메뉴 건너뛰기




Volumn 11, Issue 24, 2011, Pages 3022-3032

Amphipathic properties of HIV-1 gp41 fusion inhibitors

Author keywords

Amphiphilic; gp41; HIV 1; Hydrophobic pocket; Inhibition; Small molecules

Indexed keywords

4 (8 BETULINOYLAMINOOCTANOYLAMINO) 3 HYDROXY 6 METHYLHEPTANOIC ACID; ADSJ 1; AMPHOPHILE; ANTIRETROVIRUS AGENT; CATECHOL; CYCLOPEPTIDE; DETERGENT; DYE; EPIGALLOCATECHIN GALLATE; FLAVONOID; FORMAZAN; GALLOCATECHIN GALLATE; GLYCOPROTEIN GP 41; GLYCOPROTEIN GP 41 FUSION INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; HYBRID PROTEIN; HYDROXYTYROSOL; NATURAL PRODUCT; NB 179; NB 180; NB 214; NB 225; NB 228; NB 235; OLEUROPEIN; OLIGODEOXYNUCLEOTIDE PHOSPHOROTHIOATE; PALMITIC ACID; PEPTIDE DERIVATIVE; PEPTIDOMIMETIC AGENT; PF 68742; PLANT EXTRACT; POLYANION; POLYPHENOL DERIVATIVE; TANNIN; TIFUVIRTIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG; XTT FORMAZAN;

EID: 80054909887     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/156802611798808488     Document Type: Review
Times cited : (15)

References (113)
  • 1
    • 77949394453 scopus 로고    scopus 로고
    • Epidemiology of HIV. Update
    • Dorrucci, M. [Epidemiology of HIV. Update]. Recenti Prog. Med., 2010, 101 (1), 12-15.
    • (2010) Recenti Prog. Med , vol.101 , Issue.1 , pp. 12-15
    • Dorrucci, M.1
  • 2
    • 77950199930 scopus 로고    scopus 로고
    • Peptide-based inhibitors of the HIV envelope protein and other class I viral fusion proteins
    • Steffen, I.; Pohlmann, S. Peptide-based inhibitors of the HIV envelope protein and other class I viral fusion proteins. Curr. Pharm. Des., 2010, 16 (9), 1143-1158.
    • (2010) Curr. Pharm. Des , vol.16 , Issue.9 , pp. 1143-1158
    • Steffen, I.1    Pohlmann, S.2
  • 4
    • 44349094889 scopus 로고    scopus 로고
    • Efficient HIV-1 transmission from macrophages to T cells across transient virological synapses
    • Groot, F.; Welsch, S.; Sattentau, Q. J. Efficient HIV-1 transmission from macrophages to T cells across transient virological synapses. Blood, 2008, 111(9), 4660-4663.
    • (2008) Blood , vol.111 , Issue.9 , pp. 4660-4663
    • Groot, F.1    Welsch, S.2    Sattentau, Q.J.3
  • 5
    • 0036435762 scopus 로고    scopus 로고
    • The Mechanism of Inhibition of HIV-1 Env-Mediated Cell-Cell Fusion by Recombinant Cores of gp41 Ectodomain
    • Markosyan, R. M.; Xiuwen, M.; Lu, M.; Cohen, F. S.; Melikyan, G. B. The Mechanism of Inhibition of HIV-1 Env-Mediated Cell-Cell Fusion by Recombinant Cores of gp41 Ectodomain. Virology, 2002, 302, 174-184.
    • (2002) Virology , vol.302 , pp. 174-184
    • Markosyan, R.M.1    Xiuwen, M.2    Lu, M.3    Cohen, F.S.4    Melikyan, G.B.5
  • 6
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of Viral Membrane Fusion and Its Inhibition
    • Eckert, D. M.; Kim, P. S. Mechanisms of Viral Membrane Fusion and Its Inhibition. Annual. Rev. Biochem., 2001, 70, 777-810.
    • (2001) Annual. Rev. Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 7
    • 69249116120 scopus 로고    scopus 로고
    • Peptides in the treatment of AIDS
    • Naider, F.; Anglister, J. Peptides in the treatment of AIDS. Curr. Opin. Struct. Biol., 2009, 19 (4), 473-482.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , Issue.4 , pp. 473-482
    • Naider, F.1    Anglister, J.2
  • 8
    • 56749185286 scopus 로고    scopus 로고
    • Characterization of the steric defense of the HIV-1 gp41 N-trimer region
    • Eckert, D. M.; Shi, Y.; Kim, S.; Welch, B. D.; Kang, E.; Poff, E. S.; Kay, M. S. Characterization of the steric defense of the HIV-1 gp41 N-trimer region. Protein Sci. 2008, 17 (12), 2091-2100.
    • (2008) Protein Sci , vol.17 , Issue.12 , pp. 2091-2100
    • Eckert, D.M.1    Shi, Y.2    Kim, S.3    Welch, B.D.4    Kang, E.5    Poff, E.S.6    Kay, M.S.7
  • 9
    • 63649151400 scopus 로고    scopus 로고
    • Interactions of HIV-1 inhibitory peptide T20 with the GP41 N-HR coiled coil
    • Champagne, K.; Shishido, A.; Root, M. J. Interactions of HIV-1 inhibitory peptide T20 with the GP41 N-HR coiled coil. J. Biol. Chem., 2008, 284(6),3619-3627
    • (2008) J. Biol. Chem , vol.284 , Issue.6 , pp. 3619-3627
    • Champagne, K.1    Shishido, A.2    Root, M.J.3
  • 10
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • Steger, H. K.; Root, M. J. Kinetic dependence to HIV-1 entry inhibition. J. Biol. Chem., 2006, 281 (35), 25813-25821.
    • (2006) J. Biol. Chem , vol.281 , Issue.35 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 11
    • 73549091727 scopus 로고    scopus 로고
    • Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding
    • Kahle, K. M.; Steger, H. K.; Root, M. J. Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. PLoS Pathog., 2009, 5 (11), e1000674.
    • (2009) PLoS Pathog , vol.5 , Issue.11
    • Kahle, K.M.1    Steger, H.K.2    Root, M.J.3
  • 12
    • 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 (26), 15613-15617.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.26 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 13
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide fusion inhibitors
    • Jiang, S.; Zhao, Q.; Debnath, A. K. Peptide and non-peptide 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
  • 14
    • 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), 143-162.
    • (2007) Curr. Pharm. Des , vol.13 , Issue.2 , pp. 143-162
    • Liu, S.1    Wu, S.2    Jiang, S.3
  • 15
    • 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 (11), 1813-1824.
    • (2010) ChemMedChem , vol.5 , Issue.11 , pp. 1813-1824
    • Cai, L.1    Jiang, S.2
  • 16
    • 77449151492 scopus 로고    scopus 로고
    • HIV-1 gp41 fusion intermediate: A target for HIV therapeutics
    • Pan, C.; Liu, S.; Jiang, S. HIV-1 gp41 fusion intermediate: a target for HIV therapeutics. J. Formos Med. Assoc., 2010, 109 (2), 94-105.
    • (2010) J. Formos Med. Assoc , vol.109 , Issue.2 , pp. 94-105
    • Pan, C.1    Liu, S.2    Jiang, S.3
  • 18
    • 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 (2), 263-273.
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 19
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo, S. A.; Puri, A.; Blumenthal, R. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry (Mosc) 2001, 40 (41), 12231-12236.
    • (2001) Biochemistry (Mosc) , vol.40 , Issue.41 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 22
    • 0027203897 scopus 로고
    • Inhibition of HIV-1 Infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein gp41
    • Jiang, S.; Lin, K.; Strick, N.; Neurath, A. R. Inhibition of HIV-1 Infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein gp41. Biochem. Biophys. Res. Commun., 1993, 195, 533.
    • (1993) Biochem. Biophys. Res. Commun , vol.195 , pp. 533
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 23
    • 0027179560 scopus 로고
    • HIV-1 inhibition by a peptide
    • Jiang, S.; Lin, K.; Strick, N.; Neurath, A. R. HIV-1 inhibition by a peptide. Nature, 1993, 365 (6442), 113.
    • (1993) Nature , vol.365 , Issue.6442 , pp. 113
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 24
    • 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 (3), 465-471.
    • (1997) J. Biomol. Struct. Dyn , vol.15 , Issue.3 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 25
    • 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., 1992, 89, 10537-10541.
    • (1992) Proc. Natl. Acad. Sci , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 26
    • 0027692502 scopus 로고
    • A synthetic peptide from gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild, C. T.; Greenwell, T.; Matthews, T. A synthetic peptide from gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retrovirus., 1993, 9, 1051-1053.
    • (1993) AIDS Res. Hum. Retrovirus , vol.9 , pp. 1051-1053
    • Wild, C.T.1    Greenwell, T.2    Matthews, T.3
  • 27
    • 0034645796 scopus 로고    scopus 로고
    • Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation
    • Kliger, Y.; Shai, Y. Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation. J. Mol. Biol., 2000, 295 (2), 163-168.
    • (2000) J. Mol. Biol , vol.295 , Issue.2 , pp. 163-168
    • Kliger, Y.1    Shai, Y.2
  • 29
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore, N. R.; Salzwedel, K.; Reddick, M.; Allaway, G. P.; Wild, C. T. Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virology, 2003, 77 (13), 7669-7672.
    • (2003) J. Virology , vol.77 , Issue.13 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 32
    • 67650745033 scopus 로고    scopus 로고
    • The role of amphiphilicity and negative charge in glycoprotein 41 interactions in the hydrophobic pocket
    • Gochin, M.; Cai, L. The role of amphiphilicity and negative charge in glycoprotein 41 interactions in the hydrophobic pocket. J. Med. Chem., 2009, 52 (14), 4338-4344.
    • (2009) J. Med. Chem , vol.52 , Issue.14 , pp. 4338-4344
    • Gochin, M.1    Cai, L.2
  • 33
    • 70349191067 scopus 로고    scopus 로고
    • Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers
    • Horne, W. S.; Johnson, L. M.; Ketas, T. J.; Klasse, P. J.; Lu, M.; Moore, J. P.; Gellman, S. H. Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers. Proc. Natl. Acad. Sci. USA, 2009, 106 (35), 14751-14756.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.35 , pp. 14751-14756
    • Horne, W.S.1    Johnson, L.M.2    Ketas, T.J.3    Klasse, P.J.4    Lu, M.5    Moore, J.P.6    Gellman, S.H.7
  • 35
    • 41549147161 scopus 로고    scopus 로고
    • Inhibition of HIV-1 fusion by hydrogen-bond-surrogate-based alpha helices
    • Wang, D.; Lu, M.; Arora, P. S. Inhibition of HIV-1 fusion by hydrogen-bond-surrogate-based alpha helices. Angew Chem. Int. Ed. Engl., 2008, 47 (10), 1879-1882.
    • (2008) Angew Chem. Int. Ed. Engl , vol.47 , Issue.10 , pp. 1879-1882
    • Wang, D.1    Lu, M.2    Arora, P.S.3
  • 36
    • 45749135859 scopus 로고    scopus 로고
    • Selection of T1249-resistant human immunodeficiency virus type 1 variants
    • Eggink, D.; Baldwin, C. E.; Deng, Y.; Langedijk, J. P.; Lu, M.; Sanders, R. W.; Berkhout, B. Selection of T1249-resistant human immunodeficiency virus type 1 variants. J. Virol., 2008, 82 (13), 6678-6688.
    • (2008) J. Virol , vol.82 , Issue.13 , pp. 6678-6688
    • Eggink, D.1    Baldwin, C.E.2    Deng, Y.3    Langedijk, J.P.4    Lu, M.5    Sanders, R.W.6    Berkhout, B.7
  • 37
    • 70350371719 scopus 로고    scopus 로고
    • Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors
    • Eggink, D.; Langedijk, J. P.; Bonvin, A. M.; Deng, Y.; Lu, M.; Berkhout, B.; Sanders, R. W. Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors. J. Biol. Chem., 2009, 284 (39), 26941-26950.
    • (2009) J. Biol. Chem , vol.284 , Issue.39 , pp. 26941-26950
    • Eggink, D.1    Langedijk, J.P.2    Bonvin, A.M.3    Deng, Y.4    Lu, M.5    Berkhout, B.6    Sanders, R.W.7
  • 38
    • 8844228894 scopus 로고    scopus 로고
    • HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers. Putative correlation with improved efficiency
    • Veiga, A. S.; Santos, N. C.; Loura, L. M.; Fedorov, A.; Castanho, M. A. HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers. Putative correlation with improved efficiency. J. Am. Chem. Soc., 2004, 126 (45), 14758-14763.
    • (2004) J. Am. Chem. Soc , vol.126 , Issue.45 , pp. 14758-14763
    • Veiga, A.S.1    Santos, N.C.2    Loura, L.M.3    Fedorov, A.4    Castanho, M.A.5
  • 39
    • 43249117737 scopus 로고    scopus 로고
    • Sifuvirtide screens rigid membrane surfaces. establishment of a correlation between efficacy and membrane domain selectivity among HIV fusion inhibitor peptides
    • Franquelim, H. G.; Loura, L. M.; Santos, N. C.; Castanho, M. A. Sifuvirtide screens rigid membrane surfaces. establishment of a correlation between efficacy and membrane domain selectivity among HIV fusion inhibitor peptides. J. Am. Chem. Soc., 2008, 130 (19), 6215-6223.
    • (2008) J. Am. Chem. Soc , vol.130 , Issue.19 , pp. 6215-6223
    • Franquelim, H.G.1    Loura, L.M.2    Santos, N.C.3    Castanho, M.A.4
  • 40
    • 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 (12), 11259-11273.
    • (2005) J. Biol. Chem , vol.280 , Issue.12 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 41
    • 0037936885 scopus 로고    scopus 로고
    • C-terminal octylation rescues an inactive T20 mutant: Implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion
    • Peisajovich, S. G.; Gallo, S. A.; Blumenthal, R.; Shai, Y. C-terminal octylation rescues an inactive T20 mutant: implications for the mechanism of HIV/SIMIAN immunodeficiency virus-induced membrane fusion. J. Biol. Chem., 2003, 278 (23), 21012-21017.
    • (2003) J. Biol. Chem , vol.278 , Issue.23 , pp. 21012-21017
    • Peisajovich, S.G.1    Gallo, S.A.2    Blumenthal, R.3    Shai, Y.4
  • 42
    • 35948978102 scopus 로고    scopus 로고
    • Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition
    • Wexler-Cohen, Y.; Shai, Y. Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition. FASEB J., 2007, 21 (13), 3677-3684.
    • (2007) FASEB J , vol.21 , Issue.13 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 43
    • 33845266437 scopus 로고    scopus 로고
    • Structural analysis and assembly of the HIV-1 Gp41 amino-terminal fusion peptide and the pretransmembrane amphipathic-at-interface sequence
    • Lorizate, M.; de la Arada, I.; Huarte, N.; Sanchez-Martinez, S.; de la Torre, B. G.; Andreu, D.; Arrondo, J. L.; Nieva, J. L. Structural analysis and assembly of the HIV-1 Gp41 amino-terminal fusion peptide and the pretransmembrane amphipathic-at-interface sequence. Biochemistry (Mosc), 2006, 45 (48), 14337-14346.
    • (2006) Biochemistry (Mosc) , vol.45 , Issue.48 , pp. 14337-14346
    • Lorizate, M.1    de la Arada, I.2    Huarte, N.3    Sanchez-Martinez, S.4    de la Torre, B.G.5    Andreu, D.6    Arrondo, J.L.7    Nieva, J.L.8
  • 44
    • 33745268875 scopus 로고    scopus 로고
    • Membrane-transferring sequences of the HIV-1 Gp41 ectodomain assemble into an immunogenic complex
    • Lorizate, M.; Gomara, M. J.; de la Torre, B. G.; Andreu, D.; Nieva, J. L. Membrane-transferring sequences of the HIV-1 Gp41 ectodomain assemble into an immunogenic complex. J. Mol. Biol., 2006, 360 (1), 45-55.
    • (2006) J. Mol. Biol , vol.360 , Issue.1 , pp. 45-55
    • Lorizate, M.1    Gomara, M.J.2    de la Torre, B.G.3    Andreu, D.4    Nieva, J.L.5
  • 45
    • 34548170245 scopus 로고    scopus 로고
    • Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion
    • Bellamy-McIntyre, A. K.; Lay, C. S.; Baar, S.; Maerz, A. L.; Talbo, G. H.; Drummer, H. E.; Poumbourios, P. Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion. J. Biol. Chem., 2007, 282 (32), 23104-23116.
    • (2007) J. Biol. Chem , vol.282 , Issue.32 , pp. 23104-23116
    • Bellamy-McIntyre, A.K.1    Lay, C.S.2    Baar, S.3    Maerz, A.L.4    Talbo, G.H.5    Drummer, H.E.6    Poumbourios, P.7
  • 47
    • 70049117718 scopus 로고    scopus 로고
    • Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action
    • Wexler-Cohen, Y.; Shai, Y. Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action. PLoS Pathog., 2009, 5 (7), e1000509.
    • (2009) PLoS Pathog , vol.5 , Issue.7
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 48
    • 16244387946 scopus 로고    scopus 로고
    • A peptide pertaining to the loop segment of human immunodeficiency virus gp41 binds and interacts with model biomembranes: Implications for the fusion mechanism
    • Pascual, R.; Moreno, M. R.; Villalain, J. A peptide pertaining to the loop segment of human immunodeficiency virus gp41 binds and interacts with model biomembranes: implications for the fusion mechanism. J. Virol., 2005, 79 (8), 5142-5152.
    • (2005) J. Virol , vol.79 , Issue.8 , pp. 5142-5152
    • Pascual, R.1    Moreno, M.R.2    Villalain, J.3
  • 49
    • 1042298782 scopus 로고    scopus 로고
    • Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan
    • Moreno, M. R.; Pascual, R.; Villalain, J. Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan. Biochim. Biophys. Acta, 2004, 1661 (1), 97-105.
    • (2004) Biochim. Biophys. Acta , vol.1661 , Issue.1 , pp. 97-105
    • Moreno, M.R.1    Pascual, R.2    Villalain, J.3
  • 50
    • 65249139402 scopus 로고    scopus 로고
    • Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: Implication for mode of action
    • Lev, N.; Fridmann-Sirkis, Y.; Blank, L.; Bitler, A.; Epand, R. F.; Epand, R. M.; Shai, Y. Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action. Biochemistry (Mosc,) 2009, 48 (14), 3166-3175.
    • (2009) Biochemistry (Mosc,) , vol.48 , Issue.14 , pp. 3166-3175
    • Lev, N.1    Fridmann-Sirkis, Y.2    Blank, L.3    Bitler, A.4    Epand, R.F.5    Epand, R.M.6    Shai, Y.7
  • 51
    • 35348957822 scopus 로고    scopus 로고
    • Fatty acids can substitute the HIV fusion peptide in lipid merging and fusion: An analogy between viral and palmitoylated eukaryotic fusion proteins
    • Lev, N.; Shai, Y. Fatty acids can substitute the HIV fusion peptide in lipid merging and fusion: an analogy between viral and palmitoylated eukaryotic fusion proteins. J. Mol. Biol., 2007, 374 (1), 220-230.
    • (2007) J. Mol. Biol , vol.374 , Issue.1 , pp. 220-230
    • Lev, N.1    Shai, Y.2
  • 52
    • 33751074984 scopus 로고    scopus 로고
    • Functional and structural characterization of HIV-1 gp41 ectodomain regions in phospholipid membranes suggests that the fusion-active conformation is extended
    • Korazim, O.; Sackett, K.; Shai, Y. Functional and structural characterization of HIV-1 gp41 ectodomain regions in phospholipid membranes suggests that the fusion-active conformation is extended. J. Mol. Biol., 2006, 364 (5), 1103-1117.
    • (2006) J. Mol. Biol , vol.364 , Issue.5 , pp. 1103-1117
    • Korazim, O.1    Sackett, K.2    Shai, Y.3
  • 53
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation
    • Markosyan, R. M.; Cohen, F. S.; Melikyan, G. B. HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol. Biol. Cell, 2003, 14 (3), 926-938.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.3 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 54
    • 79251528593 scopus 로고    scopus 로고
    • Targeting cell entry of enveloped viruses as an antiviral strategy
    • Teissier, E.; Penin, F.; Pecheur, E. I. Targeting cell entry of enveloped viruses as an antiviral strategy. Molecules, 2011, 16 (1), 221-250.
    • (2011) Molecules , vol.16 , Issue.1 , pp. 221-250
    • Teissier, E.1    Penin, F.2    Pecheur, E.I.3
  • 55
    • 67649506170 scopus 로고    scopus 로고
    • Role of lipid structure in the humoral immune response in mice to covalent lipid-peptides from the membrane proximal region of HIV-1 gp41
    • Watson, D. S.; Szoka, F. C. Jr. Role of lipid structure in the humoral immune response in mice to covalent lipid-peptides from the membrane proximal region of HIV-1 gp41. Vaccine, 2009, 27 (34), 4672-4683.
    • (2009) Vaccine , vol.27 , Issue.34 , pp. 4672-4683
    • Watson, D.S.1    Szoka, F.C.2
  • 56
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M.; Delos, S. E.; Brecher, M.; Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol., 2008, 43 (3), 189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 57
    • 77957873197 scopus 로고    scopus 로고
    • Palmitic acid analogs exhibit nanomolar binding affinity for the HIV-1 CD4 receptor and nanomolar inhibition of gp120-to-CD4 fusion
    • Paskaleva, E. E.; Xue, J.; Lee, D. Y.; Shekhtman, A.; Canki, M. Palmitic acid analogs exhibit nanomolar binding affinity for the HIV-1 CD4 receptor and nanomolar inhibition of gp120-to-CD4 fusion. PLoS One, 2010, 5 (8), e12168.
    • (2010) PLoS One , vol.5 , Issue.8
    • Paskaleva, E.E.1    Xue, J.2    Lee, D.Y.3    Shekhtman, A.4    Canki, M.5
  • 59
    • 33645781308 scopus 로고    scopus 로고
    • Phosphorothioate oligonucleotides inhibit human immunodeficiency virus type 1 fusion by blocking gp41 core formation
    • Vaillant, A.; Juteau, J. M.; Lu, H.; Liu, S.; Lackman-Smith, C.; Ptak, R.; Jiang, S. Phosphorothioate oligonucleotides inhibit human immunodeficiency virus type 1 fusion by blocking gp41 core formation. Antimicrob. Agents Chemother., 2006, 50 (4), 1393-1401.
    • (2006) Antimicrob. Agents Chemother , vol.50 , Issue.4 , pp. 1393-1401
    • Vaillant, A.1    Juteau, J.M.2    Lu, H.3    Liu, S.4    Lackman-Smith, C.5    Ptak, R.6    Jiang, S.7
  • 63
    • 2942622122 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of cellulose acetate phthalate: Synergy with soluble CD4 and induction of dead-end gp41 six-helix bundles
    • Neurath, A. R.; Strick, N.; Jiang, S.; Li, Y. Y.; Debnath, A. K. Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of dead-end gp41 six-helix bundles. BMC Infect. Dis., 2002, 2, 6.
    • (2002) BMC Infect. Dis , vol.2 , pp. 6
    • Neurath, A.R.1    Strick, N.2    Jiang, S.3    Li, Y.Y.4    Debnath, A.K.5
  • 64
    • 0037153583 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of anionic polymers: A comparative study of candidate microbicides
    • Neurath, A. R.; Strick, N.; Li, Y. Y. Anti-HIV-1 activity of anionic polymers: a comparative study of candidate microbicides. BMC Infect. Dis., 2002, 2, 27-37.
    • (2002) BMC Infect. Dis , vol.2 , pp. 27-37
    • Neurath, A.R.1    Strick, N.2    Li, Y.Y.3
  • 65
    • 33646891072 scopus 로고    scopus 로고
    • Cellulose acetate 1,2-benzenedicarboxylate inhibits infection by cell-free and cell-associated primary HIV-1 isolates
    • Lu, H.; Zhao, Q.; Wallace, G.; Liu, S.; He, Y.; Shattock, R.; Neurath, A. R.; Jiang, B. S. Cellulose acetate 1,2-benzenedicarboxylate inhibits infection by cell-free and cell-associated primary HIV-1 isolates. Aids Res. Human Retroviruses, 2006, 22 (5), 411-418.
    • (2006) Aids Res. Human Retroviruses , vol.22 , Issue.5 , pp. 411-418
    • Lu, H.1    Zhao, Q.2    Wallace, G.3    Liu, S.4    He, Y.5    Shattock, R.6    Neurath, A.R.7    Jiang, B.S.8
  • 66
    • 18244385201 scopus 로고    scopus 로고
    • Combination of candidate microbicides cellulose acetate 1,2-benzenedicarboxylate and UC781 has synergistic and complementary effects against human immunodeficiency virus type 1 infection
    • Liu, S.; Lu, H.; Neurath, A. R.; Jiang, S. Combination of candidate microbicides cellulose acetate 1,2-benzenedicarboxylate and UC781 has synergistic and complementary effects against human immunodeficiency virus type 1 infection. Antimicrob. Agents Chemother., 2005, 49 (5), 1830-1836.
    • (2005) Antimicrob. Agents Chemother , vol.49 , Issue.5 , pp. 1830-1836
    • Liu, S.1    Lu, H.2    Neurath, A.R.3    Jiang, S.4
  • 67
    • 0033918345 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate and C31G as microbicidal alternatives to nonoxynol 9: Comparative sensitivity of primary human vaginal keratinocytes
    • Krebs, F. C.; Miller, S. R.; Catalone, B. J.; Welsh, P. A.; Malamud, D.; Howett, M. K.; Wigdahl, B. Sodium dodecyl sulfate and C31G as microbicidal alternatives to nonoxynol 9: comparative sensitivity of primary human vaginal keratinocytes. Antimicrob. Agents Chemother., 2000, 44 (7), 1954-1960.
    • (2000) Antimicrob. Agents Chemother , vol.44 , Issue.7 , pp. 1954-1960
    • Krebs, F.C.1    Miller, S.R.2    Catalone, B.J.3    Welsh, P.A.4    Malamud, D.5    Howett, M.K.6    Wigdahl, B.7
  • 68
    • 29744461100 scopus 로고    scopus 로고
    • Prioritizing prevention of HIV and sexually transmitted infections: First-generation vaginal microbicides
    • Madan, R. P.; Keller, M. J.; Herold, B. C. Prioritizing prevention of HIV and sexually transmitted infections: first-generation vaginal microbicides. Curr. Opin. Infect. Dis., 2006, 19 (1), 49-54.
    • (2006) Curr. Opin. Infect. Dis , vol.19 , Issue.1 , pp. 49-54
    • Madan, R.P.1    Keller, M.J.2    Herold, B.C.3
  • 69
    • 33847390394 scopus 로고    scopus 로고
    • Microbicide drug candidates to prevent HIV infection
    • Balzarini, J.; Van Damme, L. Microbicide drug candidates to prevent HIV infection. Lancet, 2007, 369 (9563), 787-97.
    • (2007) Lancet , vol.369 , Issue.9563 , pp. 787-797
    • Balzarini, J.1    van Damme, L.2
  • 70
    • 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, A. K.; 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), 3203-3209.
    • (1999) J. Med. Chem , vol.42 , Issue.17 , pp. 3203-3209
    • Debnath, A.K.1    Radigan, L.2    Jiang, S.3
  • 71
    • 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.; Liu, S.; Jiang, S. 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), 4987-4998.
    • (2009) Antimicrob. Agents Chemother , vol.53 , Issue.12 , 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    Liu, S.11    Jiang, S.12
  • 72
    • 34447260888 scopus 로고    scopus 로고
    • A Novel fluorescence intensity screening assay identifies new low molecular weight inhibitors of the gp41 coiled coil domain of HIV-1
    • Cai, L.; Gochin, M. A Novel fluorescence intensity screening assay identifies new low molecular weight inhibitors of the gp41 coiled coil domain of HIV-1. Antimicrob. Agents Chemother., 2007, 51 (7), 2388-2395.
    • (2007) Antimicrob. Agents Chemother , vol.51 , Issue.7 , pp. 2388-2395
    • Cai, L.1    Gochin, M.2
  • 73
    • 1342279557 scopus 로고    scopus 로고
    • Synthesis and anti-HIV-1 activity of 4-[4-(4,6-bisphenylamino-[1,3,5]triazin-2-ylamino)-5-methoxy-2-methylphenylazo]-5-hydroxynaphthalene-2,7-disulfonic acid and its derivatives
    • Naicker, K. P.; Jiang, S.; Lu, H.; Ni, J.; Boyer-Chatenet, L.; Wang, L.-X.; Debnath, A. K. Synthesis and anti-HIV-1 activity of 4-[4-(4,6-bisphenylamino-[1,3,5]triazin-2-ylamino)-5-methoxy-2-methylphenylazo]-5-hydroxynaphthalene-2,7-disulfonic acid and its derivatives. Bioorg. Med. Chem., 2004, 12, 1215-1220.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 1215-1220
    • Naicker, K.P.1    Jiang, S.2    Lu, H.3    Ni, J.4    Boyer-Chatenet, L.5    Wang, L.-X.6    Debnath, A.K.7
  • 75
    • 0037199880 scopus 로고    scopus 로고
    • Identification of inhibitors of the HIV-1 gp41 six-helix bundle formation from extracts of Chinese medicinal herbs Prunella vulgaris and Rhizoma cibotte
    • Liu, S.; Jiang, S.; Wu, Z.; Lv, L.; Zhang, J.; Zhu, Z.; Wu, S. Identification of inhibitors of the HIV-1 gp41 six-helix bundle formation from extracts of Chinese medicinal herbs Prunella vulgaris and Rhizoma cibotte. Life Sci., 2002, 71 (15), 1779-1791.
    • (2002) Life Sci , vol.71 , Issue.15 , pp. 1779-1791
    • Liu, S.1    Jiang, S.2    Wu, Z.3    Lv, L.4    Zhang, J.5    Zhu, Z.6    Wu, S.7
  • 76
    • 19744379597 scopus 로고    scopus 로고
    • Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41
    • Liu, S.; Lu, H.; Zhao, Q.; He, Y.; Niu, J.; Debnath, A. K.; Wu, S.; Jiang, S. Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41. Biochim. Biophys Acta, 2005, 1723 (1-3), 270-281.
    • (2005) Biochim. Biophys Acta , vol.1723 , Issue.1-3 , pp. 270-281
    • Liu, S.1    Lu, H.2    Zhao, Q.3    He, Y.4    Niu, J.5    Debnath, A.K.6    Wu, S.7    Jiang, S.8
  • 77
    • 0442309451 scopus 로고    scopus 로고
    • Tannin inhibits HIV-1 entry by targeting gp41
    • Lu, L.; Liu, S. W.; Jiang, S. B.; Wu, S. G. Tannin inhibits HIV-1 entry by targeting gp41. Acta Pharmacol. Sin., 2004, 25 (2), 213-218.
    • (2004) Acta Pharmacol. Sin , vol.25 , Issue.2 , pp. 213-218
    • Lu, L.1    Liu, S.W.2    Jiang, S.B.3    Wu, S.G.4
  • 78
    • 33846844941 scopus 로고    scopus 로고
    • Discovery of small-molecule HIV-1 fusion and integrase inhibitors oleuropein and hydroxytyrosol: Part I. fusion [corrected] inhibition
    • Lee-Huang, S.; Huang, P. L.; Zhang, D.; Lee, J. W.; Bao, J.; Sun, Y.; Chang, Y. T.; Zhang, J.; Huang, P. L. Discovery of small-molecule HIV-1 fusion and integrase inhibitors oleuropein and hydroxytyrosol: Part I. fusion [corrected] inhibition. Biochem. Biophys. Res. Commun., 2007, 354 (4), 872-878.
    • (2007) Biochem. Biophys. Res. Commun , vol.354 , Issue.4 , pp. 872-878
    • Lee-Huang, S.1    Huang, P.L.2    Zhang, D.3    Lee, J.W.4    Bao, J.5    Sun, Y.6    Chang, Y.T.7    Zhang, J.8    Huang, P.L.9
  • 79
    • 34249688326 scopus 로고    scopus 로고
    • Computational study of bindings of olive leaf extract (OLE) to HIV-1 fusion protein gp41
    • Bao, J.; Zhang, D. W.; Zhang, J. Z.; Huang, P. L.; Huang, P. L.; Lee-Huang, S. Computational study of bindings of olive leaf extract (OLE) to HIV-1 fusion protein gp41. FEBS Lett., 2007, 581 (14), 2737-2742.
    • (2007) FEBS Lett , vol.581 , Issue.14 , pp. 2737-2742
    • Bao, J.1    Zhang, D.W.2    Zhang, J.Z.3    Huang, P.L.4    Huang, P.L.5    Lee-Huang, S.6
  • 81
    • 7044231888 scopus 로고    scopus 로고
    • Conserved residues in the coiled-coil pocket of human immunodeficiency virus type 1 gp41 are essential for viral replication and interhelical interaction
    • Mo, H.; Konstantinidis, A. K.; Stewart, K.; Dekhtyar, T.; Ng, T.; Swift, K.; Matayoshi, E.; Kati, W.; Kohlbrenner, W.; Molla, A. Conserved residues in the coiled-coil pocket of human immunodeficiency virus type 1 gp41 are essential for viral replication and interhelical interaction. Virology, 2004, 329 (2), 319-327.
    • (2004) Virology , vol.329 , Issue.2 , pp. 319-327
    • Mo, H.1    Konstantinidis, A.K.2    Stewart, K.3    Dekhtyar, T.4    Ng, T.5    Swift, K.6    Matayoshi, E.7    Kati, W.8    Kohlbrenner, W.9    Molla, A.10
  • 82
    • 34247219622 scopus 로고    scopus 로고
    • Binding of antifusion peptides with HIVgp41 from molecular dynamics simulations: Quantitative correlation with experiment
    • Strockbine, B.; Rizzo, R. C. Binding of antifusion peptides with HIVgp41 from molecular dynamics simulations: quantitative correlation with experiment. Proteins, 2007, 67 (3), 630-642.
    • (2007) Proteins , vol.67 , Issue.3 , pp. 630-642
    • Strockbine, B.1    Rizzo, R.C.2
  • 85
    • 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 (1), 103-115.
    • (1999) Cell , vol.99 , Issue.1 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 86
    • 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 (24), 7843-7854.
    • (2008) J. Med. Chem , vol.51 , Issue.24 , 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
  • 87
    • 68049108497 scopus 로고    scopus 로고
    • NMR second site screening for structure determination of ligands bound in the hydrophobic pocket of HIV-1 gp41
    • Balogh, E.; Wu, D.; Zhou, G.; Gochin, M. NMR second site screening for structure determination of ligands bound in the hydrophobic pocket of HIV-1 gp41. J. Am. Chem. Soc., 2009, 131 (8), 2821-2823.
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.8 , pp. 2821-2823
    • Balogh, E.1    Wu, D.2    Zhou, G.3    Gochin, M.4
  • 89
    • 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 (5), 1500-1503.
    • (2010) Bioorg. Med. Chem. Lett , vol.20 , Issue.5 , pp. 1500-1503
    • Zhou, G.1    Wu, D.2    Hermel, E.3    Balogh, E.4    Gochin, M.5
  • 90
    • 7244253012 scopus 로고    scopus 로고
    • N-Substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors
    • 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. Antimicrob. Agents Chemother., 2004, 48 (11), 4349-4359.
    • (2004) Antimicrob. Agents Chemother , vol.48 , Issue.11 , pp. 4349-4359
    • Jiang, S.1    Lu, H.2    Liu, S.3    Zhao, Q.4    He, Y.5    Debnath, A.K.6
  • 91
    • 80054910151 scopus 로고    scopus 로고
    • Development of indole compounds as small molecule fusion inhibitors targeting HIV-1 glycoprotein-41
    • 2011 Sep 19. [Epub ahead of print]
    • 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 Sep 19. [Epub ahead of print]
    • J. Med. Chem
    • Zhou, G.1    Wu, D.2    Snyder, B.3    Ptak, R.G.4    Kaur, H.5    Gochin, M.6
  • 92
    • 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 (23), 7631-7639.
    • (2009) J. Med. Chem , vol.52 , Issue.23 , 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
  • 96
    • 78751657690 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of novel 5-((Arylfuran/1H-pyrrol-2-yl)methylene)-2-thioxo-3-(3-(trifluoromethyl)phe nyl)thiazolidin-4-ones as HIV-1 fusion inhibitors targeting gp41
    • Jiang, S.; Tala, S. R.; Lu, H.; Abo-Dya, N. E.; Avan, I.; Gyanda, K.; Lu, L.; Katritzky, A. R.; Debnath, A. K. Design, synthesis, and biological activity of novel 5-((Arylfuran/1H-pyrrol-2-yl)methylene)-2-thioxo-3-(3-(trifluoromethyl)phe nyl)thiazolidin-4-ones as HIV-1 fusion inhibitors targeting gp41. J. Med. Chem., 2011, 54 (2), 572-579.
    • (2011) J. Med. Chem , vol.54 , Issue.2 , pp. 572-579
    • Jiang, S.1    Tala, S.R.2    Lu, H.3    Abo-Dya, N.E.4    Avan, I.5    Gyanda, K.6    Lu, L.7    Katritzky, A.R.8    Debnath, A.K.9
  • 97
    • 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 (2), 278-281.
    • (2002) Angew Chem. Int. Ed. Engl , vol.41 , Issue.2 , pp. 278-281
    • Ernst, J.T.1    Kutzki, O.2    Debnath, A.K.3    Jiang, S.4    Lu, H.5    Hamilton, A.D.6
  • 100
    • 0030802750 scopus 로고    scopus 로고
    • Resistance to a drug blocking human immunodeficiency virus type 1 entry (RPR103611) is conferred by mutations in gp41
    • Labrosse, B.; Pleskoff, O.; Sol, N.; Jones, C.; Hénin, Y.; Alizon, M. Resistance to a drug blocking human immunodeficiency virus type 1 entry (RPR103611) is conferred by mutations in gp41. J. Virol., 1997, 71 (11), 8230-8236.
    • (1997) J. Virol , vol.71 , Issue.11 , pp. 8230-8236
    • Labrosse, B.1    Pleskoff, O.2    Sol, N.3    Jones, C.4    Hénin, Y.5    Alizon, M.6
  • 101
    • 77953771721 scopus 로고    scopus 로고
    • A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41
    • Murray, E. J.; Leaman, D. P.; Pawa, N.; Perkins, H.; Pickford, C.; Perros, M.; Zwick, M. B.; Butler, S. L. A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41. J. Virol., 2010, 84 (14), 7288-7299.
    • (2010) J. Virol , vol.84 , Issue.14 , pp. 7288-7299
    • Murray, E.J.1    Leaman, D.P.2    Pawa, N.3    Perkins, H.4    Pickford, C.5    Perros, M.6    Zwick, M.B.7    Butler, S.L.8
  • 102
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A.; McClendon, C. L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature, 2007, 450 (7172), 1001-1009.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 103
    • 50249154886 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • Berg, T. Small-molecule inhibitors of protein-protein interactions. Curr. Opin. Drug Discov. Devel., 2008, 11 (5), 666-674.
    • (2008) Curr. Opin. Drug Discov. Devel , vol.11 , Issue.5 , pp. 666-674
    • Berg, T.1
  • 104
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B.; Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. Discovering high-affinity ligands for proteins: SAR by NMR. Science, 1996, 274 (5292), 1531-1534.
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 105
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • Hajduk, P. J. Fragment-based drug design: how big is too big? J. Med. Chem., 2006, 49 (24), 6972-6976.
    • (2006) J. Med. Chem , vol.49 , Issue.24 , pp. 6972-6976
    • Hajduk, P.J.1
  • 106
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M. R.; Wells, J. A. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat. Rev. Drug Discov., 2004, 3 (4), 301-317.
    • (2004) Nat. Rev. Drug Discov , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 107
    • 79955639492 scopus 로고    scopus 로고
    • Paramagnetic relaxation assisted docking of a small indole compound in the HIV-1 gp41 hydrophobic pocket
    • 2010, in press
    • Gochin, M.; Zhou, G.; Phillips, A. H. Paramagnetic relaxation assisted docking of a small indole compound in the HIV-1 gp41 hydrophobic pocket. ACS Chem. Biol., 2010, in press.
    • ACS Chem. Biol
    • Gochin, M.1    Zhou, G.2    Phillips, A.H.3
  • 108
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • Berman, H.; Henrick, K.; Nakamura, H. Announcing the worldwide Protein Data Bank (www.pdb.org). Nat. Struct. Biol., 2003, 10 (12), 980.
    • (2003) Nat. Struct. Biol , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 109
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon, V.; Natrajan, G.; Schibli, D.; Campelo, F.; Kozlov, M. M.; Weissenhorn, W. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog., 2010, 6 (5), e1000880.
    • (2010) PLoS Pathog , vol.6 , Issue.5
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 110
    • 77951670043 scopus 로고    scopus 로고
    • Origins of resistance to the HIVgp41 viral entry inhibitor T20
    • McGillick, B. E.; Balius, T. E.; Mukherjee, S.; Rizzo, R. C. Origins of resistance to the HIVgp41 viral entry inhibitor T20. Biochemistry (Mosc), 2010, 49 (17), 3575-3592.
    • (2010) Biochemistry (Mosc) , vol.49 , Issue.17 , pp. 3575-3592
    • McGillick, B.E.1    Balius, T.E.2    Mukherjee, S.3    Rizzo, R.C.4
  • 111
    • 33746838814 scopus 로고    scopus 로고
    • Characterization of the HIV N-terminal fusion peptide-containing region in context of key gp41 fusion conformations
    • Sackett, K.; Wexler-Cohen, Y.; Shai, Y. Characterization of the HIV N-terminal fusion peptide-containing region in context of key gp41 fusion conformations. J. Biol. Chem., 2006, 281 (31), 21755-21762.
    • (2006) J. Biol. Chem , vol.281 , Issue.31 , pp. 21755-21762
    • Sackett, K.1    Wexler-Cohen, Y.2    Shai, Y.3
  • 112
    • 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 (6), 685-693.
    • (2003) J. Biomol. Screen , vol.8 , Issue.6 , pp. 685-693
    • Liu, S.1    Boyer-Chatenet, L.2    Lu, H.3    Jiang, S.4
  • 113
    • 64149114614 scopus 로고    scopus 로고
    • 1,2,6-tri-O-galloyl-beta-D-glucopyranose inhibits gp41-mediated HIV envelope fusion with target cell membrane
    • Sun, W.; Wang, H. T.; Xia, C. L.; Wu, S. G.; Jiang, S. B.; Jiang, Z. H.; Liu, S. W. [1,2,6-tri-O-galloyl-beta-D-glucopyranose inhibits gp41-mediated HIV envelope fusion with target cell membrane]. Nan Fang Yi Ke Da Xue Xue Bao, 2008, 28 (7), 1127-1131.
    • (2008) Nan Fang Yi Ke Da Xue Xue Bao , vol.28 , Issue.7 , pp. 1127-1131
    • Sun, W.1    Wang, H.T.2    Xia, C.L.3    Wu, S.G.4    Jiang, S.B.5    Jiang, Z.H.6    Liu, S.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.