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Volumn 5, Issue 1, 2013, Pages 127-149

Approaches for identification of HIV-1 entry inhibitors targeting gp41 pocket

Author keywords

gp41; HIV fusion entry inhibitors; HIV 1; Hydrophobic pocket; Small molecule compounds

Indexed keywords

2 CHLORO 5 (1 PYRROLYL)BENZOIC ACID; 4 [(4 BROMOPHENYL)(ETHOXYIMINO)METHYL] 1' [(2,4 DIMETHYL 3 PYRIDINYL)CARBONYL] 4' METHYL 1,4' BIPIPERIDINE; 5 [(4 CHLORO 6 PHENYLAMIN 1,3,5 TRIAZIN 2 YL)AMINO] 4 HYDROXYL 3 [(4 METHOXY 6 SULFOPHENYL)AZO] 2,7 NAPHTHALENE DISULFONIC ACID; 7 [6 PHENYLAMINO 4 [4 [(3,5 DISULFO 6 HYDROXYNAPHTHYL)AZO] 2 METHOXY 5 METHYLPHENYLAMINO] 1,3,5 TRIAZIN 2 YL] 4 HYDROXYL 3 [(2 METHOXY 5 SULFOPHENYL)AZO] 2 NAPHTHALENE SULFONIC ACID; A 12; ADS J 1; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIRETROVIRUS AGENT; C PEPTIDE; CD4 IMMUNOGLOBULIN G2; ENFUVIRTIDE; GLS 22; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; NB 2; NB 206; PLERIXAFOR; SB C 01; SB D 10; SIFUVIRTIDE; T 1144; T 149; T 2635; TIFUVIRTIDE; TLT 35; UNCLASSIFIED DRUG;

EID: 84872844514     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v5010127     Document Type: Review
Times cited : (52)

References (95)
  • 1
    • 41849127131 scopus 로고    scopus 로고
    • The spread, treatment, and prevention of HIV-1: Evolution of a global pandemic
    • Cohen, M.S.; Hellmann, N.; Levy, J.A.; DeCock, K.; Lange, J. The spread, treatment, and prevention of HIV-1: Evolution of a global pandemic. J. Clin. Invest. 2008, 118, 1244-1254.
    • (2008) J. Clin. Invest , vol.118 , pp. 1244-1254
    • Cohen, M.S.1    Hellmann, N.2    Levy, J.A.3    Decock, K.4    Lange, J.5
  • 3
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang, S.; Zhao, Q.; Debnath, A.K. Peptide and non-peptide HIV fusion inhibitors. Curr. Pharm. Des. 2002, 8, 563-580.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 5
  • 6
    • 0031298109 scopus 로고    scopus 로고
    • HIV entry and tropism: The chemokine receptor connection
    • Berger, E.A. HIV entry and tropism: the chemokine receptor connection. AIDS 1997, 11 Suppl. A, S3-S16.
    • (1997) AIDS , vol.11 , Issue.SUPPL. A
    • Berger, E.A.1
  • 7
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D.C.; Kim, P.S. HIV entry and its inhibition. Cell 1998, 93, 681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 8
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D.C.; Chutkowski, C.T.; Kim, P.S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA 1998, 95, 15613-15617.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 9
    • 0032850583 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infectivity by the gp41 core: Role of a conserved hydrophobic cavity in membrane fusion
    • Ji, H.; Shu, W.; Burling, T.; Jiang, S.; Lu, M. Inhibition of HIV-1 infectivity by the gp41 core: Role of a conserved hydrophobic cavity in membrane fusion. J. Virol. 1999, 73, 8578-8586.
    • (1999) J. Virol , vol.73 , pp. 8578-8586
    • Ji, H.1    Shu, W.2    Burling, T.3    Jiang, S.4    Lu, M.5
  • 10
    • 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
  • 11
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • Lu, M.; Kim, P.S. A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. 1997, 15, 465-471.
    • (1997) J. Biomol. Struct. Dyn , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 12
    • 0346729750 scopus 로고    scopus 로고
    • Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: Applicable for identification of HIV-1 fusion inhibitors
    • Liu, S.; Zhao, Q.; Jiang, S. Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: applicable for identification of HIV-1 fusion inhibitors. Peptides 2003, 24, 1303-1313.
    • (2003) Peptides , vol.24 , pp. 1303-1313
    • Liu, S.1    Zhao, Q.2    Jiang, S.3
  • 13
    • 15744393651 scopus 로고    scopus 로고
    • Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120
    • Liu, S.; Lu, H.; Niu, J.; Xu, Y.; Wu, S.; Jiang, S. Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120. J. Biol. Chem. 2005, 280, 11259-11273.
    • (2005) J. Biol. Chem , vol.280 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 14
    • 7244253012 scopus 로고    scopus 로고
    • N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion
    • Jiang, S.; Lu, H.; Liu, S.; Zhao, Q.; He, Y.; Debnath, A.K. N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion. Antimicrob. Agents Chemother. 2004, 48, 4349-4359.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 4349-4359
    • Jiang, S.1    Lu, H.2    Liu, S.3    Zhao, Q.4    He, Y.5    Debnath, A.K.6
  • 15
    • 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.; Mao, Q.; Lu, H.; An, X.; Xia, C.; Li, X; Debnath, A.K.; Wu, S., 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, 4987-4998.
    • (2009) Antimicrob. Agents Chemother , vol.53 , pp. 4987-4998
    • Wang, H.1    Qi, Z.2    Guo, A.3    Mao, Q.4    Lu, H.5    An, X.6    Xia, C.7    Li, X.8    Debnath, A.K.9    Wu, S.10
  • 17
    • 0027203897 scopus 로고
    • Inhibition of HIV-1 infection by a fusion domain binding peptide from HIV-1 envelope glycoprotein gp41
    • Jiang, S.; Lin, K.; Strick, N.; Neurath, A.R. Inhibition of HIV-1 infection by a fusion domain binding peptide from HIV-1 envelope glycoprotein gp41. Biochem. Biophys. Res. Commun. 1993, 195, 533-538.
    • (1993) Biochem. Biophys. Res. Commun , vol.195 , pp. 533-538
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 18
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C.; Dubay, J.W.; Greenwell, T.; Baird, T., Jr.; Oas, T.G.; McDanal, C.; Hunter, E.; Matthews, T. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA 1994, 91, 12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 22
    • 1142310723 scopus 로고    scopus 로고
    • Enfuvirtide, a new fusion inhibitor for therapy of human immunodeficiency virus infection
    • Hardy, H.; Skolnik, P.R. Enfuvirtide, a new fusion inhibitor for therapy of human immunodeficiency virus infection. Pharmacotherapy 2004, 24, 198-211.
    • (2004) Pharmacotherapy , vol.24 , pp. 198-211
    • Hardy, H.1    Skolnik, P.R.2
  • 24
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L.T.; Shugars, D.C.; Matthews, T.J. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 1998, 72, 986-993.
    • (1998) J. Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 25
    • 27944455637 scopus 로고    scopus 로고
    • Enfuvirtide, the first fusion inhibitor to treat HIV infection
    • Poveda, E.; Briz, V.; Soriano, V. Enfuvirtide, the first fusion inhibitor to treat HIV infection. AIDS Rev. 2005, 7, 139-147.
    • (2005) AIDS Rev , vol.7 , pp. 139-147
    • Poveda, E.1    Briz, V.2    Soriano, V.3
  • 27
    • 2342550183 scopus 로고    scopus 로고
    • Discontinuation of the clinical development of fusion inhibitor T-1249
    • Martin-Carbonero, L. Discontinuation of the clinical development of fusion inhibitor T-1249. AIDS Rev. 2004, 6, 61.
    • (2004) AIDS Rev , vol.6 , pp. 61
    • Martin-Carbonero, L.1
  • 29
    • 4444310448 scopus 로고    scopus 로고
    • Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates
    • Sista, P.R.; Melby, T.; Davison, D.; Jin, L.; Mosier, S.; Mink, M.; Nelson, E.L.; Demasi, R.; Cammack, N.; Salgo, M.P., et al. Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates. AIDS 2004, 18, 1787-1794.
    • (2004) AIDS , vol.18 , pp. 1787-1794
    • Sista, P.R.1    Melby, T.2    Davison, D.3    Jin, L.4    Mosier, S.5    Mink, M.6    Nelson, E.L.7    Demasi, R.8    Cammack, N.9    Salgo, M.P.10
  • 31
    • 45749112585 scopus 로고    scopus 로고
    • Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: Implications for designing novel anti-HIV fusion inhibitors
    • He, Y.; Cheng, J.; Li, J.; Qi, Z.; Lu, H.; Dong, M.; Jiang, S.; Dai, Q. Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors. J. Virol. 2008, 82, 6349-6358.
    • (2008) J. Virol , vol.82 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3    Qi, Z.4    Lu, H.5    Dong, M.6    Jiang, S.7    Dai, Q.8
  • 33
    • 84862927851 scopus 로고    scopus 로고
    • Mutations of Gln64 in the HIV-1 gp41 N-terminal heptad repeat render viruses resistant to peptide HIV fusion inhibitors targeting the gp41 pocket
    • Yu, X.; Lu, L.; Cai, L.; Tong, P.; Tan, S.; Zou, P.; Meng, F.; Chen, Y.H.; Jiang, S. Mutations of Gln64 in the HIV-1 gp41 N-terminal heptad repeat render viruses resistant to peptide HIV fusion inhibitors targeting the gp41 pocket. J. Virol. 2012, 86, 589-593.
    • (2012) J. Virol , vol.86 , pp. 589-593
    • Yu, X.1    Lu, L.2    Cai, L.3    Tong, P.4    Tan, S.5    Zou, P.6    Meng, F.7    Chen, Y.H.8    Jiang, S.9
  • 37
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C.; Oas, T.; McDanal, C.; Bolognesi, D.; Matthews, T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 1992, 89, 10537-10541.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 38
    • 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, 143-162.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 143-162
    • Liu, S.1    Wu, S.2    Jiang, S.3
  • 39
    • 78349299437 scopus 로고    scopus 로고
    • Development of peptide and small-molecule HIV-1 fusion inhibitors that target gp41
    • Cai, L.; Jiang, S. Development of peptide and small-molecule HIV-1 fusion inhibitors that target gp41. ChemMedChem. 2010, 5, 1813-1824.
    • (2010) ChemMedChem , vol.5 , pp. 1813-1824
    • Cai, L.1    Jiang, S.2
  • 40
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M.J.; Kay, M.S.; Kim, P.S. Protein design of an HIV-1 entry inhibitor. Science 2001, 291, 884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 41
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley, C.A.; Louis, J.M.; Ghirlando, R.; Clore, G.M. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 2002, 277, 14238-14245.
    • (2002) J. Biol. Chem , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 42
    • 33748276474 scopus 로고    scopus 로고
    • Protein-ligand docking: Current status and future challenges
    • Sousa, S.F.; Fernandes, P.A.; Ramos, M.J. Protein-ligand docking: current status and future challenges. Proteins 2006, 65, 15-26.
    • (2006) Proteins , vol.65 , pp. 15-26
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 44
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G.; Willett, P.; Glen, R.C. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 1995, 245, 43-53.
    • (1995) J. Mol. Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 45
    • 6244283606 scopus 로고    scopus 로고
    • Critical evaluation of search algorithms for automated molecular docking and database screening
    • Ewing, T.J.A.; Kuntz, I.D. Critical evaluation of search algorithms for automated molecular docking and database screening. J. Comput. Chem. 1997, 18, 1175-1189.
    • (1997) J. Comput. Chem , vol.18 , pp. 1175-1189
    • Ewing, T.J.A.1    Kuntz, I.D.2
  • 46
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • Ewing, T.J.; Makino, S.; Skillman, A.G.; Kuntz, I.D. DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases. J. Comput. Aided Mol. Des. 2001, 15, 411-428.
    • (2001) J. Comput. Aided Mol. Des , vol.15 , pp. 411-428
    • Ewing, T.J.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 47
    • 2442511737 scopus 로고    scopus 로고
    • High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques
    • Liu, S.; Jiang, S. High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques. Curr. Pharm. Des. 2004, 10, 1827-1843.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 1827-1843
    • Liu, S.1    Jiang, S.2
  • 48
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D.C.; Fass, D.; Berger, J.M.; Kim, P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89, 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 50
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K.; Liu, J.; Wang, J.; Shen, S.; Liu, M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 1997, 94, 12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Liu, M.5
  • 51
    • 0033607028 scopus 로고    scopus 로고
    • Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodecifiency virus type 1
    • Debnath, A.K.; Radigan, L.; Jiang, S. Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodecifiency virus type 1. J. Med. Chem. 1999, 42, 3203-3209.
    • (1999) J. Med. Chem , vol.42 , pp. 3203-3209
    • Debnath, A.K.1    Radigan, L.2    Jiang, S.3
  • 52
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang, S.; Lin, K.; Zhang, L.; Debnath, A.K. A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 1999, 80, 85-96.
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 53
    • 2442511737 scopus 로고    scopus 로고
    • High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques
    • Liu, S.; Jiang, S. High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques. Curr. Pharm. Des. 2004, 10, 1827-1843.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 1827-1843
    • Liu, S.1    Jiang, S.2
  • 54
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D.M.; Malashkevich, V.N.; Hong, L.H.; Carr, P.A.; Kim, P.S. Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 1999, 99, 103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 57
    • 84859437944 scopus 로고    scopus 로고
    • Footprint-based identification of viral entry inhibitors targeting HIVgp41
    • Holden, P.M.; Kaur, H.; Goyal, R.; Gochin, M.; Rizzo, R.C. Footprint-based identification of viral entry inhibitors targeting HIVgp41. Bioorg. Med. Chem. Lett. 2012, 22, 3011-3016.
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 3011-3016
    • Holden, P.M.1    Kaur, H.2    Goyal, R.3    Gochin, M.4    Rizzo, R.C.5
  • 58
    • 13844312649 scopus 로고    scopus 로고
    • ZINC-a free database of commercially available compounds for virtual screening
    • 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.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 61
    • 72249122328 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors
    • Katritzky, A.R.; Tala, S.R.; Lu, H.; Vakulenko, A.V.; Chen, Q.Y.; Sivapackiam, J.; Pandya, K.; Jiang, S; Debnath, A.K. Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors. J. Med. Chem. 2009, 52, 7631-7639.
    • (2009) J. Med. Chem , vol.52 , pp. 7631-7639
    • Katritzky, A.R.1    Tala, S.R.2    Lu, H.3    Vakulenko, A.V.4    Chen, Q.Y.5    Sivapackiam, J.6    Pandya, K.7    Jiang, S.8    Debnath, A.K.9
  • 62
    • 80054910151 scopus 로고    scopus 로고
    • Development of indole compounds as small molecule fusion inhibitors targeting HIV-1 glycoprotein-41
    • Zhou, G.; Wu, D.; Snyder, B.; Ptak, R.G.; Kaur, H.; Gochin, M. Development of indole compounds as small molecule fusion inhibitors targeting HIV-1 glycoprotein-41. J. Med. Chem. 2011, 54, 7220-7231.
    • (2011) J. Med. Chem , vol.54 , pp. 7220-7231
    • Zhou, G.1    Wu, D.2    Snyder, B.3    Ptak, R.G.4    Kaur, H.5    Gochin, M.6
  • 63
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang, S.; Lin, K.; Zhang, L.; Debnath, A.K. A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 1999, 80, 85-96.
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 64
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang, S.; Lin, K.; Lu, M. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 1998, 72, 10213-10217.
    • (1998) J. Virol , vol.72 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 65
    • 0347689876 scopus 로고    scopus 로고
    • Rapid and automated fluorescence-linked immunosorbent assay for high-throughput screening of HIV-1 fusion inhibitors targeting gp41
    • Liu, S.; Boyer-Chatenet, L.; Lu, H.; Jiang, S. Rapid and automated fluorescence-linked immunosorbent assay for high-throughput screening of HIV-1 fusion inhibitors targeting gp41. J. Biomol. Screen. 2003, 8, 685-693.
    • (2003) J. Biomol. Screen , vol.8 , pp. 685-693
    • Liu, S.1    Boyer-Chatenet, L.2    Lu, H.3    Jiang, S.4
  • 66
    • 58149090406 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of N-carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41
    • Liu, K.; Lu, H.; Hou, L.; Qi, Z.; Teixeira, C.; Barbault, F.; Fan, B.T.; Liu, S.; Jiang, S.; Xie, L. Design, synthesis, and biological evaluation of N-carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41. J. Med. Chem. 2008, 51, 7843-7854.
    • (2008) J. Med. Chem , vol.51 , pp. 7843-7854
    • Liu, K.1    Lu, H.2    Hou, L.3    Qi, Z.4    Teixeira, C.5    Barbault, F.6    Fan, B.T.7    Liu, S.8    Jiang, S.9    Xie, L.10
  • 67
    • 72049084473 scopus 로고    scopus 로고
    • Structure-based design, synthesis and biological evaluation of new N-carboxyphenylpyrrole derivatives as HIV fusion inhibitors targeting gp41
    • Wang, Y.; Lu, H.; Zhu, Q.; Jiang, S.; Liao, Y. Structure-based design, synthesis and biological evaluation of new N-carboxyphenylpyrrole derivatives as HIV fusion inhibitors targeting gp41. Bioorg. Med. Chem. Lett. 2010, 20, 189-192.
    • (2010) Bioorg. Med. Chem. Lett , vol.20 , pp. 189-192
    • Wang, Y.1    Lu, H.2    Zhu, Q.3    Jiang, S.4    Liao, Y.5
  • 68
    • 72249122328 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship of a novel series of 2-Aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidin-ylidenemethyl)furans as HIV-1 entry inhibitors
    • Katritzky, A.R.; Tala, S.R.; Lu, H.; Vakulenko, A.V.; Chen, Q.Y.; Sivapackiam, J.; Pandya, K.; Jiang, S.; Debnath, A.K. Design, synthesis, and structure-activity relationship of a novel series of 2-Aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidin-ylidenemethyl)furans as HIV-1 entry inhibitors. J. Med. Chem. 2009, 52, 7631-7639.
    • (2009) J. Med. Chem , vol.52 , pp. 7631-7639
    • Katritzky, A.R.1    Tala, S.R.2    Lu, H.3    Vakulenko, A.V.4    Chen, Q.Y.5    Sivapackiam, J.6    Pandya, K.7    Jiang, S.8    Debnath, A.K.9
  • 70
    • 78751657690 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of novel 5-((arylfuran/1H-pyrrol-2-yl)methylene)-2-thioxo-3-(3-(trifluoromethyl)phenyl)thi azolidin-4-ones as HIV-1 fusion inhibitors targeting gp41
    • Jiang, S.; Tala, S.R.; Lu, H.; bo-Dya, N.E.; Avan, I.; Gyanda, K.; Lu, L.; Katritzky, A.R.; Debnath, A.K. Design, synthesis, and biological activity of novel 5-((arylfuran/1H-pyrrol-2-yl)methylene)-2-thioxo-3-(3-(trifluoromethyl)phenyl)thi azolidin-4-ones as HIV-1 fusion inhibitors targeting gp41. J. Med. Chem. 2011, 54, 572-579.
    • (2011) J. Med. Chem , vol.54 , pp. 572-579
    • Jiang, S.1    Tala, S.R.2    Lu, H.3    Bo-Dya, N.E.4    Avan, I.5    Gyanda, K.6    Lu, L.7    Katritzky, A.R.8    Debnath, A.K.9
  • 72
    • 0344444157 scopus 로고    scopus 로고
    • A metallopeptide assembly of the HIV-1 gp41 coiled coil is an ideal receptor in fluorescence detection of ligand binding
    • Gochin, M.; Kiplin, G.R.; Case, M.A. A metallopeptide assembly of the HIV-1 gp41 coiled coil is an ideal receptor in fluorescence detection of ligand binding. Angew. Chem. Int. Ed. Engl. 2003, 42, 5325-5328.
    • (2003) Angew. Chem. Int. Ed. Engl , vol.42 , pp. 5325-5328
    • Gochin, M.1    Kiplin, G.R.2    Case, M.A.3
  • 73
    • 34447260888 scopus 로고    scopus 로고
    • A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1
    • Cai, L.; Gochin, M. A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 2007, 51, 2388-2395.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 2388-2395
    • Cai, L.1    Gochin, M.2
  • 74
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M.J.; Kay, M.S.; Kim, P.S. Protein design of an HIV-1 entry inhibitor. Science 2001, 291, 884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 75
    • 0030987357 scopus 로고    scopus 로고
    • Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli
    • Weissenhorn, W.; Calder, L.J.; Dessen, A.; Laue, T.; Skehel, J.J.; Wiley, D.C. Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli. Proc. Natl. Acad. Sci. USA 1997, 94, 6065-6069.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6065-6069
    • Weissenhorn, W.1    Calder, L.J.2    Dessen, A.3    Laue, T.4    Skehel, J.J.5    Wiley, D.C.6
  • 76
    • 77955275844 scopus 로고    scopus 로고
    • Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides
    • Chen, X.; Lu, L.; Qi, Z.; Lu, H.; Wang, J.; Yu, X.; Chen, Y.; Jiang, S. Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides. J. Biol. Chem. 2010, 285, 25506-25515.
    • (2010) J. Biol. Chem , vol.285 , pp. 25506-25515
    • Chen, X.1    Lu, L.2    Qi, Z.3    Lu, H.4    Wang, J.5    Yu, X.6    Chen, Y.7    Jiang, S.8
  • 77
    • 0037490139 scopus 로고    scopus 로고
    • Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion
    • Louis, J.M.; Nesheiwat, I.; Chang, L.; Clore, G.M.; Bewley, C.A. Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion. J. Biol. Chem. 2003, 278, 20278-20285.
    • (2003) J. Biol. Chem , vol.278 , pp. 20278-20285
    • Louis, J.M.1    Nesheiwat, I.2    Chang, L.3    Clore, G.M.4    Bewley, C.A.5
  • 78
    • 0037130657 scopus 로고    scopus 로고
    • Structural characterization of a paramagnetic metal-ion-assembled three-stranded alpha-helical coiled coil
    • Gochin, M.; Khorosheva, V.; Case, M.A. Structural characterization of a paramagnetic metal-ion-assembled three-stranded alpha-helical coiled coil. J. Am. Chem. Soc. 2002, 124, 11018-11028.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 11018-11028
    • Gochin, M.1    Khorosheva, V.2    Case, M.A.3
  • 79
    • 33645760751 scopus 로고    scopus 로고
    • A fluorescence assay for rapid detection of ligand binding affinity to HIV-1 gp41
    • Gochin, M.; Savage, R.; Hinckley, S.; Cai, L. A fluorescence assay for rapid detection of ligand binding affinity to HIV-1 gp41. Biol. Chem. 2006, 387, 477-483.
    • (2006) Biol. Chem , vol.387 , pp. 477-483
    • Gochin, M.1    Savage, R.2    Hinckley, S.3    Cai, L.4
  • 80
    • 76649145391 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of indole compounds as novel inhibitors targeting Gp41
    • Zhou, G.; Wu, D.; Hermel, E.; Balogh, E.; Gochin, M. Design, synthesis, and evaluation of indole compounds as novel inhibitors targeting Gp41. Bioorg. Med. Chem. Lett. 2010, 20, 1500-1503.
    • (2010) Bioorg. Med. Chem. Lett , vol.20 , pp. 1500-1503
    • Zhou, G.1    Wu, D.2    Hermel, E.3    Balogh, E.4    Gochin, M.5
  • 81
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • Root, M.J.; Steger, H.K. HIV-1 gp41 as a target for viral entry inhibition. Curr. Pharm. Des. 2004, 10, 1805-1825.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 1805-1825
    • Root, M.J.1    Steger, H.K.2
  • 83
    • 0037126834 scopus 로고    scopus 로고
    • Design of a protein surface antagonist based on alpha-helix mimicry: Inhibition of gp41 assembly and viral fusion
    • Ernst, J.T.; Kutzki, O.; Debnath, A.K.; Jiang, S.; Lu, H.; Hamilton, A.D. Design of a protein surface antagonist based on alpha-helix mimicry: inhibition of gp41 assembly and viral fusion. Angew. Chem. Int. Ed. Engl. 2002, 41, 278-281.
    • (2002) Angew. Chem. Int. Ed. Engl , vol.41 , pp. 278-281
    • Ernst, J.T.1    Kutzki, O.2    Debnath, A.K.3    Jiang, S.4    Lu, H.5    Hamilton, A.D.6
  • 84
    • 0034801374 scopus 로고    scopus 로고
    • Toward proteomimetics: Terphenyl derivatives as structural and functional mimics of extended regions of an alpha-helix
    • Orner, B.P.; Ernst, J.T.; Hamilton, A.D. Toward proteomimetics: terphenyl derivatives as structural and functional mimics of extended regions of an alpha-helix. J. Am. Chem. Soc. 2001, 123, 5382-5383.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 5382-5383
    • Orner, B.P.1    Ernst, J.T.2    Hamilton, A.D.3
  • 85
    • 84859442418 scopus 로고    scopus 로고
    • Discovery of HIV fusion inhibitors targeting gp41 using a comprehensive alpha-helix mimetic library
    • Whitby, L.R.; Boyle, K.E.; Cai, L.; Yu, X.; Gochin, M.; Boger, D.L. Discovery of HIV fusion inhibitors targeting gp41 using a comprehensive alpha-helix mimetic library. Bioorg. Med. Chem. Lett. 2012, 22, 2861-2865.
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 2861-2865
    • Whitby, L.R.1    Boyle, K.E.2    Cai, L.3    Yu, X.4    Gochin, M.5    Boger, D.L.6
  • 88
    • 10144244674 scopus 로고    scopus 로고
    • A trial comparing nucleoside monotherapy with combination therapy in HIV-infected adults with CD4 cell counts from 200 to 500 per cubic millimeter
    • AIDS Clinical Trials Group Study 175 Study Team
    • Hammer, S.M.; Katzenstein, D.A.; Hughes, M.D.; Gundacker, H.; Schooley, R.T.; Haubrich, R.H.; Henry, W.K.; Lederman, M.M.; Phair, J.P.; Niu, M., et al. A trial comparing nucleoside monotherapy with combination therapy in HIV-infected adults with CD4 cell counts from 200 to 500 per cubic millimeter. AIDS Clinical Trials Group Study 175 Study Team. N. Engl. J. Med. 1996, 335, 1081-1090.
    • (1996) N. Engl. J. Med , vol.335 , pp. 1081-1090
    • Hammer, S.M.1    Katzenstein, D.A.2    Hughes, M.D.3    Gundacker, H.4    Schooley, R.T.5    Haubrich, R.H.6    Henry, W.K.7    Lederman, M.M.8    Phair, J.P.9    Niu, M.10
  • 89
    • 0035313589 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion
    • Nagashima, K.A.; Thompson, D.A.; Rosenfield, S.I.; Maddon, P.J.; Dragic, T.; Olson, W.C. Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion. J. Infect. Dis. 2001, 183, 1121-1125.
    • (2001) J. Infect. Dis , vol.183 , pp. 1121-1125
    • Nagashima, K.A.1    Thompson, D.A.2    Rosenfield, S.I.3    Maddon, P.J.4    Dragic, T.5    Olson, W.C.6
  • 91
    • 0036232981 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro
    • Tremblay, C.L.; Giguel, F.; Kollmann, C.; Guan, Y.; Chou, T.C.; Baroudy, B.M.; Hirsch, M.S. Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro. Antimicrob. Agents Chemother. 2002, 46, 1336-1339.
    • (2002) Antimicrob. Agents Chemother , vol.46 , pp. 1336-1339
    • Tremblay, C.L.1    Giguel, F.2    Kollmann, C.3    Guan, Y.4    Chou, T.C.5    Baroudy, B.M.6    Hirsch, M.S.7
  • 92
    • 63149114263 scopus 로고    scopus 로고
    • Synergistic efficacy of combination of enfuvirtide and sifuvirtide, the first- and next-generation HIV-fusion inhibitors
    • Pan, C.; Lu, H.; Qi, Z.; Jiang, S. Synergistic efficacy of combination of enfuvirtide and sifuvirtide, the first- and next-generation HIV-fusion inhibitors. AIDS 2009, 23, 639-641.
    • (2009) AIDS , vol.23 , pp. 639-641
    • Pan, C.1    Lu, H.2    Qi, Z.3    Jiang, S.4
  • 93
    • 67749147470 scopus 로고    scopus 로고
    • Combinations of the first and next generations of human immunodeficiency virus (HIV) fusion inhibitors exhibit a highly potent synergistic effect against enfuvirtide- sensitive and -resistant HIV type 1 strains
    • Pan, C.; Cai, L.; Lu, H.; Qi, Z.; Jiang, S. Combinations of the first and next generations of human immunodeficiency virus (HIV) fusion inhibitors exhibit a highly potent synergistic effect against enfuvirtide- sensitive and -resistant HIV type 1 strains. J. Virol. 2009, 83, 7862-7872.
    • (2009) J. Virol , vol.83 , pp. 7862-7872
    • Pan, C.1    Cai, L.2    Lu, H.3    Qi, Z.4    Jiang, S.5
  • 94
    • 80051516345 scopus 로고    scopus 로고
    • A novel chimeric protein-based HIV-1 fusion inhibitor targeting gp41 glycoprotein with high potency and stability
    • Pan, C.; Cai, L.; Lu, H.; Lu, L.; Jiang, S. A novel chimeric protein-based HIV-1 fusion inhibitor targeting gp41 glycoprotein with high potency and stability. J. Biol. Chem. 2011, 286, 28425-28434.
    • (2011) J. Biol. Chem , vol.286 , pp. 28425-28434
    • Pan, C.1    Cai, L.2    Lu, H.3    Lu, L.4    Jiang, S.5
  • 95
    • 84863249782 scopus 로고    scopus 로고
    • Interactions between different generation HIV-1 fusion inhibitors and the putative mechanism underlying the synergistic anti-HIV-1 effect resulting from their combination
    • Cai, L.; Pan, C.; Xu, L.; Shui, Y.; Liu, K.; Jiang, S. Interactions between different generation HIV-1 fusion inhibitors and the putative mechanism underlying the synergistic anti-HIV-1 effect resulting from their combination. FASEB J. 2012, 26, 1018-1026.
    • (2012) FASEB J , vol.26 , pp. 1018-1026
    • Cai, L.1    Pan, C.2    Xu, L.3    Shui, Y.4    Liu, K.5    Jiang, S.6


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