Blair, W.2    Wang, T.3
  • 50
    • 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 PM, Bjorkman PJ. 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 (5): 608-13.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.5 , pp. 608-613
    • Diskin, R.1    Marcovecchio, P.M.2    Bjorkman, P.J.3
  • 51
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang CC, Tang M, Zhang MY, et al. Structure of a V3-containing HIV-1 gp120 core. Science 2005; 310 (5750): 1025-8.
    • (2005) Science , vol.310 , Issue.5750 , pp. 1025-1028
    • Huang, C.C.1    Tang, M.2    Zhang, M.Y.3
  • 52
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera M, Majeed S, Ban YE, et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc Natl Acad Sci USA 2010; 107 (3): 1166-71.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.3 , pp. 1166-1171
    • Pancera, M.1    Majeed, S.2    Ban, Y.E.3
  • 53
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393 (6686): 648-59.
    • (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
  • 54
    • 0034482696 scopus 로고    scopus 로고
    • Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    • Kwong PD, Wyatt R, Majeed S, et al. Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. Structure 2000; 8 (12): 1329-39.
    • (2000) Structure , vol.8 , Issue.12 , pp. 1329-1339
    • Kwong, P.D.1    Wyatt, R.2    Majeed, S.3
  • 55
    • 0029062687 scopus 로고
    • Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates
    • Allaway GP, Davis-Bruno KL, Beaudry GA, et al. Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates. AIDS Res. Hum. Retroviruses 1995; 11 (5): 533-9.
    • (1995) AIDS Res. Hum. Retroviruses. , vol.11 , Issue.5 , pp. 533-539
    • Allaway, G.P.1    Davis-Bruno, K.L.2    Beaudry, G.A.3
  • 56
    • 0033914939 scopus 로고    scopus 로고
    • Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults
    • Jacobson JM, Lowy I, Fletcher CV, et al. Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults. J. Infect. Dis 2000; 182 (1): 326-9.
    • (2000) J. Infect. Dis. , vol.182 , Issue.1 , pp. 326-329
    • Jacobson, J.M.1    Lowy, I.2    Fletcher, C.V.3
  • 57
    • 54249125999 scopus 로고    scopus 로고
    • Antiviral activity of single-dose PRO 140, a CCR5 monoclonal antibody, in HIVinfected adults
    • Jacobson JM, Saag MS, Thompson MA, et al. Antiviral activity of single-dose PRO 140, a CCR5 monoclonal antibody, in HIVinfected adults. J. Infect. Dis 2008; 198 (9): 1345-52.
    • (2008) J. Infect. Dis. , vol.198 , Issue.9 , pp. 1345-1352
    • Jacobson, J.M.1    Saag, M.S.2    Thompson, M.A.3
  • 58
    • 0035173073 scopus 로고    scopus 로고
    • Potent, broad-spectrum inhibition of human immunodeficiency virus type 1 by the CCR5 monoclonal antibody PRO 140
    • Trkola A, Ketas TJ, Nagashima KA, et al. Potent, broad-spectrum inhibition of human immunodeficiency virus type 1 by the CCR5 monoclonal antibody PRO 140. J. Virol 2001; 75 (2): 579-88.
    • (2001) J. Virol. , vol.75 , Issue.2 , pp. 579-588
    • Trkola, A.1    Ketas, T.J.2    Nagashima, K.A.3
  • 59
    • 34547646483 scopus 로고    scopus 로고
    • Ibalizumab, a CD4-specific mAb to inhibit HIV-1 infection
    • Dimitrov A. Ibalizumab, a CD4-specific mAb to inhibit HIV-1 infection. Curr Opin Investig Drugs 2007; 8 (8): 653-61.
    • (2007) Curr Opin Investig Drugs , vol.8 , Issue.8 , pp. 653-661
    • Dimitrov, A.1
  • 60
    • 9144236197 scopus 로고    scopus 로고
    • Antiretroviral activity of the anti-CD4 monoclonal antibody TNX-355 in patients infected with HIV type 1
    • Kuritzkes DR, Jacobson J, Powderly WG, et al. Antiretroviral activity of the anti-CD4 monoclonal antibody TNX-355 in patients infected with HIV type 1. J. Infect. Dis 2004; 189 (2): 286-91.
    • (2004) J. Infect. Dis. , vol.189 , Issue.2 , pp. 286-291
    • Kuritzkes, D.R.1    Jacobson, J.2    Powderly, W.G.3
  • 61
    • 72249103816 scopus 로고    scopus 로고
    • Inhibitors of human immunodeficiency virus type 1 (HIV-1) attachment. 5. An evolution from indole to azaindoles leading to the discovery of 1-(4- benzoylpiperazin-1-yl)-2-(4,7-dimethoxy-1H-pyrrolo[2,3-c]pyridin-3-yl)ethane-1,2-dione (BMS-488043), a drug candidate that demonstrates antiviral activity in HIV-1-infected subjects
    • Wang T, Yin Z, Zhang Z, et al. Inhibitors of human immunodeficiency virus type 1 (HIV-1) attachment. 5. An evolution from indole to azaindoles leading to the discovery of 1-(4- benzoylpiperazin-1-yl)-2-(4,7-dimethoxy-1H-pyrrolo[2,3-c]pyridin-3-yl)ethane-1,2-dione (BMS-488043), a drug candidate that demonstrates antiviral activity in HIV-1-infected subjects. J Med Chem 2009; 52 (23): 7778-87.
    • (2009) J Med Chem , vol.52 , Issue.23 , pp. 7778-7787
    • Wang, T.1    Yin, Z.2    Zhang, Z.3
  • 62
    • 0141856289 scopus 로고    scopus 로고
    • Biochemical and genetic characterizations of a novel human immunodeficiency virus type 1 inhibitor that blocks gp120-CD4 interactions
    • Guo Q, Ho HT, Dicker I, et al. Biochemical and genetic characterizations of a novel human immunodeficiency virus type 1 inhibitor that blocks gp120-CD4 interactions. J Virol 2003; 77 (19): 10528-36.
    • (2003) J Virol , vol.77 , Issue.19 , pp. 10528-10536
    • Guo, Q.1    Ho, H.T.2    Dicker, I.3
  • 63
    • 33645766774 scopus 로고    scopus 로고
    • Envelope conformational changes induced by human immunodeficiency virus type 1 attachment inhibitors prevent CD4 binding and downstream entry events
    • Ho HT, Fan L, Nowicka-Sans B, et al. Envelope conformational changes induced by human immunodeficiency virus type 1 attachment inhibitors prevent CD4 binding and downstream entry events. J. Virol 2006; 80 (8): 4017-25.
    • (2006) J. Virol. , vol.80 , Issue.8 , pp. 4017-4025
    • Ho, H.T.1    Fan, L.2    Nowicka-Sans, B.3
  • 64
    • 18744416007 scopus 로고    scopus 로고
    • Highly active antiretroviral therapy: Current state of the art, new agents and their pharmacological interactions useful for improving therapeutic outcome
    • Barbaro G, Scozzafava A, Mastrolorenzo A, Supuran CT. Highly active antiretroviral therapy: current state of the art, new agents and their pharmacological interactions useful for improving therapeutic outcome. Curr Pharm Des 2005; 11 (14): 1805-43.
    • (2005) Curr Pharm Des , vol.11 , Issue.14 , pp. 1805-1843
    • Barbaro, G.1    Scozzafava, A.2    Mastrolorenzo, A.3    Supuran, C.T.4
  • 65
    • 0029160239 scopus 로고
    • Novel sulfonated and phosphonated analogs of distamycin which inhibit the replication of HIV
    • Clanton DJ, Buckheit RW., Jr, Terpening SJ, et al. Novel sulfonated and phosphonated analogs of distamycin which inhibit the replication of HIV. Antiviral Res 1995, 27 (4): 335-54.
    • (1995) Antiviral Res , vol.27 , Issue.4 , pp. 335-354
    • Clanton, D.J.1    Buckheit Jr., R.W.2    Terpening, S.J.3
  • 66
    • 0030727495 scopus 로고    scopus 로고
    • Inhibition of growth factor mitogenicity and growth of tumor cell xenografts by a sulfonated distamycin A derivative
    • Finch PW, Yee LK, Chu MY, et al. Inhibition of growth factor mitogenicity and growth of tumor cell xenografts by a sulfonated distamycin A derivative. Pharmacology 1997, 55 (6): 269-78.
    • (1997) Pharmacology , vol.55 , Issue.6 , pp. 269-278
    • Finch, P.W.1    Yee, L.K.2    Chu, M.Y.3
  • 67
    • 0031694297 scopus 로고    scopus 로고
    • Synthesis and binding mode of heterocyclic analogues of suramin inhibiting the human basic fibroblast growth factor
    • Manetti F, Cappello V, Botta M, et al. Synthesis and binding mode of heterocyclic analogues of suramin inhibiting the human basic fibroblast growth factor. Bioorg. Med Chem 1998, 6 (7): 947-58.
    • (1998) Bioorg. Med Chem. , vol.6 , Issue.7 , pp. 947-958
    • Manetti, F.1    Cappello, V.2    Botta, M.3
  • 68
    • 33745305095 scopus 로고    scopus 로고
    • Anti-angiogenic drugs: From bench to clinical trials
    • Quesada AR, Munoz-Chapuli R, Medina MA. Anti-angiogenic drugs: from bench to clinical trials. Med Res. Rev 2006; 26 (4): 483-530.
    • (2006) Med Res. Rev. , vol.26 , Issue.4 , pp. 483-530
    • Quesada, A.R.1    Munoz-Chapuli, R.2    Medina, M.A.3
  • 69
    • 0026783885 scopus 로고
    • Sulfated polyester interactions with the CD4 molecule and with the third variable loop domain (v3) of gp120 are chemically distinct
    • Lederman S, Bergmann JE, Cleary AM, Yellin MJ, Fusco PJ, Chess L. Sulfated polyester interactions with the CD4 molecule and with the third variable loop domain (v3) of gp120 are chemically distinct. AIDS Res. Hum. Retroviruses 1992, 8 (9): 1599-610.
    • (1992) AIDS Res. Hum. Retroviruses. , vol.8 , Issue.9 , pp. 1599-1610
    • Lederman, S.1    Bergmann, J.E.2    Cleary, A.M.3    Yellin, M.J.4    Fusco, P.J.5    Chess, L.6
  • 70
    • 14444281533 scopus 로고    scopus 로고
    • Polyanion inhibitors of human immunodeficiency virus and other viruses. 6. Micelle-like anti-HIV polyanionic compounds based on a carbohydrate core
    • Leydet A, Jeantet-Segonds C, Bouchitte C, et al. Polyanion inhibitors of human immunodeficiency virus and other viruses. 6. Micelle-like anti-HIV polyanionic compounds based on a carbohydrate core. J. Med Chem 1997, 40 (3): 350-6.
    • (1997) J. Med Chem. , vol.40 , Issue.3 , pp. 350-356
    • Leydet, A.1    Jeantet-Segonds, C.2    Bouchitte, C.3
  • 71
    • 7844226324 scopus 로고    scopus 로고
    • Polyanion inhibitors of HIV and other viruses. 7. Polyanionic compounds and polyzwitterionic compounds derived from cyclodextrins as inhibitors of HIV transmission
    • Leydet A, Moullet C, Roque JP, et al. Polyanion inhibitors of HIV and other viruses. 7. Polyanionic compounds and polyzwitterionic compounds derived from cyclodextrins as inhibitors of HIV transmission. J. Med Chem 1998, 41 (25): 4927-32.
    • (1998) J. Med Chem. , vol.41 , Issue.25 , pp. 4927-4932
    • Leydet, A.1    Moullet, C.2    Roque, J.P.3
  • 72
    • 0027296716 scopus 로고
    • Structure-activity relationship studies with symmetric naphthalenesulfonic acid derivatives. Synthesis and influence of spacer and naphthalenesulfonic acid moiety on anti-HIV-1 activity
    • Mohan P, Wong MF, Verma S, Huang PP, Wickramasinghe A, Baba M. Structure-activity relationship studies with symmetric naphthalenesulfonic acid derivatives. Synthesis and influence of spacer and naphthalenesulfonic acid moiety on anti-HIV-1 activity. J. Med Chem 1993, 36 (14) 1996-2003.
    • (1993) J. Med Chem. , vol.36 , Issue.14 , pp. 1996-2003
    • Mohan, P.1    Wong, M.F.2    Verma, S.3    Huang, P.P.4    Wickramasinghe, A.5    Baba, M.6
  • 73
    • 0034007915 scopus 로고    scopus 로고
    • Research on anti-HIV-1 agents. Investigation on the CD4-Suradista binding mode through docking experiments
    • Manetti F, Corelli F, Mongelli N, Borgia AL, Botta M. Research on anti-HIV-1 agents. Investigation on the CD4-Suradista binding mode through docking experiments. J. Comput. Aided Mol Des 2000; 14 (4): 355-68.
    • (2000) J. Comput. Aided Mol Des. , vol.14 , Issue.4 , pp. 355-368
    • Manetti, F.1    Corelli, F.2    Mongelli, N.3    Borgia, A.L.4    Botta, M.5
  • 74
    • 0033041322 scopus 로고    scopus 로고
    • 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 (1): 85-96.
    • (1999) J. Virol. Methods. , vol.80 , Issue.1 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.A.4
  • 75
    • 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 (17): 3203-9.
    • (1999) J. Med Chem. , vol.42 , Issue.17 , pp. 3203-3209
    • Debnath, A.K.1    Radigan, L.2    Jiang, S.3
  • 76
    • 71249111434 scopus 로고    scopus 로고
    • ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation
    • Wang H, Qi Z, Guo A, et al. ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation. Antimicrob. Agents Chemother 2009; 53 (12): 4987-98.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.12 , pp. 4987-4998
    • Wang, H.1    Qi, Z.2    Guo, A.3
  • 79
    • 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
    • Zhao Q, Ma L, Jiang S, et al. 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 (2): 213-25.
    • (2005) Virology , vol.339 , Issue.2 , pp. 213-225
    • Zhao, Q.1    Ma, L.2    Jiang, S.3
  • 80
    • 77949537282 scopus 로고    scopus 로고
    • Naturally occurring variability in the envelope glycoprotein of HIV-1 and development of cell entry inhibitors
    • Brower ET, Schon A, Freire E. Naturally occurring variability in the envelope glycoprotein of HIV-1 and development of cell entry inhibitors. Biochemistry 2010; 49 (11): 2359-67.
    • (2010) Biochemistry , vol.49 , Issue.11 , pp. 2359-2367
    • Brower, E.T.1    Schon, A.2    Freire, E.3
  • 81
    • 55249083812 scopus 로고    scopus 로고
    • Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120
    • Madani N, Schon A, Princiotto AM, et al. Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120. Structure 2008; 16 (11): 1689-701.
    • (2008) Structure , vol.16 , Issue.11 , pp. 1689-1701
    • Madani, N.1    Schon, A.2    Princiotto, A.M.3
  • 82
    • 71749107966 scopus 로고    scopus 로고
    • dynamic target-based pharmacophoric model mapping the CD4 binding site on HIV-1 gp120 to identify new inhibitors of gp120- CD4 protein-protein interactions
    • Caporuscio F, Tafi A, Gonzalez E, Manetti F, Este JA, Botta M. A dynamic target-based pharmacophoric model mapping the CD4 binding site on HIV-1 gp120 to identify new inhibitors of gp120- CD4 protein-protein interactions. Bioorg. Med Chem Lett 2009; 19 (21): 6087-91.
    • (2009) Bioorg. Med Chem Lett. , vol.19 , Issue.21 , pp. 6087-6091
    • Caporuscio, F.1    Tafi, A.2    Gonzalez, E.3    Manetti, F.4    Este, J.A.5    Botta, M.A.6
  • 83
    • 0038748179 scopus 로고    scopus 로고
    • Virtual screening of virtual libraries
    • Green DV. Virtual screening of virtual libraries. Prog. Med Chem 2003; 41: 61-97.
    • (2003) Prog. Med Chem. , vol.41 , pp. 61-97
    • Green, D.V.1
  • 84
    • 39049094335 scopus 로고    scopus 로고
    • Virtual screening and its integration with modern drug design technologies
    • Guido RV, Oliva G, Andricopulo AD. Virtual screening and its integration with modern drug design technologies. Curr Med Chem 2008; 15 (1): 37-46.
    • (2008) Curr Med Chem , vol.15 , Issue.1 , pp. 37-46
    • Guido, R.V.1    Oliva, G.2    Andricopulo, A.D.3
  • 85
    • 41149151814 scopus 로고    scopus 로고
    • Anti-HIV activity and resistance profile of the CXC chemokine receptor 4 antagonist POL3026
    • Moncunill G, Armand-Ugon M, Clotet-Codina I, et al. Anti-HIV activity and resistance profile of the CXC chemokine receptor 4 antagonist POL3026. Mol Pharmacol 2008; 73 (4): 1264-73.
    • (2008) Mol Pharmacol , vol.73 , Issue.4 , pp. 1264-1273
    • Moncunill, G.1    Armand-Ugon, M.2    Clotet-Codina, I.3
  • 86
    • 37349119039 scopus 로고    scopus 로고
    • HIV-1 escape to CCR5 coreceptor antagonism through selection of CXCR4-using variants in vitro
    • Moncunill G, Armand-Ugon M, Pauls E, Clotet B, Este JA. HIV-1 escape to CCR5 coreceptor antagonism through selection of CXCR4-using variants in vitro. AIDS 2008; 22 (1): 23-31.
    • (2008) AIDS , vol.22 , Issue.1 , pp. 23-31
    • Moncunill, G.1    Armand-Ugon, M.2    Pauls, E.3    Clotet, B.4    Este, J.A.5
  • 88
    • 0026503970 scopus 로고
    • RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms
    • Restle T, Muller B, Goody RS. RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms. FEBS Lett 1992 300 (1): 97-100.
    • (1992) FEBS Lett , vol.300 , Issue.1 , pp. 97-100
    • Restle, T.1    Muller, B.2    Goody, R.S.3
  • 89
    • 0026647870 scopus 로고
    • Structurefunction relationships of HIV-1 reverse transcriptase determined using monoclonal antibodies
    • Restle T, Pawlita M, Sczakiel G, Muller B, Goody RS. Structurefunction relationships of HIV-1 reverse transcriptase determined using monoclonal antibodies. J Biol Chem 1992, 267 (21): 14654-61.
    • (1992) J Biol Chem , vol.267 , Issue.21 , pp. 14654-14661
    • Restle, T.1    Pawlita, M.2    Sczakiel, G.3    Muller, B.4    Goody, R.S.5
  • 90
    • 0028964233 scopus 로고
    • Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: A two step process
    • Divita G, Rittinger K, Geourjon C, Deleage G, Goody RS. Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: a two step process. J Mol Biol 1995, 245 (5): 508-21.
    • (1995) J Mol Biol , vol.245 , Issue.5 , pp. 508-521
    • Divita, G.1    Rittinger, K.2    Geourjon, C.3    Deleage, G.4    Goody, R.S.5
  • 91
    • 0037436335 scopus 로고    scopus 로고
    • Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization
    • Tachedjian G, Aronson HE, de los SM, Seehra J, McCoy JM, Goff SP. Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization. J Mol Biol 2003; 326 (2): 381-96.
    • (2003) J Mol Biol , vol.326 , Issue.2 , pp. 381-396
    • Tachedjian, G.1    Aronson, H.E.2    de los, S.M.3    Seehra, J.4    McCoy, J.M.5    Goff, S.P.6
  • 92
    • 19444375120 scopus 로고    scopus 로고
    • Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions
    • Mulky A, Sarafianos SG, Jia Y, Arnold E, Kappes JC. Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions. J Mol Biol 2005; 349 (4): 673-84.
    • (2005) J Mol Biol , vol.349 , Issue.4 , pp. 673-684
    • Mulky, A.1    Sarafianos, S.G.2    Jia, Y.3    Arnold, E.4    Kappes, J.C.5
  • 93
    • 70350066155 scopus 로고    scopus 로고
    • Crystallographic study of a novel subnanomolar inhibitor provides insight on the binding interactions of alkenyldiarylmethanes with human immunodeficiency virus-1 reverse transcriptase
    • Cullen MD, Ho WC, Bauman JD, et al. Crystallographic study of a novel subnanomolar inhibitor provides insight on the binding interactions of alkenyldiarylmethanes with human immunodeficiency virus-1 reverse transcriptase. J. Med Chem 2009; 52 (20): 6467-73.
    • (2009) J. Med Chem. , vol.52 , Issue.20 , pp. 6467-6473
    • Cullen, M.D.1    Ho, W.C.2    Bauman, J.D.3
  • 94
    • 77952724079 scopus 로고    scopus 로고
    • Crystal Structures of HIV-1 Reverse Transcriptase with Etravirine (TMC125) and Rilpivirine (TMC278): Implications for Drug Design
    • Lansdon EB, Brendza KM, Hung M, et al. Crystal Structures of HIV-1 Reverse Transcriptase with Etravirine (TMC125) and Rilpivirine (TMC278): Implications for Drug Design. J Med Chem 2010.
    • (2010) J Med Chem
    • Lansdon, E.B.1    Brendza, K.M.2    Hung, M.3
  • 95
    • 0028947588 scopus 로고
    • High resolution structures of HIV-1 RT from four RT-inhibitor complexes
    • Ren J, Esnouf R, Garman E, et al. High resolution structures of HIV-1 RT from four RT-inhibitor complexes. Nat Struct Biol 1995, 2 (4): 293-302.
    • (1995) Nat Struct Biol , vol.2 , Issue.4 , pp. 293-302
    • Ren, J.1    Esnouf, R.2    Garman, E.3
  • 96
    • 58649097300 scopus 로고    scopus 로고
    • A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility
    • Agopian A, Gros E, Aldrian-Herrada G, Bosquet N, Clayette P, Divita G. A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. J Biol Chem 2009; 284 (1): 254-64.
    • (2009) J Biol Chem , vol.284 , Issue.1 , pp. 254-264
    • Agopian, A.1    Gros, E.2    Aldrian-Herrada, G.3    Bosquet, N.4    Clayette, P.5    Divita, G.6
  • 97
    • 0028308202 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain
    • Divita G, Restle T, Goody RS, Chermann JC, Baillon JG. Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. J. Biol Chem 1994; 269 (18): 13080-3.
    • (1994) J. Biol Chem. , vol.269 , Issue.18 , pp. 13080-13083
    • Divita, G.1    Restle, T.2    Goody, R.S.3    Chermann, J.C.4    Baillon, J.G.5
  • 98
    • 0033609895 scopus 로고    scopus 로고
    • New potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains
    • Morris MC, Robert-Hebmann V, Chaloin L, et al. new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains. J Biol Chem 1999, 274 (35): 24941-6.
    • (1999) J Biol Chem , vol.274 , Issue.35 , pp. 24941-24946
    • Morris, M.C.1    Robert-Hebmann, V.2    Chaloin, L.3
  • 99
    • 0025992146 scopus 로고
    • A leucine zipper-like motif may mediate HIV reverse transcriptase subunit binding
    • Baillon JG, Nashed NT, Kumar A, Wilson SH, Jerina DM. A leucine zipper-like motif may mediate HIV reverse transcriptase subunit binding. New Biol 1991, 3 (10): 1015-1019.
    • (1991) New Biol , vol.3 , Issue.10 , pp. 1015-1019
    • Baillon, J.G.1    Nashed, N.T.2    Kumar, A.3    Wilson, S.H.4    Jerina, D.M.5
  • 100
    • 0034673154 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[Spiro[4-amino-2,2 -dioxo-1,2 - oxathiole-5,3'-[2', 5'-bis-O-(tert-butyldimethylsilyl)-beta-Dribofuranosyl]]]-3-ethylthy mine
    • Sluis-Cremer N, Dmitrienko GI, Balzarini J, Camarasa MJ, Parniak MA. Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[Spiro[4-amino-2,2 -dioxo-1,2 - oxathiole-5,3'-[2', 5'-bis-O-(tert-butyldimethylsilyl)-beta-Dribofuranosyl]]]-3-ethylthy mine. Biochemistry 2000; 39 (6): 1427-33.
    • (2000) Biochemistry , vol.39 , Issue.6 , pp. 1427-1433
    • Sluis-Cremer, N.1    Dmitrienko, G.I.2    Balzarini, J.3    Camarasa, M.J.4    Parniak, M.A.5
  • 101
    • 33746948397 scopus 로고    scopus 로고
    • Structure-activity relationships of [2',5'-bis-O-(tertbutyldimethylsilyl)- beta-D-ribofuranosyl]- 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization
    • Sluis-Cremer N, Hamamouch N, San FA, Velazquez S, Balzarini J, Camarasa MJ. Structure-activity relationships of [2',5'-bis-O-(tertbutyldimethylsilyl)- beta-D-ribofuranosyl]- 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization. J Med Chem 2006; 49 (16): 4834-41.
    • (2006) J Med Chem , vol.49 , Issue.16 , pp. 4834-4841
    • Sluis-Cremer, N.1    Hamamouch, N.2    San, F.A.3    Velazquez, S.4    Balzarini, J.5    Camarasa, M.J.6
  • 102
    • 79955434216 scopus 로고    scopus 로고
    • Crystal structure of tertbutyldimethylsilyl - spiroaminooxathioledioxide-thymine (TSAO-T) in complex with HIV-1 reverse transcriptase (RT) redefines the elastic limits of the non-nucleoside inhibitor-binding pocket
    • Das K, Bauman JD, Rim AS, et al. Crystal structure of tertbutyldimethylsilyl- spiroaminooxathioledioxide-thymine (TSAO-T) in complex with HIV-1 reverse transcriptase (RT) redefines the elastic limits of the non-nucleoside inhibitor-binding pocket. J Med Chem 2011; 54 (8): 2727-37.
    • (2011) J Med Chem , vol.54 , Issue.8 , pp. 2727-2737
    • Das, K.1    Bauman, J.D.2    Rim, A.S.3
  • 103
    • 0036076157 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors
    • Sluis-Cremer N, Arion D, Parniak MA. Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors. Mol Pharmacol 2002; 62 (2): 398-405.
    • (2002) Mol Pharmacol , vol.62 , Issue.2 , pp. 398-405
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 104
    • 44049097439 scopus 로고    scopus 로고
    • Small molecule inhibitors targeting HIV-1 reverse transcriptase dimerization
    • Grohmann D, Corradi V, Elbasyouny M, et al. Small molecule inhibitors targeting HIV-1 reverse transcriptase dimerization. Chembiochem 2008; 9 (6): 916-22.
    • (2008) Chembiochem , vol.9 , Issue.6 , pp. 916-922
    • Grohmann, D.1    Corradi, V.2    Elbasyouny, M.3
  • 105
    • 73449135109 scopus 로고    scopus 로고
    • Chemical library screens targeting an HIV-1 accessory factor/host cell kinase complex identify novel antiretroviral compounds
    • Emert-Sedlak L, Kodama T, Lerner EC, et al. Chemical library screens targeting an HIV-1 accessory factor/host cell kinase complex identify novel antiretroviral compounds. ACS Chem Biol 2009; 4 (11): 939-947.
    • (2009) ACS Chem Biol , vol.4 , Issue.11 , pp. 939-947
    • Emert-Sedlak, L.1    Kodama, T.2    Lerner, E.C.3
  • 106
    • 0031464721 scopus 로고    scopus 로고
    • Structure, biological functions and inhibition of the HIV-1 proteins Vpr and NCp7
    • Roques BP, Morellet N, de RH, Demene H, Schueler W, Jullian N. Structure, biological functions and inhibition of the HIV-1 proteins Vpr and NCp7. Biochimie 1997; 79 (11): 673-80.
    • (1997) Biochimie , vol.79 , Issue.11 , pp. 673-680
    • Roques, B.P.1    Morellet, N.2    de, R.H.3    Demene, H.4    Schueler, W.5    Jullian, N.6
  • 108
    • 0028128116 scopus 로고
    • Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR
    • Morellet N, de Rocquigny H, Mely Y, et al. Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR. J. Mol Biol 1994; 235 (1): 287-301.
    • (1994) J. Mol Biol. , vol.235 , Issue.1 , pp. 287-301
    • Morellet, N.1    de Rocquigny, H.2    Mely, Y.3
  • 109
    • 52249111350 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein NCp7 and its RNA stem loop 3 partner: Rotational dynamics of spin-labeled RNA stem loop 3
    • Xi X, Sun Y, Karim CB, Grigoryants VM, Scholes CP. HIV-1 nucleocapsid protein NCp7 and its RNA stem loop 3 partner: rotational dynamics of spin-labeled RNA stem loop 3. Biochemistry 2008; 47 (38): 10099-110.
    • (2008) Biochemistry , vol.47 , Issue.38 , pp. 10099-10110
    • Xi, X.1    Sun, Y.2    Karim, C.B.3    Grigoryants, V.M.4    Scholes, C.P.5
  • 110
    • 77951677592 scopus 로고    scopus 로고
    • The nucleocapsid protein of HIV-1 as a promising therapeuic target for antiviral drugs
    • Goldschmidt V, MIller Jenkins ML, de Rocquigny H, Darlix JL, Mely Y. The nucleocapsid protein of HIV-1 as a promising therapeuic target for antiviral drugs. HIV Ther 2010; 4 (2): 179-98.
    • (2010) HIV Ther , vol.4 , Issue.2 , pp. 179-198
    • Goldschmidt, V.1    MIller Jenkins, M.L.2    de Rocquigny, H.3    Darlix, J.L.4    Mely, Y.5
  • 111
    • 0032570327 scopus 로고    scopus 로고
    • The annealing of tRNA3Lys to human immunodeficiency virus type 1 primer binding site is critically dependent on the NCp7 zinc fingers structure
    • Remy E, de Rocquigny H, Petitjean P, et al. The annealing of tRNA3Lys to human immunodeficiency virus type 1 primer binding site is critically dependent on the NCp7 zinc fingers structure. J. Biol Chem 1998, 273 (9): 4819-22.
    • (1998) J. Biol Chem. , vol.273 , Issue.9 , pp. 4819-4822
    • Remy, E.1    de Rocquigny, H.2    Petitjean, P.3
  • 112
    • 20844463873 scopus 로고    scopus 로고
    • Structural determinants of HIV-1 nucleocapsid protein for cTAR DNA binding and destabilization, and correlation with inhibition of self-primed DNA synthesis
    • Beltz H, Clauss C, Piemont E, et al. Structural determinants of HIV-1 nucleocapsid protein for cTAR DNA binding and destabilization, and correlation with inhibition of self-primed DNA synthesis. J Mol Biol 2005; 348 (5): 1113-26.
    • (2005) J Mol Biol , vol.348 , Issue.5 , pp. 1113-11126
    • Beltz, H.1    Clauss, C.2    Piemont, E.3
  • 113
    • 0033020588 scopus 로고    scopus 로고
    • Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: Influence of the binding of nucleic acids
    • Bombarda E, Ababou A, Vuilleumier C, et al. Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: influence of the binding of nucleic acids. Biophys J 1999, 76 (3): 1561-70.
    • (1999) Biophys J , vol.76 , Issue.3 , pp. 1561-1570
    • Bombarda, E.1    Ababou, A.2    Vuilleumier, C.3
  • 114
    • 0027374171 scopus 로고
    • Structural and dynamic characterization of the aromatic amino acids of the human immunodeficiency virus type I nucleocapsid protein zinc fingers and their involvement in heterologous tRNA(Phe) binding: A steady-state and time-resolved fluorescence study
    • Mely Y, Piemont E, Sorinas-Jimeno M, et al. Structural and dynamic characterization of the aromatic amino acids of the human immunodeficiency virus type I nucleocapsid protein zinc fingers and their involvement in heterologous tRNA(Phe) binding: a steady-state and time-resolved fluorescence study. Biophys J 1993, 65 (4): 1513-22.
    • (1993) Biophys J , vol.65 , Issue.4 , pp. 1513-1522
    • Mely, Y.1    Piemont, E.2    Sorinas-Jimeno, M.3
  • 116
    • 23144448275 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: Critical role in reverse transcription and molecular mechanism
    • Levin JG, Guo J, Rouzina I, Musier-Forsyth K. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. Prog Nucleic Acid Res Mol Biol 2005; 80: 217-86.
    • (2005) Prog Nucleic Acid Res Mol Biol , vol.80 , pp. 217-286
    • Levin, J.G.1    Guo, J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 117
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • Rein A, Henderson LE, Levin JG. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem Sci 1998, 23 (8): 297-301.
    • (1998) Trends Biochem Sci , vol.23 , Issue.8 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 118
    • 18544382982 scopus 로고    scopus 로고
    • Mechanism of zinc coordination by point-mutated structures of the distal CCHC binding motif of the HIV-1 NCp7 protein
    • Bombarda E, Roques BP, Mely Y, Grell E. Mechanism of zinc coordination by point-mutated structures of the distal CCHC binding motif of the HIV-1 NCp7 protein. Biochemistry 2005; 44 (19): 7315-25.
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7315-7325
    • Bombarda, E.1    Roques, B.P.2    Mely, Y.3    Grell, E.4
  • 120
    • 2942739181 scopus 로고    scopus 로고
    • Structure of the His44 --> Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: A combined NMR, molecular dynamics simulation, and fluorescence study
    • Stote RH, Kellenberger E, Muller H, et al. Structure of the His44 --> Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: a combined NMR, molecular dynamics simulation, and fluorescence study. Biochemistry 2004; 43 (24): 7687-97.
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7687-7697
    • Stote, R.H.1    Kellenberger, E.2    Muller, H.3
  • 121
    • 36749073433 scopus 로고    scopus 로고
    • The design of drugs for HIV and HCV
    • De Clercq E. The design of drugs for HIV and HCV. Nat Rev Drug Discov 2007; 6 (12): 1001-18.
    • (2007) Nat Rev Drug Discov , vol.6 , Issue.12 , pp. 1001-1018
    • de Clercq, E.1
  • 122
    • 0030667386 scopus 로고    scopus 로고
    • The zinc fingers of HIV nucleocapsid protein NCp7 direct interactions with the viral regulatory protein Vpr
    • de Rocquigny H, Petitjean P, Tanchou V, et al. The zinc fingers of HIV nucleocapsid protein NCp7 direct interactions with the viral regulatory protein Vpr. J. Biol Chem 1997, 272 (49): 30753-9.
    • (1997) J. Biol Chem. , vol.272 , Issue.49 , pp. 30753-30759
    • de Rocquigny, H.1    Petitjean, P.2    Tanchou, V.3
  • 123
    • 0033574629 scopus 로고    scopus 로고
    • Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1
    • Druillennec S, Caneparo A, de Rocquigny H, Roques BP. Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1. J. Biol Chem 1999, 274 (16): 11283-8.
    • (1999) J. Biol Chem. , vol.274 , Issue.16 , pp. 11283-11288
    • Druillennec, S.1    Caneparo, A.2    de Rocquigny, H.3    Roques, B.P.4
  • 124
    • 33645231680 scopus 로고    scopus 로고
    • Basic residues in the nucleocapsid domain of Gag are required for interaction of HIV-1 gag with ABCE1 (HP68), a cellular protein important for HIV-1 capsid assembly
    • Lingappa JR, Dooher JE, Newman MA, Kiser PK, Klein KC. Basic residues in the nucleocapsid domain of Gag are required for interaction of HIV-1 gag with ABCE1 (HP68), a cellular protein important for HIV-1 capsid assembly. J. Biol Chem 2006; 281 (7): 3773-84.
    • (2006) J. Biol Chem. , vol.281 , Issue.7 , pp. 3773-3784
    • Lingappa, J.R.1    Dooher, J.E.2    Newman, M.A.3    Kiser, P.K.4    Klein, K.C.5
  • 125
    • 38349174466 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid
    • Popov S, Popova E, Inoue M, Gottlinger HG. Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid. J. Virol 2008; 82 (3): 1389-98.
    • (2008) J. Virol. , vol.82 , Issue.3 , pp. 1389-1398
    • Popov, S.1    Popova, E.2    Inoue, M.3    Gottlinger, H.G.4
  • 126
    • 20944436272 scopus 로고    scopus 로고
    • Studies on the mechanism of inactivation of the HIV-1 nucleocapsid protein NCp7 with 2- mercaptobenzamide thioesters
    • Jenkins LM, Byrd JC, Hara T, et al. Studies on the mechanism of inactivation of the HIV-1 nucleocapsid protein NCp7 with 2- mercaptobenzamide thioesters. J. Med Chem 2005; 48 (8): 2847-58.
    • (2005) J. Med Chem. , vol.48 , Issue.8 , pp. 2847-2858
    • Jenkins, L.M.1    Byrd, J.C.2    Hara, T.3
  • 127
    • 34548775160 scopus 로고    scopus 로고
    • Specificity of acyl transfer from 2-mercaptobenzamide thioesters to the HIV-1 nucleocapsid protein
    • Miller Jenkins LM, Hara T, Durell SR, et al. Specificity of acyl transfer from 2-mercaptobenzamide thioesters to the HIV-1 nucleocapsid protein. J. Am. Chem Soc 2007; 129 (36): 11067-78.
    • (2007) J. Am. Chem Soc. , vol.129 , Issue.36 , pp. 11067-11078
    • Miller Jenkins, L.M.1    Hara, T.2    Durell, S.R.3
  • 129
    • 49149112473 scopus 로고    scopus 로고
    • Examination of specific binding activity of aptamer RNAs to the HIV-NC by using a cellbased in vivo assay for protein-RNA interaction
    • Jeong YY, Kim SH, Jang SI, You JC. Examination of specific binding activity of aptamer RNAs to the HIV-NC by using a cellbased in vivo assay for protein-RNA interaction. BMB. Rep 2008; 41 (7): 511-5.
    • (2008) BMB. Rep. , vol.41 , Issue.7 , pp. 511-515
    • Jeong, Y.Y.1    Kim, S.H.2    Jang, S.I.3    You, J.C.4
  • 130
    • 0036296520 scopus 로고    scopus 로고
    • Selection and stabilization of the RNA aptamers against the human immunodeficiency virus type-1 nucleocapsid protein
    • Kim SJ, Kim MY, Lee JH, You JC, Jeong S. Selection and stabilization of the RNA aptamers against the human immunodeficiency virus type-1 nucleocapsid protein. Biochem Biophys Res. Commun 2002; 291 (4): 925-31.
    • (2002) Biochem Biophys Res. Commun. , vol.291 , Issue.4 , pp. 925-931
    • Kim, S.J.1    Kim, M.Y.2    Lee, J.H.3    You, J.C.4    Jeong, S.5
  • 131
    • 47649101873 scopus 로고    scopus 로고
    • Inhibition of HIV-1 by a peptide ligand of the genomic RNA packaging signal Psi
    • Dietz J, Koch J, Kaur A, et al. Inhibition of HIV-1 by a peptide ligand of the genomic RNA packaging signal Psi. ChemMedChem 2008; 3 (5): 749-55.
    • (2008) ChemMedChem , vol.3 , Issue.5 , pp. 749-755
    • Dietz, J.1    Koch, J.2    Kaur, A.3
  • 132
    • 33746610513 scopus 로고    scopus 로고
    • tryptophan-rich hexapeptide inhibits nucleic acid destabilization chaperoned by the HIV-1 nucleocapsid protein
    • Raja C, Ferner J, Dietrich U, et al tryptophan-rich hexapeptide inhibits nucleic acid destabilization chaperoned by the HIV-1 nucleocapsid protein. Biochemistry 2006; 45 (30): 9254-9265.
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9254-9265
    • Raja, C.1    Ferner, J.2    Dietrich, U.3
  • 133
    • 77950405709 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by small interfering RNAs directed against glioma pathogenesis related protein (GliPR) expression
    • Capalbo G, Muller-Kuller T, Dietrich U, Hoelzer D, Ottmann OG, Scheuring UJ. Inhibition of HIV-1 replication by small interfering RNAs directed against glioma pathogenesis related protein (GliPR) expression. Retrovirology 2010; 7: 26.
    • (2010) Retrovirology , vol.7 , pp. 26
    • Capalbo, G.1    Muller-Kuller, T.2    Dietrich, U.3    Hoelzer, D.4    Ottmann, O.G.5    Scheuring, U.J.6
  • 135
    • 0036392158 scopus 로고    scopus 로고
    • Identification of HIV-1 nucleocapsid protein: Nucleic acid antagonists with cellular anti-HIV activity
    • Stephen AG, Worthy KM, Towler E, et al. Identification of HIV-1 nucleocapsid protein: nucleic acid antagonists with cellular anti-HIV activity. Biochem Biophys Res. Commun 2002; 296 (5): 1228-37.
    • (2002) Biochem Biophys Res. Commun. , vol.296 , Issue.5 , pp. 1228-1237
    • Stephen, A.G.1    Worthy, K.M.2    Towler, E.3
  • 136
    • 40049099434 scopus 로고    scopus 로고
    • Targeting the viral nucleocapsid protein in anti-HIV-1 therapy
    • de Rocquigny H, Shvadchak V, Avilov S, et al. Targeting the viral nucleocapsid protein in anti-HIV-1 therapy. Mini. Rev Med Chem 2008; 8 (1): 24-35.
    • (2008) Mini. Rev Med Chem. , vol.8 , Issue.1 , pp. 24-35
    • de Rocquigny, H.1    Shvadchak, V.2    Avilov, S.3
  • 137
    • 66049123942 scopus 로고    scopus 로고
    • Identification by high throughput screening of small compounds inhibiting the nucleic acid destabilization activity of the HIV-1 nucleocapsid protein
    • Shvadchak V, Sanglier S, Rocle S, et al. Identification by high throughput screening of small compounds inhibiting the nucleic acid destabilization activity of the HIV-1 nucleocapsid protein. Biochimie 2009; 91 (7): 916-23.
    • (2009) Biochimie , vol.91 , Issue.7 , pp. 916-923
    • Shvadchak, V.1    Sanglier, S.2    Rocle, S.3
  • 138
    • 53749093357 scopus 로고    scopus 로고
    • How the HIV-1 nucleocapsid protein binds and destabilises the (-)primer binding site during reverse transcription
    • Bourbigot S, Ramalanjaona N, Boudier C, et al. How the HIV-1 nucleocapsid protein binds and destabilises the (-)primer binding site during reverse transcription. J. Mol Biol 2008; 383 (5): 1112-28.
    • (2008) J. Mol Biol. , vol.383 , Issue.5 , pp. 1112-1128
    • Bourbigot, S.1    Ramalanjaona, N.2    Boudier, C.3
  • 139
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 1998, 279 (5349): 384-8.
    • (1998) Science , vol.279 , Issue.5349 , pp. 384-388
    • de Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 140
    • 41949132326 scopus 로고    scopus 로고
    • Overcoming the inadequacies or limitations of experimental structures as drug targets by using computational modeling tools and molecular dynamics simulations
    • Marco E, Gago F. Overcoming the inadequacies or limitations of experimental structures as drug targets by using computational modeling tools and molecular dynamics simulations. ChemMedChem 2007; 2 (10): 1388-401.
    • (2007) ChemMedChem , vol.2 , Issue.10 , pp. 1388-1401
    • Marco, E.1    Gago, F.2
  • 141
    • 77951998515 scopus 로고    scopus 로고
    • Molecular dynamics and DFT study on HIV-1 nucleocapsid protein-7 in complex with viral genome
    • Mori M, Dietrich U, Manetti F, Botta M. Molecular dynamics and DFT study on HIV-1 nucleocapsid protein-7 in complex with viral genome. J. Chem Inf. Model 2010; 50 (4): 638-50.
    • (2010) J. Chem Inf. Model. , vol.50 , Issue.4 , pp. 638-650
    • Mori, M.1    Dietrich, U.2    Manetti, F.3    Botta, M.4
  • 142
    • 79952168198 scopus 로고    scopus 로고
    • Predicting the binding mode of known NCp7 inhibitors to facilitate the design of novel modulators
    • Mori M, Manetti F, Botta M. Predicting the binding mode of known NCp7 inhibitors to facilitate the design of novel modulators. J. Chem Inf. Model 2011; 51 (2): 446-54.
    • (2011) J. Chem Inf. Model. , vol.51 , Issue.2 , pp. 446-454
    • Mori, M.1    Manetti, F.2    Botta, M.3
  • 144
    • 59849109511 scopus 로고    scopus 로고
    • Dimer disruption and monomer sequestration by alkyl tripeptides are successful strategies for inhibiting wild-type and multidrug-resistant mutated HIV-1 proteases
    • Bannwarth L, Rose T, Dufau L, et al. Dimer disruption and monomer sequestration by alkyl tripeptides are successful strategies for inhibiting wild-type and multidrug-resistant mutated HIV-1 proteases. Biochemistry 2009; 48 (2): 379-87.
    • (2009) Biochemistry , vol.48 , Issue.2 , pp. 379-387
    • Bannwarth, L.1    Rose, T.2    Dufau, L.3
  • 145
    • 0026031075 scopus 로고
    • Inhibition of HIV protease activity by heterodimer formation
    • Babe LM, Pichuantes S, Craik CS. Inhibition of HIV protease activity by heterodimer formation. Biochemistry 1991, 30 (1): 106-11.
    • (1991) Biochemistry , vol.30 , Issue.1 , pp. 106-111
    • Babe, L.M.1    Pichuantes, S.2    Craik, C.S.3
  • 146
    • 0025986843 scopus 로고
    • Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide
    • Zhang ZY, Poorman RA, Maggiora LL, Heinrikson RL, Kezdy FJ. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. J. Biol Chem 1991, 266 (24): 15591-94.
    • (1991) J. Biol Chem. , vol.266 , Issue.24 , pp. 15591-15594
    • Zhang, Z.Y.1    Poorman, R.A.2    Maggiora, L.L.3    Heinrikson, R.L.4    Kezdy, F.J.5
  • 147
    • 0030969462 scopus 로고    scopus 로고
    • Targeting the dimerization interface of HIV-1 protease: Inhibition with crosslinked interfacial peptides
    • Zutshi R, Franciskovich J, Shultz M, et al. Targeting the dimerization interface of HIV-1 protease: Inhibition with crosslinked interfacial peptides. Journal of the American Chemical Society 1997, 119 (21): 4841-5.
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.21 , pp. 4841-4845
    • Zutshi, R.1    Franciskovich, J.2    Shultz, M.3
  • 148
    • 0033602546 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of conformationally constrained tongs, new inhibitors of HIV-1 protease dimerization
    • Bouras A, Boggetto N, Benatalah Z, de RE, Sicsic S, Reboud- Ravaux M. Design, synthesis, and evaluation of conformationally constrained tongs, new inhibitors of HIV-1 protease dimerization. J. Med Chem 1999, 42 (6): 957-62.
    • (1999) J. Med Chem. , vol.42 , Issue.6 , pp. 957-962
    • Bouras, A.1    Boggetto, N.2    Benatalah, Z.3    de, R.E.4    Sicsic, S.5    Reboud-Ravaux, M.6
  • 149
    • 9744250914 scopus 로고    scopus 로고
    • New constrainedmolecular tongs designed to dissociate HIV-1 protease dimer
    • Merabet N, Dumond J, Collinet B, et al. New constrainedmolecular tongs designed to dissociate HIV-1 protease dimer. J. Med Chem 2004; 47 (25): 6392-400.
    • (2004) J. Med Chem. , vol.47 , Issue.25 , pp. 6392-6400
    • Merabet, N.1    Dumond, J.2    Collinet, B.3
  • 150
    • 0035903892 scopus 로고    scopus 로고
    • Design and synthesis of new inhibitors of HIV-1 protease dimerization with conformationally constrained templates
    • Song M, Rajesh S, Hayashi Y, Kiso Y. Design and synthesis of new inhibitors of HIV-1 protease dimerization with conformationally constrained templates. Bioorg. Med Chem Lett 2001; 11 (18): 2465-8.
    • (2001) Bioorg. Med Chem Lett. , vol.11 , Issue.18 , pp. 2465-2468
    • Song, M.1    Rajesh, S.2    Hayashi, Y.3    Kiso, Y.4
  • 151
    • 33746701342 scopus 로고    scopus 로고
    • Molecular tongs containing amino acid mimetic fragments: New inhibitors of wild-type and mutated HIV-1 protease dimerization
    • Bannwarth L, Kessler A, Pethe S, et al. Molecular tongs containing amino acid mimetic fragments: new inhibitors of wild-type and mutated HIV-1 protease dimerization. J. Med Chem 2006; 49 (15): 4657-64.
    • (2006) J. Med Chem. , vol.49 , Issue.15 , pp. 4657-4664
    • Bannwarth, L.1    Kessler, A.2    Pethe, S.3
  • 152
    • 78349245937 scopus 로고    scopus 로고
    • Toward the first nonpeptidic molecular tong inhibitor of wild-type and mutated HIV-1 protease dimerization
    • Vidu A, Dufau L, Bannwarth L, et al. Toward the first nonpeptidic molecular tong inhibitor of wild-type and mutated HIV-1 protease dimerization. ChemMedChem 2010; 5 (11): 1899-906.
    • (2010) ChemMedChem , vol.5 , Issue.11 , pp. 1899-1906
    • Vidu, A.1    Dufau, L.2    Bannwarth, L.3


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