메뉴 건너뛰기




Volumn 19, Issue 10, 2013, Pages 1800-1809

Synthesized peptide inhibitors of HIV-1 gp41-dependent membrane fusion

Author keywords

Antivirals; HIV 1; Membrane fusion; Peptide inhibitor

Indexed keywords

ALBUVIRTIDE; C 34; C 34M3; CP 32M; CP 621 652; DP 107; ENFUVIRTIDE; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; IQN 17; IQN 23; N 36; PLERIXAFOR; SC 22EK; SC 29EK; SC 34EK; SC 35EK; SIFUVIRTIDE; SJ 2176; T 21; T 2544; T 2635; T 267229; T 651; TIFUVIRTIDE; UNCLASSIFIED DRUG; VIR 353; VIR 576; VIRUS INHIBITORY PEPTIDE; ZIDOVUDINE;

EID: 84875685505     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319100004     Document Type: Review
Times cited : (55)

References (107)
  • 1
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC. Viral membrane fusion. Nat Struct Mol Biol 2008; 15: 690-8.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1
  • 2
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS. Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 2001; 70: 777-810.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 3
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman PM, Lawrence MC. The structural biology of type I viral membrane fusion. Nat Rev Mol Cell Biol 2003; 4: 309-19.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 4
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS. HIV entry and its inhibition. Cell 1998; 93: 681-4.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997; 89: 263-73.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 6
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu J, Wang J, Shen S, Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci USA 1997; 94: 12303-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 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 DC, Chutkowski CT, Kim PS. 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: 15613-7.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 9
    • 2942590370 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides
    • Bosch BJ, Martina BE, Van Der Zee R, et al. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Proc Natl Acad Sci USA 2004; 101: 8455-60.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8455-8460
    • Bosch, B.J.1    Martina, B.E.2    van der Zee, R.3
  • 10
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994; 371: 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 11
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W, Carfi A, Lee KH, Skehel JJ, Wiley DC. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol Cell 1998; 2: 605-16.
    • (1998) Mol Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 12
  • 13
    • 79960463354 scopus 로고    scopus 로고
    • Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor
    • Ashkenazi A, Wexler-Cohen Y, Shai Y. Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor. Biochim Biophys Acta 2011; 1808: 2352-8.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 2352-2358
    • Ashkenazi, A.1    Wexler-Cohen, Y.2    Shai, Y.3
  • 14
    • 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: 1143-58.
    • (2010) Curr Pharm Des , vol.16 , pp. 1143-1158
    • Steffen, I.1    Pohlmann, S.2
  • 15
    • 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: 10537-41.
    • (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
  • 17
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild C, Greenwell T, Matthews T. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res Hum Retroviruses 1993; 9: 1051-3.
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 18
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, Kim PS. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 1995; 2: 1075-82.
    • (1995) Nat Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 19
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • Lu M, Kim PS. A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J Biomol Struct Dyn 1997; 15: 465-71.
    • (1997) J Biomol Struct Dyn , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 20
    • 0032899254 scopus 로고    scopus 로고
    • Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: Implications for viral membrane fusion
    • Lu M, Ji H, Shen S. Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion. J Virol 1999; 73: 4433-8.
    • (1999) J Virol , vol.73 , pp. 4433-4438
    • Lu, M.1    Ji, H.2    Shen, S.3
  • 22
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc Natl Acad Sci USA 1994; 91: 9770-4.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 23
    • 27544447546 scopus 로고    scopus 로고
    • Inhibition of HIV-1 group M and O isolates by fusion inhibitors
    • Chinnadurai R, Munch J, Dittmar MT, Kirchhoff F. Inhibition of HIV-1 group M and O isolates by fusion inhibitors. AIDS 2005; 19: 1919-22.
    • (2005) AIDS , vol.19 , pp. 1919-1922
    • Chinnadurai, R.1    Munch, J.2    Dittmar, M.T.3    Kirchhoff, F.4
  • 24
    • 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: 1302-7.
    • (1998) Nat Med , vol.4 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3
  • 25
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults
    • Kilby JM, Lalezari JP, Eron JJ, et al. The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults. AIDS Res Hum Retroviruses 2002; 18: 685-93.
    • (2002) AIDS Res Hum Retroviruses , vol.18 , pp. 685-693
    • Kilby, J.M.1    Lalezari, J.P.2    Eron, J.J.3
  • 26
    • 0037471311 scopus 로고    scopus 로고
    • A phase II clinical study of the long-term safety and antiviral activity of enfuvirtide-based antiretroviral therapy
    • Lalezari JP, Eron JJ, Carlson M, et al. A phase II clinical study of the long-term safety and antiviral activity of enfuvirtide-based antiretroviral therapy. AIDS 2003; 17: 691-8.
    • (2003) AIDS , vol.17 , pp. 691-698
    • Lalezari, J.P.1    Eron, J.J.2    Carlson, M.3
  • 27
    • 10744229122 scopus 로고    scopus 로고
    • A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in nonnucleoside reverse transcriptase inhibitor-naive HIV-infected adults
    • Lalezari JP, DeJesus E, Northfelt DW, et al. A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in nonnucleoside reverse transcriptase inhibitor-naive HIV-infected adults. Antivir Ther 2003; 8: 279-87.
    • (2003) Antivir Ther , vol.8 , pp. 279-287
    • Lalezari, J.P.1    DeJesus, E.2    Northfelt, D.W.3
  • 28
    • 27944453927 scopus 로고    scopus 로고
    • Safety of enfuvirtide in combination with an optimized background of antiretrovirals in treatment-experienced HIV-1-infected adults over 48 weeks
    • Trottier B, Walmsley S, Reynes J, et al. Safety of enfuvirtide in combination with an optimized background of antiretrovirals in treatment-experienced HIV-1-infected adults over 48 weeks. J Acquir Immune Defic Syndr 2005; 40: 413-21.
    • (2005) J Acquir Immune Defic Syndr , vol.40 , pp. 413-421
    • Trottier, B.1    Walmsley, S.2    Reynes, J.3
  • 29
    • 33644834760 scopus 로고    scopus 로고
    • Week-12 response to therapy as a predictor of week 24, 48, and 96 outcome in patients receiving the HIV fusion inhibitor enfuvirtide in the T-20 versus Optimized Regimen Only (TORO) trials
    • Raffi F, Katlama C, Saag M, et al. Week-12 response to therapy as a predictor of week 24, 48, and 96 outcome in patients receiving the HIV fusion inhibitor enfuvirtide in the T-20 versus Optimized Regimen Only (TORO) trials. Clin Infect Dis 2006; 42: 870-7.
    • (2006) Clin Infect Dis , vol.42 , pp. 870-877
    • Raffi, F.1    Katlama, C.2    Saag, M.3
  • 30
    • 0038576281 scopus 로고    scopus 로고
    • Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America
    • Lalezari JP, Henry K, O'Hearn M, et al. Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America. N Engl J Med 2003; 348: 2175-85.
    • (2003) N Engl J Med , vol.348 , pp. 2175-2185
    • Lalezari, J.P.1    Henry, K.2    O'Hearn, M.3
  • 31
    • 0037849954 scopus 로고    scopus 로고
    • Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia
    • Lazzarin A, Clotet B, Cooper D, et al. Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia. N Engl J Med 2003; 348: 2186-95.
    • (2003) N Engl J Med , vol.348 , pp. 2186-2195
    • Lazzarin, A.1    Clotet, B.2    Cooper, D.3
  • 32
    • 63649151400 scopus 로고    scopus 로고
    • Interactions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coil
    • Champagne K, Shishido A, Root MJ. Interactions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coil. J Biol Chem 2009; 284: 3619-27.
    • (2009) J Biol Chem , vol.284 , pp. 3619-3627
    • Champagne, K.1    Shishido, A.2    Root, M.J.3
  • 33
    • 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 SG, Gallo SA, 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: 21012-7.
    • (2003) J Biol Chem , vol.278 , pp. 21012-21017
    • Peisajovich, S.G.1    Gallo, S.A.2    Blumenthal, R.3    Shai, Y.4
  • 34
    • 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: 3677-84.
    • (2007) FASEB J , vol.21 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 35
    • 0035846960 scopus 로고    scopus 로고
    • Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage
    • Kliger Y, Gallo SA, Peisajovich SG, et al. Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage. J Biol Chem 2001; 276: 1391-7.
    • (2001) J Biol Chem , vol.276 , pp. 1391-1397
    • Kliger, Y.1    Gallo, S.A.2    Peisajovich, S.G.3
  • 36
    • 33646903467 scopus 로고    scopus 로고
    • Structurally altered peptides reveal an important role for N-terminal heptad repeat binding and stability in the inhibitory action of HIV-1 peptide DP178
    • Wexler-Cohen Y, Johnson BT, Puri A, Blumenthal R, Shai Y. Structurally altered peptides reveal an important role for N-terminal heptad repeat binding and stability in the inhibitory action of HIV-1 peptide DP178. J Biol Chem 2006; 281: 9005-10.
    • (2006) J Biol Chem , vol.281 , pp. 9005-9010
    • Wexler-Cohen, Y.1    Johnson, B.T.2    Puri, A.3    Blumenthal, R.4    Shai, Y.5
  • 37
    • 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: 11259-73.
    • (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
  • 38
    • 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 MM, Weissenhorn W. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog 2010; 6: e1000880.
    • (2010) PLoS Pathog , vol.6
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 39
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn CA, Decker JM, Sfakianos JN, et al. Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J Virol 2001; 75: 8605-14.
    • (2001) J Virol , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3
  • 40
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves JD, Gallo SA, Ahmad N, et al. Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc Natl Acad Sci USA 2002; 99: 16249-54.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmad, N.3
  • 41
    • 2342466810 scopus 로고    scopus 로고
    • CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor
    • Yuan W, Craig S, Si Z, Farzan M, Sodroski J. CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor. J Virol 2004; 78: 5448-57.
    • (2004) J Virol , vol.78 , pp. 5448-5457
    • Yuan, W.1    Craig, S.2    Si, Z.3    Farzan, M.4    Sodroski, J.5
  • 43
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, Matthews TJ. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 1998; 72: 986-93.
    • (1998) J Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 44
    • 7644236011 scopus 로고    scopus 로고
    • Emergence of a drugdependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor
    • Baldwin CE, Sanders RW, Deng Y, et al. Emergence of a drugdependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor. J Virol 2004; 78: 12428-37.
    • (2004) J Virol , vol.78 , pp. 12428-12437
    • Baldwin, C.E.1    Sanders, R.W.2    Deng, Y.3
  • 45
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • Wei X, Decker JM, Liu H, et al. Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob Agents Chemother 2002; 46: 1896-905.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3
  • 46
    • 25144489604 scopus 로고    scopus 로고
    • Impact of human immunodeficiency virus type 1 gp41 amino acid substitutions selected during enfuvirtide treatment on gp41 binding and antiviral potency of enfuvirtide in vitro
    • Mink M, Mosier SM, Janumpalli S, et al. Impact of human immunodeficiency virus type 1 gp41 amino acid substitutions selected during enfuvirtide treatment on gp41 binding and antiviral potency of enfuvirtide in vitro. J Virol 2005; 79: 12447-54.
    • (2005) J Virol , vol.79 , pp. 12447-12454
    • Mink, M.1    Mosier, S.M.2    Janumpalli, S.3
  • 47
    • 4444310448 scopus 로고    scopus 로고
    • Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates
    • Sista PR, Melby T, Davison D, et al. Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates. AIDS 2004; 18: 1787-94.
    • (2004) AIDS , vol.18 , pp. 1787-1794
    • Sista, P.R.1    Melby, T.2    Davison, D.3
  • 48
    • 4344685387 scopus 로고    scopus 로고
    • Genotype and phenotype patterns of human immunodeficiency virus type 1 resistance to enfuvirtide during long-term treatment
    • Menzo S, Castagna A, Monachetti A, et al. Genotype and phenotype patterns of human immunodeficiency virus type 1 resistance to enfuvirtide during long-term treatment. Antimicrob Agents Chemother 2004; 48: 3253-9.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3253-3259
    • Menzo, S.1    Castagna, A.2    Monachetti, A.3
  • 49
    • 33646868062 scopus 로고    scopus 로고
    • Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2
    • Melby T, Sista P, DeMasi R, et al. Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2. AIDS Res Hum Retroviruses 2006; 22: 375-85.
    • (2006) AIDS Res Hum Retroviruses , vol.22 , pp. 375-385
    • Melby, T.1    Sista, P.2    DeMasi, R.3
  • 50
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • Greenberg ML, Cammack N. Resistance to enfuvirtide, the first HIV fusion inhibitor. J Antimicrob Chemother 2004; 54: 333-40.
    • (2004) J Antimicrob Chemother , vol.54 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 51
    • 63149093637 scopus 로고    scopus 로고
    • HR-2 mutations in human immunodeficiency virus type 1 gp41 restore fusion kinetics delayed by HR-1 mutations that cause clinical resistance to enfuvirtide
    • Ray N, Blackburn LA, Doms RW. HR-2 mutations in human immunodeficiency virus type 1 gp41 restore fusion kinetics delayed by HR-1 mutations that cause clinical resistance to enfuvirtide. J Virol 2009; 83: 2989-95.
    • (2009) J Virol , vol.83 , pp. 2989-2995
    • Ray, N.1    Blackburn, L.A.2    Doms, R.W.3
  • 52
    • 33847020059 scopus 로고    scopus 로고
    • Full fusion competence rescue of the enfuvirtide resistant HIV-1 gp41 genotype (43D) by a prevalent polymorphism (137K)
    • Tolstrup M, Selzer-Plon J, Laursen AL, et al. Full fusion competence rescue of the enfuvirtide resistant HIV-1 gp41 genotype (43D) by a prevalent polymorphism (137K). AIDS 2007; 21: 519-21.
    • (2007) AIDS , vol.21 , pp. 519-521
    • Tolstrup, M.1    Selzer-Plon, J.2    Laursen, A.L.3
  • 53
    • 20044371998 scopus 로고    scopus 로고
    • Emergence and evolution of enfuvirtide resistance following long-term therapy involves heptad repeat 2 mutations within gp41
    • Xu L, Pozniak A, Wildfire A, et al. Emergence and evolution of enfuvirtide resistance following long-term therapy involves heptad repeat 2 mutations within gp41. Antimicrob Agents Chemother 2005; 49: 1113-9.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1113-1119
    • Xu, L.1    Pozniak, A.2    Wildfire, A.3
  • 54
    • 70350371719 scopus 로고    scopus 로고
    • Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors
    • Eggink D, Langedijk JP, Bonvin AM, et al. Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors. J Biol Chem 2009; 284: 26941-50.
    • (2009) J Biol Chem , vol.284 , pp. 26941-26950
    • Eggink, D.1    Langedijk, J.P.2    Bonvin, A.M.3
  • 55
    • 65349113010 scopus 로고    scopus 로고
    • Mutations in gp120 contribute to the resistance of human immunodeficiency virus type 1 to membrane-anchored C-peptide maC46
    • Hermann FG, Egerer L, Brauer F, et al. Mutations in gp120 contribute to the resistance of human immunodeficiency virus type 1 to membrane-anchored C-peptide maC46. J Virol 2009; 83: 4844-53.
    • (2009) J Virol , vol.83 , pp. 4844-4853
    • Hermann, F.G.1    Egerer, L.2    Brauer, F.3
  • 56
    • 13244288179 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics and drug interaction potential of enfuvirtide
    • Patel IH, Zhang X, Nieforth K, Salgo M, Buss N. Pharmacokinetics, pharmacodynamics and drug interaction potential of enfuvirtide. Clin Pharmacokinet 2005; 44: 175-86.
    • (2005) Clin Pharmacokinet , vol.44 , pp. 175-186
    • Patel, I.H.1    Zhang, X.2    Nieforth, K.3    Salgo, M.4    Buss, N.5
  • 57
    • 0142244854 scopus 로고    scopus 로고
    • Injection site reactions with the HIV-1 fusion inhibitor enfuvirtide
    • Ball RA, Kinchelow T. Injection site reactions with the HIV-1 fusion inhibitor enfuvirtide. J Am Acad Dermatol 2003; 49: 826-31.
    • (2003) J Am Acad Dermatol , vol.49 , pp. 826-831
    • Ball, R.A.1    Kinchelow, T.2
  • 58
    • 54849410704 scopus 로고    scopus 로고
    • Adverse cutaneous reactions associated with the newest antiretroviral drugs in patients with human immunodeficiency virus infection
    • Borras-Blasco J, Navarro-Ruiz A, Borras C, Castera E. Adverse cutaneous reactions associated with the newest antiretroviral drugs in patients with human immunodeficiency virus infection. J Antimicrob Chemother 2008; 62: 879-88.
    • (2008) J Antimicrob Chemother , vol.62 , pp. 879-888
    • Borras-Blasco, J.1    Navarro-Ruiz, A.2    Borras, C.3    Castera, E.4
  • 59
    • 34249935492 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 variants resistant to first-and second-version fusion inhibitors and cytopathic in ex vivo human lymphoid tissue
    • Chinnadurai R, Rajan D, Munch J, Kirchhoff F. Human immunodeficiency virus type 1 variants resistant to first-and second-version fusion inhibitors and cytopathic in ex vivo human lymphoid tissue. J Virol 2007; 81: 6563-72.
    • (2007) J Virol , vol.81 , pp. 6563-6572
    • Chinnadurai, R.1    Rajan, D.2    Munch, J.3    Kirchhoff, F.4
  • 60
    • 20144386372 scopus 로고    scopus 로고
    • T-1249 retains potent antiretroviral activity in patients who had experienced virological failure while on an enfuvirtide-containing treatment regimen
    • Lalezari JP, Bellos NC, Sathasivam K, et al. T-1249 retains potent antiretroviral activity in patients who had experienced virological failure while on an enfuvirtide-containing treatment regimen. J Infect Dis 2005; 191: 1155-63.
    • (2005) J Infect Dis , vol.191 , pp. 1155-1163
    • Lalezari, J.P.1    Bellos, N.C.2    Sathasivam, K.3
  • 61
    • 12144290487 scopus 로고    scopus 로고
    • Short-term safety and antiretroviral activity of T-1249, a second-generation fusion inhibitor of HIV
    • Eron JJ, Gulick RM, Bartlett JA, et al. Short-term safety and antiretroviral activity of T-1249, a second-generation fusion inhibitor of HIV. J Infect Dis 2004; 189: 1075-83.
    • (2004) J Infect Dis , vol.189 , pp. 1075-1083
    • Eron, J.J.1    Gulick, R.M.2    Bartlett, J.A.3
  • 62
    • 27544461723 scopus 로고    scopus 로고
    • Effect of naturally-occurring gp41 HR1 variations on susceptibility of HIV-1 to fusion inhibitors
    • Chinnadurai R, Munch J, Kirchhoff F. Effect of naturally-occurring gp41 HR1 variations on susceptibility of HIV-1 to fusion inhibitors. Aids 2005; 19: 1401-5.
    • (2005) Aids , vol.19 , pp. 1401-1405
    • Chinnadurai, R.1    Munch, J.2    Kirchhoff, F.3
  • 63
    • 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 AS, Santos NC, Loura LM, Fedorov A, Castanho MA. 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: 14758-63.
    • (2004) J Am Chem Soc , vol.126 , pp. 14758-14763
    • Veiga, A.S.1    Santos, N.C.2    Loura, L.M.3    Fedorov, A.4    Castanho, M.A.5
  • 64
    • 16244380203 scopus 로고    scopus 로고
    • Enfuvirtide resistance mutations: Impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization
    • Reeves JD, Lee FH, Miamidian JL, Jabara CB, Juntilla MM, Doms RW. Enfuvirtide resistance mutations: impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization. J Virol 2005; 79: 4991-9.
    • (2005) J Virol , vol.79 , pp. 4991-4999
    • Reeves, J.D.1    Lee, F.H.2    Miamidian, J.L.3    Jabara, C.B.4    Juntilla, M.M.5    Doms, R.W.6
  • 65
    • 38449106443 scopus 로고    scopus 로고
    • Evolution of genotypic and phenotypic resistance during chronic treatment with the fusion inhibitor T-1249
    • Melby T, Demasi R, Cammack N, Miralles GD, Greenberg ML. Evolution of genotypic and phenotypic resistance during chronic treatment with the fusion inhibitor T-1249. AIDS Res Hum Retroviruses 2007; 23: 1366-73.
    • (2007) AIDS Res Hum Retroviruses , vol.23 , pp. 1366-1373
    • Melby, T.1    Demasi, R.2    Cammack, N.3    Miralles, G.D.4    Greenberg, M.L.5
  • 66
    • 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
  • 67
    • 45749135859 scopus 로고    scopus 로고
    • Selection of T1249-resistant human immunodeficiency virus type 1 variants
    • Eggink D, Baldwin CE, Deng Y, et al. Selection of T1249-resistant human immunodeficiency virus type 1 variants. J Virol 2008; 82: 6678-88.
    • (2008) J Virol , vol.82 , pp. 6678-6688
    • Eggink, D.1    Baldwin, C.E.2    Deng, Y.3
  • 68
    • 0036896463 scopus 로고    scopus 로고
    • env chimeric virus technology for evaluating human immunodeficiency virus susceptibility to entry inhibitors
    • Fikkert V, Cherepanov P, Van Laethem K, et al. env chimeric virus technology for evaluating human immunodeficiency virus susceptibility to entry inhibitors. Antimicrob Agents Chemother 2002; 46: 3954-62.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3954-3962
    • Fikkert, V.1    Cherepanov, P.2    van Laethem, K.3
  • 69
    • 33748115445 scopus 로고    scopus 로고
    • Rapid emergence of enfuvirtide resistance in HIV-1-infected patients: Results of a clonal analysis
    • Lu J, Deeks SG, Hoh R, et al. Rapid emergence of enfuvirtide resistance in HIV-1-infected patients: results of a clonal analysis. J Acquir Immune Defic Syndr 2006; 43: 60-4.
    • (2006) J Acquir Immune Defic Syndr , vol.43 , pp. 60-64
    • Lu, J.1    Deeks, S.G.2    Hoh, R.3
  • 70
    • 33846029516 scopus 로고    scopus 로고
    • Increased polymorphism in the HR-1 gp41 env gene encoding the enfuvirtide (T-20) target in HIV-1 variants harboring multiple antiretroviral drug resistance mutations in the pol gene
    • Si-Mohamed A, Piketty C, Tisserand P, et al. Increased polymorphism in the HR-1 gp41 env gene encoding the enfuvirtide (T-20) target in HIV-1 variants harboring multiple antiretroviral drug resistance mutations in the pol gene. J Acquir Immune Defic Syndr 2007; 44: 1-5.
    • (2007) J Acquir Immune Defic Syndr , vol.44 , pp. 1-5
    • Si-Mohamed, A.1    Piketty, C.2    Tisserand, P.3
  • 71
    • 45549093277 scopus 로고    scopus 로고
    • Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor
    • He Y, Xiao Y, Song H, et al. Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem 2008; 283: 11126-34.
    • (2008) J Biol Chem , vol.283 , pp. 11126-11134
    • He, Y.1    Xiao, Y.2    Song, H.3
  • 72
    • 84863116316 scopus 로고    scopus 로고
    • Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor Sifuvirtide
    • Yao X, Chong H, Zhang C, et al. Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor Sifuvirtide. J Biol Chem 2012; 287: 6788-96.
    • (2012) J Biol Chem , vol.287 , pp. 6788-6796
    • Yao, X.1    Chong, H.2    Zhang, C.3
  • 73
    • 79952781156 scopus 로고    scopus 로고
    • In vitro selection and characterization of HIV-1 variants with increased resistance to sifuvirtide, a novel HIV-1 fusion inhibitor
    • Liu Z, Shan M, Li L, et al. In vitro selection and characterization of HIV-1 variants with increased resistance to sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem 2011; 286: 3277-87.
    • (2011) J Biol Chem , vol.286 , pp. 3277-3287
    • Liu, Z.1    Shan, M.2    Li, L.3
  • 74
    • 1642494594 scopus 로고    scopus 로고
    • Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level
    • Veiga S, Henriques S, Santos NC, Castanho M. Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level. Biochem J 2004; 377: 107-10.
    • (2004) Biochem J , vol.377 , pp. 107-110
    • Veiga, S.1    Henriques, S.2    Santos, N.C.3    Castanho, M.4
  • 75
    • 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 HG, Loura LM, Santos NC, Castanho MA. 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: 6215-23.
    • (2008) J Am Chem Soc , vol.130 , pp. 6215-6223
    • Franquelim, H.G.1    Loura, L.M.2    Santos, N.C.3    Castanho, M.A.4
  • 76
    • 77952551415 scopus 로고    scopus 로고
    • Unravelling the molecular basis of the selectivity of the HIV-1 fusion inhibitor sifuvirtide towards phosphatidylcholine-rich rigid membranes
    • Franquelim HG, Veiga AS, Weissmuller G, Santos NC, Castanho MA. Unravelling the molecular basis of the selectivity of the HIV-1 fusion inhibitor sifuvirtide towards phosphatidylcholine-rich rigid membranes. Biochim Biophys Acta 2010; 1798: 1234-43.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1234-1243
    • Franquelim, H.G.1    Veiga, A.S.2    Weissmuller, G.3    Santos, N.C.4    Castanho, M.A.5
  • 77
    • 78650172669 scopus 로고    scopus 로고
    • The role of blood cell membrane lipids on the mode of action of HIV-1 fusion inhibitor sifuvirtide
    • Matos PM, Freitas T, Castanho MA, Santos NC. The role of blood cell membrane lipids on the mode of action of HIV-1 fusion inhibitor sifuvirtide. Biochem Biophys Res Commun 2010; 403: 270-4.
    • (2010) Biochem Biophys Res Commun , vol.403 , pp. 270-274
    • Matos, P.M.1    Freitas, T.2    Castanho, M.A.3    Santos, N.C.4
  • 78
    • 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, et al. 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: 6349-58.
    • (2008) J Virol , vol.82 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3
  • 79
    • 84862001877 scopus 로고    scopus 로고
    • Discovery of critical residues for viral entry and inhibition through structural insight of HIV-1 fusion inhibitor CP621-652
    • Chong H, Yao X, Qiu Z, et al. Discovery of critical residues for viral entry and inhibition through structural insight of HIV-1 fusion inhibitor CP621-652. J Biol Chem 2012; 287:20281-9.
    • (2012) J Biol Chem , vol.287 , pp. 20281-20289
    • Chong, H.1    Yao, X.2    Qiu, Z.3
  • 80
    • 55849137299 scopus 로고    scopus 로고
    • Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strains
    • He Y, Cheng J, Lu H, et al. Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strains. Proc Natl Acad Sci USA 2008; 105: 16332-7.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16332-16337
    • He, Y.1    Cheng, J.2    Lu, H.3
  • 81
    • 84864545376 scopus 로고    scopus 로고
    • Structural basis of potent and broad HIV-1 fusion inhibitor CP32M
    • Yao X, Chong H, Zhang C, et al. Structural basis of potent and broad HIV-1 fusion inhibitor CP32M. J Biol Chem 2012; 287: 16618-29.
    • (2012) J Biol Chem , vol.287 , pp. 16618-16629
    • Yao, X.1    Chong, H.2    Zhang, C.3
  • 82
    • 42149132659 scopus 로고    scopus 로고
    • T-20 and T-1249 HIV fusion inhibitors' structure and conformation in solution: A molecular dynamics study
    • Martins Do Canto AM, Palace Carvalho AJ, Prates Ramalho JP, Loura LM. T-20 and T-1249 HIV fusion inhibitors' structure and conformation in solution: a molecular dynamics study. J Pept Sci 2008; 14: 442-7.
    • (2008) J Pept Sci , vol.14 , pp. 442-447
    • Martins Do Canto, A.M.1    Palace Carvalho, A.J.2    Prates Ramalho, J.P.3    Loura, L.M.4
  • 83
    • 73849105973 scopus 로고    scopus 로고
    • Long-lasting enfuvirtide carrier pentasaccharide conjugates with potent anti-human immunodeficiency virus type 1 activity
    • Huet T, Kerbarh O, Schols D, et al. Long-lasting enfuvirtide carrier pentasaccharide conjugates with potent anti-human immunodeficiency virus type 1 activity. Antimicrob Agents Chemother 2010; 54: 134-42.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 134-142
    • Huet, T.1    Kerbarh, O.2    Schols, D.3
  • 84
    • 57749122064 scopus 로고    scopus 로고
    • Albumin-conjugated C34 peptide HIV-1 fusion inhibitor: Equipotent to C34 and T-20 in vitro with sustained activity in SCID-hu Thy/Liv mice
    • Stoddart CA, Nault G, Galkina SA, et al. Albumin-conjugated C34 peptide HIV-1 fusion inhibitor: equipotent to C34 and T-20 in vitro with sustained activity in SCID-hu Thy/Liv mice. J Biol Chem 2008; 283: 34045-52.
    • (2008) J Biol Chem , vol.283 , pp. 34045-34052
    • Stoddart, C.A.1    Nault, G.2    Galkina, S.A.3
  • 85
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert DM, Malashkevich VN, Hong LH, Carr PA, Kim PS. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 1999; 99: 103-15.
    • (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
  • 86
    • 34547854349 scopus 로고    scopus 로고
    • Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus
    • Dwyer JJ, Wilson KL, Davison DK, et al. Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus. Proc Natl Acad Sci USA 2007; 104: 12772-7.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12772-12777
    • Dwyer, J.J.1    Wilson, K.L.2    Davison, D.K.3
  • 87
    • 80055013474 scopus 로고    scopus 로고
    • Resistance of Human Immunodeficiency Virus Type 1 to a Third-Generation Fusion Inhibitor Requires Multiple Mutations in gp41 and Is Accompanied by a Dramatic Loss of gp41 Function
    • Eggink D, Bontjer I, Langedijk JP, Berkhout B, Sanders RW. Resistance of Human Immunodeficiency Virus Type 1 to a Third-Generation Fusion Inhibitor Requires Multiple Mutations in gp41 and Is Accompanied by a Dramatic Loss of gp41 Function. J Virol 2011; 85: 10785-97.
    • (2011) J Virol , vol.85 , pp. 10785-10797
    • Eggink, D.1    Bontjer, I.2    Langedijk, J.P.3    Berkhout, B.4    Sanders, R.W.5
  • 88
    • 59649099932 scopus 로고    scopus 로고
    • Electrostatically constrained alpha-helical peptide inhibits replication of HIV-1 resistant to enfuvirtide
    • Nishikawa H, Nakamura S, Kodama E, et al. Electrostatically constrained alpha-helical peptide inhibits replication of HIV-1 resistant to enfuvirtide. Int J Biochem Cell Biol 2009; 41: 891-9.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 891-899
    • Nishikawa, H.1    Nakamura, S.2    Kodama, E.3
  • 89
    • 0037119022 scopus 로고    scopus 로고
    • Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells
    • Otaka A, Nakamura M, Nameki D, et al. Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells. Angew Chem Int Ed Engl 2002; 41: 2937-40.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 2937-2940
    • Otaka, A.1    Nakamura, M.2    Nameki, D.3
  • 90
    • 62949102876 scopus 로고    scopus 로고
    • SC29EK, a peptide fusion inhibitor with enhanced alpha-helicity, inhibits replication of human immunodeficiency virus type 1 mutants resistant to enfuvirtide
    • Naito T, Izumi K, Kodama E, et al. SC29EK, a peptide fusion inhibitor with enhanced alpha-helicity, inhibits replication of human immunodeficiency virus type 1 mutants resistant to enfuvirtide. Antimicrob Agents Chemother 2009; 53: 1013-8.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1013-1018
    • Naito, T.1    Izumi, K.2    Kodama, E.3
  • 91
    • 39149127330 scopus 로고    scopus 로고
    • Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity
    • Oishi S, Ito S, Nishikawa H, Watanabe K, et al. Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity. J Med Chem 2008; 51: 388-91.
    • (2008) J Med Chem , vol.51 , pp. 388-391
    • Oishi, S.1    Ito, S.2    Nishikawa, H.3    Watanabe, K.4
  • 92
    • 78649842313 scopus 로고    scopus 로고
    • Resistance profiles of novel electrostatically constrained HIV-1 fusion inhibitors
    • Shimura K, Nameki D, Kajiwara K, et al. Resistance profiles of novel electrostatically constrained HIV-1 fusion inhibitors. J Biol Chem 2010; 285: 39471-80.
    • (2010) J Biol Chem , vol.285 , pp. 39471-39480
    • Shimura, K.1    Nameki, D.2    Kajiwara, K.3
  • 93
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley CA, Louis JM, Ghirlando R, Clore GM. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J Biol Chem 2002; 277: 14238-45.
    • (2002) J Biol Chem , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 94
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert DM, Kim PS. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc Natl Acad Sci USA 2001; 98: 11187-92.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 95
    • 24644449058 scopus 로고    scopus 로고
    • Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection
    • Bianchi E, Finotto M, Ingallinella P, et al. Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection. Proc Natl Acad Sci USA 2005; 102: 12903-8.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12903-12908
    • Bianchi, E.1    Finotto, M.2    Ingallinella, P.3
  • 96
    • 0035800816 scopus 로고    scopus 로고
    • Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • Louis JM, Bewley CA, Clore GM. Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J Biol Chem 2001; 276: 29485-9.
    • (2001) J Biol Chem , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 97
    • 73849087593 scopus 로고    scopus 로고
    • An albumin-conjugated peptide exhibits potent anti-HIV activity and long in vivo half-life
    • Xie D, Yao C, Wang L, et al. An albumin-conjugated peptide exhibits potent anti-HIV activity and long in vivo half-life. Antimicrob Agents Chemother 2010; 54: 191-6.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 191-196
    • Xie, D.1    Yao, C.2    Wang, L.3
  • 98
    • 84863275072 scopus 로고    scopus 로고
    • Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acidmodified peptide fusion inhibitor
    • Chong H, Yao X, Zhang C, et al. Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acidmodified peptide fusion inhibitor. PLoS One 2012; 7: e32599.
    • (2012) PLoS One , vol.7
    • Chong, H.1    Yao, X.2    Zhang, C.3
  • 99
    • 65249085618 scopus 로고    scopus 로고
    • Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency
    • Ingallinella P, Bianchi E, Ladwa NA, et al. Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency. Proc Natl Acad Sci USA 2009; 106: 5801-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5801-5806
    • Ingallinella, P.1    Bianchi, E.2    Ladwa, N.A.3
  • 100
    • 67650507291 scopus 로고    scopus 로고
    • Enzymatic glycosylation of triazole-linked GlcNAc/Glc-peptides: Synthesis, stability and anti-HIV activity of triazole-linked HIV-1 gp41 glycopeptide C34 analogues
    • Huang W, Groothuys S, Heredia A, et al. Enzymatic glycosylation of triazole-linked GlcNAc/Glc-peptides: synthesis, stability and anti-HIV activity of triazole-linked HIV-1 gp41 glycopeptide C34 analogues. Chembiochem 2009; 10: 1234-42.
    • (2009) Chembiochem , vol.10 , pp. 1234-1242
    • Huang, W.1    Groothuys, S.2    Heredia, A.3
  • 102
    • 65549161084 scopus 로고    scopus 로고
    • Development and characterization of peptidic fusion inhibitors derived from HIV-1 gp41 with partial D-amino acid substitutions
    • Gaston F, Granados GC, Madurga S, et al. Development and characterization of peptidic fusion inhibitors derived from HIV-1 gp41 with partial D-amino acid substitutions. ChemMedChem 2009; 4: 570-81.
    • (2009) ChemMedChem , vol.4 , pp. 570-581
    • Gaston, F.1    Granados, G.C.2    Madurga, S.3
  • 103
    • 34147137981 scopus 로고    scopus 로고
    • Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide
    • Munch J, Standker L, Adermann K, et al. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. Cell 2007; 129: 263-75.
    • (2007) Cell , vol.129 , pp. 263-275
    • Munch, J.1    Standker, L.2    Adermann, K.3
  • 104
    • 78650646547 scopus 로고    scopus 로고
    • Short-term monotherapy in HIV-infected patients with a virus entry inhibitor against the gp41 fusion peptide
    • Forssmann WG, The YH, Stoll M, et al. Short-term monotherapy in HIV-infected patients with a virus entry inhibitor against the gp41 fusion peptide. Sci Transl Med 2010; 2: 63re3.
    • (2010) Sci Transl Med , vol.2
    • Forssmann, W.G.1    The, Y.H.2    Stoll, M.3
  • 105
    • 80051781764 scopus 로고    scopus 로고
    • Development of resistance to VIR-353 with cross-resistance to the natural HIV-1 entry virus inhibitory peptide (VIRIP)
    • Gonzalez E, Ballana E, Clotet B, Este JA. Development of resistance to VIR-353 with cross-resistance to the natural HIV-1 entry virus inhibitory peptide (VIRIP). AIDS 2011; 25: 1557-83.
    • (2011) AIDS , vol.25 , pp. 1557-1583
    • Gonzalez, E.1    Ballana, E.2    Clotet, B.3    Este, J.A.4
  • 106
    • 84858736184 scopus 로고    scopus 로고
    • Compensatory mutations rescue the virus replicative capacity of VIRIP-resistant HIV-1
    • Gonzalez-Ortega E, Ballana E, Badia R, Clotet B, Este JA. Compensatory mutations rescue the virus replicative capacity of VIRIP-resistant HIV-1. Antiviral Res 2011; 92: 479-83.
    • (2011) Antiviral Res , vol.92 , pp. 479-483
    • Gonzalez-Ortega, E.1    Ballana, E.2    Badia, R.3    Clotet, B.4    Este, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.