메뉴 건너뛰기




Volumn 16, Issue 33, 2010, Pages 3716-3728

Inhibition of HIV-1 by fusion inhibitors

Author keywords

Antiviral peptide; Enfuvirtide; Fusion inhibitors; Hiv; Resistance; T20; Virip; Virus entry

Indexed keywords

1 BENZOYL 4 [(4,7 DIMETHOXY 1H PYRROLO[2,3 C]PYRIDIN 3 YL)OXOACETYL]PIPERAZINE; 4 BENZOYL 1 [(4 METHOXY 1H PYRROLO[2,3 B]PYRIDIN 3 YL)OXOACETYL] 2 METHYLPIPERAZINE; 5 M 030; 5 M 038; 5 M 041; 8 [(4 AMINOBUTYL)(2 BENZIMIDAZOLYLMETHYL)AMINO] 1,2,3,4 TETRAHYDROQUINOLINE; C 34; C 52 D; C 52 L; CP 32 M; DP 107; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; INTEGRASE INHIBITOR; IQN 17; IQN 23; IZN 17; MARAVIROC; N 36; NB 2; NB 64; P 5; PBD 3 HRLBD; PC 1505; PEPTIDE DERIVATIVE; PF 68742; PROTEINASE INHIBITOR; RALTEGRAVIR; RC 100; RC 101; RC 106; RC 115; RC 116; RNA DIRECTED DNA POLYMERASE INHIBITOR; SC 22 EK; SC 29 EK; SC 34 EK; SC 35 EK; SIFUVIRTIDE; SJ 2176; T 20 EK; T 20 S 138 A; T 21; T 2410; T 2635; T 649; TIFUVIRTIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VICRIVIROC; VIR 164; VIR 165; VIR 175; VIR 353; VIR 449; VIR 576; VIRUS ENVELOPE PROTEIN; ALPHA 1 ANTITRYPSIN; DRUG CARRIER; PEPTIDE FRAGMENT; VIRIP PEPTIDE, HUMAN;

EID: 79955701366     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161210794079218     Document Type: Article
Times cited : (83)

References (175)
  • 1
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq E. Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV. Int J Antimicrob Agents 2009; 33: 307-20.
    • (2009) Int J Antimicrob Agents , vol.33 , pp. 307-320
    • de Clercq, E.1
  • 2
    • 77249134151 scopus 로고    scopus 로고
    • Twenty-six years of anti-HIV drug discovery: Where do we stand and where do we go?
    • Mehellou Y, De Clercq E. Twenty-six years of anti-HIV drug discovery: where do we stand and where do we go? J Med Chem 2010; 53: 521-38.
    • (2010) J Med Chem , vol.53 , pp. 521-538
    • Mehellou, Y.1    de Clercq, E.2
  • 3
    • 0037624182 scopus 로고    scopus 로고
    • Twenty years of therapy for HIV-1 infection
    • Pomerantz RJ, Horn DL. Twenty years of therapy for HIV-1 infection. Nat Med 2003; 9: 867-73.
    • (2003) Nat Med , vol.9 , pp. 867-873
    • Pomerantz, R.J.1    Horn, D.L.2
  • 4
    • 0036888142 scopus 로고    scopus 로고
    • Initial therapy of HIV infection
    • Gallant JE. Initial therapy of HIV infection. J Clin Virol 2002; 25: 317-33.
    • (2002) J Clin Virol , vol.25 , pp. 317-333
    • Gallant, J.E.1
  • 5
    • 5644267113 scopus 로고    scopus 로고
    • Inhibition of HIV-1 reverse transcription: Basic principles of drug action and resistance
    • Gotte M. Inhibition of HIV-1 reverse transcription: basic principles of drug action and resistance. Expert Rev Anti Infect Ther 2004; 2: 707-16.
    • (2004) Expert Rev Anti Infect Ther , vol.2 , pp. 707-716
    • Gotte, M.1
  • 6
    • 0028924567 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Esnouf R, Ren J, Ross C, Jones Y, Stammers D, Stuart D. Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors. Nat Struct Biol 1995; 2: 303-8.
    • (1995) Nat Struct Biol , vol.2 , pp. 303-308
    • Esnouf, R.1    Ren, J.2    Ross, C.3    Jones, Y.4    Stammers, D.5    Stuart, D.6
  • 7
    • 0035988450 scopus 로고    scopus 로고
    • Mechanisms of resistance to antiretroviral drugs--clinical implications
    • de Mendoza C, Gallego O, Soriano V. Mechanisms of resistance to antiretroviral drugs--clinical implications. AIDS Rev 2002; 4: 64-82.
    • (2002) AIDS Rev , vol.4 , pp. 64-82
    • de Mendoza, C.1    Gallego, O.2    Soriano, V.3
  • 8
    • 73549092917 scopus 로고    scopus 로고
    • Fifteen years of HIV Protease Inhibitors: Raising the barrier to resistance
    • Wensing AM, van Maarseveen NM, Nijhuis M. Fifteen years of HIV Protease Inhibitors: raising the barrier to resistance. Antiviral Res 2010; 85: 59-74.
    • (2010) Antiviral Res , vol.85 , pp. 59-74
    • Wensing, A.M.1    van Maarseveen, N.M.2    Nijhuis, M.3
  • 9
    • 66949136295 scopus 로고    scopus 로고
    • Raltegravir: A review of its use in the management of HIV infection in treatment-experienced patients
    • Croxtall JD, Keam SJ. Raltegravir: a review of its use in the management of HIV infection in treatment-experienced patients. Drugs 2009; 69: 1059-75.
    • (2009) Drugs , vol.69 , pp. 1059-1075
    • Croxtall, J.D.1    Keam, S.J.2
  • 11
    • 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
  • 12
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian M, Rey FA. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 2006; 4: 67-76.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0141703204 scopus 로고    scopus 로고
    • A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding
    • Lin PF, Blair W, Wang T, et al. A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding. Proc Natl Acad Sci USA 2003; 100: 11013-8.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11013-11018
    • Lin, P.F.1    Blair, W.2    Wang, T.3
  • 16
    • 72249103816 scopus 로고    scopus 로고
    • Inhibitors of human immunodeficiency virus type 1 (HIV-1) attachment. 5. An evolution from indole to azaindoles leading to the discovery of 1-(4- benzoylpiperazin-1-yl)-2-(4,7-dimethoxy-1H-pyrrolo[2,3- c]pyridin-3-yl)ethane-1,2-dione (BMS-488043), a drug candidate that demonstrates antiviral activity in HIV-1-infected subjects
    • Wang T, Yin Z, Zhang Z, et al. Inhibitors of human immunodeficiency virus type 1 (HIV-1) attachment. 5. An evolution from indole to azaindoles leading to the discovery of 1-(4- benzoylpiperazin-1-yl)-2-(4,7-dimethoxy-1H-pyrrolo[2,3- c]pyridin-3-yl)ethane-1,2-dione (BMS-488043), a drug candidate that demonstrates antiviral activity in HIV-1-infected subjects. J Med Chem 2009; 52: 7778-87.
    • (2009) J Med Chem , vol.52 , pp. 7778-7787
    • Wang, T.1    Yin, Z.2    Zhang, Z.3
  • 17
    • 33746571624 scopus 로고    scopus 로고
    • Susceptibility of pediatric HIV-1 isolates to recombinant CD4-IgG2 (PRO 542) and humanized mAb to the chemokine receptor CCR5 (PRO 140)
    • Shearer WT, DeVille JG, Samson PM, et al. Susceptibility of pediatric HIV-1 isolates to recombinant CD4-IgG2 (PRO 542) and humanized mAb to the chemokine receptor CCR5 (PRO 140). J Allergy Clin Immunol 2006; 118: 518-21.
    • (2006) J Allergy Clin Immunol , vol.118 , pp. 518-521
    • Shearer, W.T.1    Deville, J.G.2    Samson, P.M.3
  • 18
    • 0029062687 scopus 로고
    • Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates
    • Allaway GP, Davis-Bruno KL, Beaudry GA, et al. Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates. AIDS Res Hum Retroviruses 1995; 11: 533-9.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 533-539
    • Allaway, G.P.1    Davis-Bruno, K.L.2    Beaudry, G.A.3
  • 19
    • 1842415431 scopus 로고    scopus 로고
    • Coreceptor usage of primary human immunodeficiency virus type 1 isolates varies according to biological phenotype
    • Bjorndal A, Deng H, Jansson M, et al. Coreceptor usage of primary human immunodeficiency virus type 1 isolates varies according to biological phenotype. J Virol 1997; 71: 7478-87.
    • (1997) J Virol , vol.71 , pp. 7478-7487
    • Bjorndal, A.1    Deng, H.2    Jansson, M.3
  • 20
    • 10344266976 scopus 로고    scopus 로고
    • Primary, syncytiuminducing human immunodeficiency virus type 1 isolates are dualtropic and most can use either Lestr or CCR5 as coreceptors for virus entry
    • Simmons G, Wilkinson D, Reeves JD, et al. Primary, syncytiuminducing human immunodeficiency virus type 1 isolates are dualtropic and most can use either Lestr or CCR5 as coreceptors for virus entry. J Virol 1996; 70: 8355-60.
    • (1996) J Virol , vol.70 , pp. 8355-8360
    • Simmons, G.1    Wilkinson, D.2    Reeves, J.D.3
  • 21
    • 15844389650 scopus 로고    scopus 로고
    • HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5
    • Dragic T, Litwin V, Allaway GP, et al. HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5. Nature 1996; 381: 667-73.
    • (1996) Nature , vol.381 , pp. 667-673
    • Dragic, T.1    Litwin, V.2    Allaway, G.P.3
  • 22
    • 0030932188 scopus 로고    scopus 로고
    • Chemokine receptors as fusion cofactors for human immunodeficiency virus type 1 (HIV-1)
    • Doranz BJ, Berson JF, Rucker J, Doms RW. Chemokine receptors as fusion cofactors for human immunodeficiency virus type 1 (HIV-1). Immunol Res 1997; 16: 15-28.
    • (1997) Immunol Res , vol.16 , pp. 15-28
    • Doranz, B.J.1    Berson, J.F.2    Rucker, J.3    Doms, R.W.4
  • 23
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major coreceptor for primary isolates of HIV-1
    • Deng H, Liu R, Ellmeier W, et al. Identification of a major coreceptor for primary isolates of HIV-1. Nature 1996; 381: 661-6.
    • (1996) Nature , vol.381 , pp. 661-666
    • Deng, H.1    Liu, R.2    Ellmeier, W.3
  • 24
    • 0021720872 scopus 로고
    • T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
    • Klatzmann D, Champagne E, Chamaret S, et al. T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature 1984; 312: 767-8.
    • (1984) Nature , vol.312 , pp. 767-768
    • Klatzmann, D.1    Champagne, E.2    Chamaret, S.3
  • 25
    • 0035918220 scopus 로고    scopus 로고
    • N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization
    • Pollakis G, Kang S, Kliphuis A, Chalaby MI, Goudsmit J, Paxton WA. N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. J Biol Chem 2001; 276: 13433-41.
    • (2001) J Biol Chem , vol.276 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5    Paxton, W.A.6
  • 26
    • 30744447460 scopus 로고    scopus 로고
    • Efficacy of shortterm monotherapy with maraviroc, a new CCR5 antagonist, in patients infected with HIV-1
    • Fatkenheuer G, Pozniak AL, Johnson MA, et al. Efficacy of shortterm monotherapy with maraviroc, a new CCR5 antagonist, in patients infected with HIV-1. Nat Med 2005; 11: 1170-2.
    • (2005) Nat Med , vol.11 , pp. 1170-1172
    • Fatkenheuer, G.1    Pozniak, A.L.2    Johnson, M.A.3
  • 27
    • 28944454412 scopus 로고    scopus 로고
    • Discovery and characterization of vicriviroc (SCH 417690), a CCR5 antagonist with potent activity against human immunodeficiency virus type 1
    • Strizki JM, Tremblay C, Xu S, et al. Discovery and characterization of vicriviroc (SCH 417690), a CCR5 antagonist with potent activity against human immunodeficiency virus type 1. Antimicrob Agents Chemother 2005; 49: 4911-9.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4911-4919
    • Strizki, J.M.1    Tremblay, C.2    Xu, S.3
  • 28
    • 34250006524 scopus 로고    scopus 로고
    • Antiviral activity, pharmacokinetics and safety of vicriviroc, an oral CCR5 antagonist, during 14-day monotherapy in HIV-infected adults
    • Schurmann D, Fatkenheuer G, Reynes J, et al. Antiviral activity, pharmacokinetics and safety of vicriviroc, an oral CCR5 antagonist, during 14-day monotherapy in HIV-infected adults. AIDS 2007; 21: 1293-9.
    • (2007) AIDS , vol.21 , pp. 1293-1299
    • Schurmann, D.1    Fatkenheuer, G.2    Reynes, J.3
  • 29
    • 42949117215 scopus 로고    scopus 로고
    • Effect of low-dose ritonavir on the pharmacokinetics of the CXCR4 antagonist AMD070 in healthy volunteers
    • Cao YJ, Flexner CW, Dunaway S, et al. Effect of low-dose ritonavir on the pharmacokinetics of the CXCR4 antagonist AMD070 in healthy volunteers. Antimicrob Agents Chemother 2008; 52: 1630-4.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1630-1634
    • Cao, Y.J.1    Flexner, C.W.2    Dunaway, S.3
  • 30
    • 0034602736 scopus 로고    scopus 로고
    • The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions
    • Murakami T, Freed EO. The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proc Natl Acad Sci USA 2000; 97: 343-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 31
    • 0034467955 scopus 로고    scopus 로고
    • Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: Effects on glycoprotein incorporation and infectivity
    • Piller SC, Dubay JW, Derdeyn CA, Hunter E. Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycoprotein incorporation and infectivity. J Virol 2000; 74: 11717-23.
    • (2000) J Virol , vol.74 , pp. 11717-11723
    • Piller, S.C.1    Dubay, J.W.2    Derdeyn, C.A.3    Hunter, E.4
  • 32
    • 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 SA, 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 2001; 40: 12231-6.
    • (2001) Biochemistry , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 33
    • 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
  • 34
    • 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
  • 35
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: The HIV-1 paradigm
    • Melikyan GB. Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm. Retrovirology 2008; 5: 111.
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 36
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, Markosyan RM, Hemmati H, Delmedico MK, Lambert DM, Cohen FS. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J Cell Biol 2000; 151: 413-23.
    • (2000) J Cell Biol , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 37
    • 0035937255 scopus 로고    scopus 로고
    • Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein
    • Jelesarov I, Lu M. Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein. J Mol Biol 2001; 307: 637-56.
    • (2001) J Mol Biol , vol.307 , pp. 637-656
    • Jelesarov, I.1    Lu, M.2
  • 38
    • 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
  • 39
    • 10344234242 scopus 로고    scopus 로고
    • Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core
    • Xu Y, Lou Z, Liu Y, et al. Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core. J Biol Chem 2004; 279: 49414-9.
    • (2004) J Biol Chem , vol.279 , pp. 49414-49419
    • Xu, Y.1    Lou, Z.2    Liu, Y.3
  • 40
    • 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
  • 41
    • 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
  • 42
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009; 137: 433-44.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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
  • 46
    • 0042706375 scopus 로고    scopus 로고
    • HIV-1 resistance to the gp41-dependent fusion inhibitor C-34
    • Armand-Ugon M, Gutierrez A, Clotet B, Este JA. HIV-1 resistance to the gp41-dependent fusion inhibitor C-34. Antiviral Res 2003; 59: 137-42.
    • (2003) Antiviral Res , vol.59 , pp. 137-142
    • Armand-Ugon, M.1    Gutierrez, A.2    Clotet, B.3    Este, J.A.4
  • 48
    • 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
  • 49
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J Cell Biol 1998; 140: 315-23.
    • (1998) J Cell Biol , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 50
    • 77949412821 scopus 로고    scopus 로고
    • Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition
    • Martin N, Welsch S, Jolly C, Briggs JA, Vaux D, Sattentau QJ. Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition. J Virol 2010; 84: 3516-27.
    • (2010) J Virol , vol.84 , pp. 3516-3527
    • Martin, N.1    Welsch, S.2    Jolly, C.3    Briggs, J.A.4    Vaux, D.5    Sattentau, Q.J.6
  • 51
    • 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 HIVinfected 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 HIVinfected 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
  • 52
    • 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
  • 53
    • 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
  • 54
    • 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
  • 55
    • 35448948367 scopus 로고    scopus 로고
    • TORO: Ninety-six-week virologic and immunologic response and safety evaluation of enfuvirtide with an optimized background of antiretrovirals
    • Reynes J, Arasteh K, Clotet B, et al. TORO: ninety-six-week virologic and immunologic response and safety evaluation of enfuvirtide with an optimized background of antiretrovirals. AIDS Patient Care STDS 2007; 21: 533-43.
    • (2007) AIDS Patient Care STDS , vol.21 , pp. 533-543
    • Reynes, J.1    Arasteh, K.2    Clotet, B.3
  • 56
    • 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
  • 57
    • 0037877472 scopus 로고    scopus 로고
    • In vitro antiviral activity of T-1249 a second generation fusion ihibitor
    • Greenberg A, Davison D, Jin L, et al. In vitro antiviral activity of T-1249 a second generation fusion ihibitor. Antivir Ther 2002; 7: S14.
    • (2002) Antivir Ther , vol.7
    • Greenberg, A.1    Davison, D.2    Jin, L.3
  • 58
    • 19744363341 scopus 로고    scopus 로고
    • Rational design of highly potent HIV-1 fusion inhibitory proteins: Implication for developing antiviral therapeutics
    • Ni L, Gao GF, Tien P. Rational design of highly potent HIV-1 fusion inhibitory proteins: implication for developing antiviral therapeutics. Biochem Biophys Res Commun 2005; 332: 831-6.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 831-836
    • Ni, L.1    Gao, G.F.2    Tien, P.3
  • 59
    • 57649155175 scopus 로고    scopus 로고
    • Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors
    • Qi Z, Shi W, Xue N, Pan C, Jing W, Liu K, Jiang S. Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors. J Biol Chem 2008; 283: 30376-84.
    • (2008) J Biol Chem , vol.283 , pp. 30376-30384
    • Qi, Z.1    Shi, W.2    Xue, N.3    Pan, C.4    Jing, W.5    Liu, K.6    Jiang, S.7
  • 60
    • 34248155890 scopus 로고    scopus 로고
    • HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides
    • Liu S, Jing W, Cheung B, et al. HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides. J Biol Chem 2007; 282: 9612-20.
    • (2007) J Biol Chem , vol.282 , pp. 9612-9620
    • Liu, S.1    Jing, W.2    Cheung, B.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
    • 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
  • 63
    • 0037444053 scopus 로고    scopus 로고
    • Determining the relative efficacy of highly active antiretroviral therapy
    • Louie M, Hogan C, Di Mascio M, et al. Determining the relative efficacy of highly active antiretroviral therapy. J Infect Dis 2003; 187: 896-900.
    • (2003) J Infect Dis , vol.187 , pp. 896-900
    • Louie, M.1    Hogan, C.2    Di Mascio, M.3
  • 64
    • 0037539520 scopus 로고    scopus 로고
    • Enfuvirtide (T-20) and T- 1249 resistance: Observations from Phase II clinical trials of enfuvirtide in combination with oral antiretrovirals and a Phase I/II dose-ranging monotherapy trial of T-1249
    • [Greenberg A, Sista P, Miralles GD, et al. Enfuvirtide (T-20) and T- 1249 resistance: observations from Phase II clinical trials of enfuvirtide in combination with oral antiretrovirals and a Phase I/II dose-ranging monotherapy trial of T-1249 Antivir Ther 2002; 7: S140.
    • (2002) Antivir Ther , vol.7
    • Greenberg, A.1    Sista, P.2    Miralles, G.D.3
  • 65
    • 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
    • do Martins, C.A.M.1    Palace, C.A.J.2    Prates, R.J.P.3    Loura, L.M.4
  • 66
    • 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
  • 67
    • 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
  • 68
    • 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
  • 69
    • 0034693932 scopus 로고    scopus 로고
    • Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1
    • Jin BS, Ryu JR, Ahn K, Yu YG. Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 2000; 16: 1797-804.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1797-1804
    • Jin, B.S.1    Ryu, J.R.2    Ahn, K.3    Yu, Y.G.4
  • 70
    • 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
  • 71
    • 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
  • 72
    • 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
  • 73
    • 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
  • 74
    • 26044470938 scopus 로고    scopus 로고
    • Pharmacokinetics of sifuvirtide, a novel anti-HIV-1 peptide, in monkeys and its inhibitory concentration in vitro
    • Dai SJ, Dou GF, Qiang XH, et al. Pharmacokinetics of sifuvirtide, a novel anti-HIV-1 peptide, in monkeys and its inhibitory concentration in vitro. Acta Pharmacol Sin 2005; 26: 1274-80.
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 1274-1280
    • Dai, S.J.1    Dou, G.F.2    Qiang, X.H.3
  • 75
    • 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
  • 76
    • 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, 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
  • 77
    • 66349103418 scopus 로고    scopus 로고
    • Development of a novel fusion inhibitor against T-20-resistant HIV-1
    • Oishi S, Ito S, Nishikawa H, et al. Development of a novel fusion inhibitor against T-20-resistant HIV-1. Adv Exp Med Biol 2009; 611: 389-91.
    • (2009) Adv Exp Med Biol , vol.611 , pp. 389-391
    • Oishi, S.1    Ito, S.2    Nishikawa, H.3
  • 78
    • 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
  • 79
    • 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
  • 80
    • 72149087467 scopus 로고    scopus 로고
    • Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group
    • Kajiwara K, Watanabe K, Tokiwa R, et al. Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group. Bioorg Med Chem 2009; 17: 7964-70.
    • (2009) Bioorg Med Chem , vol.17 , pp. 7964-7970
    • Kajiwara, K.1    Watanabe, K.2    Tokiwa, R.3
  • 82
    • 0034697649 scopus 로고    scopus 로고
    • An All-Hydrocarbon Cross- Linking System for Enhancing the Helicity and Metabolic Stability of Peptides
    • Schafmeister CE, Po J, Verdine GL. An All-Hydrocarbon Cross- Linking System for Enhancing the Helicity and Metabolic Stability of Peptides. J Am Chem Soc 2000; 122: 5891-5892.
    • (2000) J Am Chem Soc , vol.122 , pp. 5891-5892
    • Schafmeister, C.E.1    Po, J.2    Verdine, G.L.3
  • 83
    • 4444291734 scopus 로고    scopus 로고
    • Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix
    • Walensky LD, Kung AL, Escher I, et al. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Science 2004; 305: 1466-70.
    • (2004) Science , vol.305 , pp. 1466-1470
    • Walensky, L.D.1    Kung, A.L.2    Escher, I.3
  • 84
    • 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
  • 85
    • 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
  • 86
    • 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
  • 87
    • 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
  • 88
    • 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
  • 89
    • 64149109197 scopus 로고    scopus 로고
    • Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20
    • Izumi K, Kodama E, Shimura K, et al. Design of peptide-based inhibitors for human immunodeficiency virus type 1 strains resistant to T-20. J Biol Chem 2009; 284: 4914-20.
    • (2009) J Biol Chem , vol.284 , pp. 4914-4920
    • Izumi, K.1    Kodama, E.2    Shimura, K.3
  • 90
    • 2942729771 scopus 로고    scopus 로고
    • Activity of alpha- and theta-defensins against primary isolates of HIV-1
    • Wang W, Owen SM, Rudolph DL, et al. Activity of alpha- and theta-defensins against primary isolates of HIV-1. J Immunol 2004; 173: 515-20.
    • (2004) J Immunol , vol.173 , pp. 515-520
    • Wang, W.1    Owen, S.M.2    Rudolph, D.L.3
  • 91
    • 9344221638 scopus 로고    scopus 로고
    • RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates
    • Owen SM, Rudolph DL, Wang W, et al. RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates. AIDS Res Hum Retroviruses 2004; 20: 1157-65.
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 1157-1165
    • Owen, S.M.1    Rudolph, D.L.2    Wang, W.3
  • 92
    • 50949120543 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins
    • Wang G, Watson KM, Buckheit RW, Jr. Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. Antimicrob Agents Chemother 2008; 52: 3438-40.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 3438-3440
    • Wang, G.1    Watson, K.M.2    Buckheit Jr., R.W.3
  • 93
    • 37249041669 scopus 로고    scopus 로고
    • Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion
    • Plaza A, Gustchina E, Baker HL, Kelly M, Bewley CA. Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion. J Nat Prod 2007; 70: 1753-60.
    • (2007) J Nat Prod , vol.70 , pp. 1753-1760
    • Plaza, A.1    Gustchina, E.2    Baker, H.L.3    Kelly, M.4    Bewley, C.A.5
  • 94
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root MJ, Kay MS, Kim PS. Protein design of an HIV-1 entry inhibitor. Science 2001; 291: 884-8.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 95
    • 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
  • 96
    • 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
  • 97
    • 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
  • 98
    • 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
  • 99
    • 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
  • 100
    • 20744450475 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency
    • Stoller JK, Aboussouan LS. Alpha1-antitrypsin deficiency. Lancet 2005; 365: 2225-36.
    • (2005) Lancet , vol.365 , pp. 2225-2236
    • Stoller, J.K.1    Aboussouan, L.S.2
  • 101
    • 31944450675 scopus 로고    scopus 로고
    • Pharmacokinetics of enfuvirtide in patients treated in typical routine clinical settings
    • Stocker H, Kloft C, Plock N, et al. Pharmacokinetics of enfuvirtide in patients treated in typical routine clinical settings. Antimicrob Agents Chemother 2006; 50: 667-73.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 667-673
    • Stocker, H.1    Kloft, C.2    Plock, N.3
  • 102
    • 0036335809 scopus 로고    scopus 로고
    • Pharmacokinetics of plasma enfuvirtide after subcutaneous administration to patients with human immunodeficiency virus: Inverse Gaussian density absorption and 2-compartment disposition
    • Zhang X, Nieforth K, Lang JM, et al. Pharmacokinetics of plasma enfuvirtide after subcutaneous administration to patients with human immunodeficiency virus: Inverse Gaussian density absorption and 2-compartment disposition. Clin Pharmacol Ther 2002; 72: 10-9.
    • (2002) Clin Pharmacol Ther , vol.72 , pp. 10-19
    • Zhang, X.1    Nieforth, K.2    Lang, J.M.3
  • 103
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese FM, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov Today 2005; 10: 1451-8.
    • (2005) Drug Discov Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 104
    • 27744454297 scopus 로고    scopus 로고
    • Pharmacologic modifications of hormones to improve their therapeutic potential for diabetes management
    • Garber AJ. Pharmacologic modifications of hormones to improve their therapeutic potential for diabetes management. Diabetes Obes Metab 2005; 7: 666-74.
    • (2005) Diabetes Obes Metab , vol.7 , pp. 666-674
    • Garber, A.J.1
  • 105
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins
    • Sinclair AM, Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci 2005; 94: 1626-35.
    • (2005) J Pharm Sci , vol.94 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 106
    • 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
  • 107
    • 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
  • 108
    • 34147124231 scopus 로고    scopus 로고
    • Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor
    • Deng Y, Zheng Q, Ketas TJ, Moore JP, Lu M. Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor. Biochemistry 2007; 46: 4360-9.
    • (2007) Biochemistry , vol.46 , pp. 4360-4369
    • Deng, Y.1    Zheng, Q.2    Ketas, T.J.3    Moore, J.P.4    Lu, M.5
  • 109
    • 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
  • 110
    • 34548481743 scopus 로고    scopus 로고
    • Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry
    • He Y, Liu S, Jing W, et al. Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry. J Biol Chem 2007; 282: 25631-9.
    • (2007) J Biol Chem , vol.282 , pp. 25631-25639
    • He, Y.1    Liu, S.2    Jing, W.3
  • 111
    • 71249111434 scopus 로고    scopus 로고
    • ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation
    • Wang H, Qi Z, Guo A, et al. ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation. Antimicrob Agents Chemother 2009; 53: 4987-98.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 4987-4998
    • Wang, H.1    Qi, Z.2    Guo, A.3
  • 112
    • 33749032790 scopus 로고    scopus 로고
    • Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion
    • G, Rits-Volloch S, Zhang XQ, Schooley RT, Chen B, Harrison SC. Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion. Proc Natl Acad Sci USA 2006; 103: 13938-43.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13938-13943
  • 113
    • 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, et al. Design, synthesis, and biological evaluation of N-carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41. J Med Chem 2008; 51: 7843-54.
    • (2008) J Med Chem , vol.51 , pp. 7843-7854
    • Liu, K.1    Lu, H.2    Hou, L.3
  • 114
    • 7244253012 scopus 로고    scopus 로고
    • N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion
    • Jiang S, Lu H, Liu S, Zhao Q, He Y, Debnath AK. N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion. Antimicrob Agents Chemother 2004; 48: 4349-59.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4349-4359
    • Jiang, S.1    Lu, H.2    Liu, S.3    Zhao, Q.4    He, Y.5    Debnath, A.K.6
  • 115
    • 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 AR, Tala SR, Lu H, et al. Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo- 3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors. J Med Chem 2009; 52: 7631-9.
    • (2009) J Med Chem , vol.52 , pp. 7631-7639
    • Katritzky, A.R.1    Tala, S.R.2    Lu, H.3
  • 116
    • 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 EJ, Leaman DP, Pawa N, et al. 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: 7288-99.
    • (2010) J Virol , vol.84 , pp. 7288-7299
    • Murray, E.J.1    Leaman, D.P.2    Pawa, N.3
  • 117
    • 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
  • 118
    • 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
  • 119
    • 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
  • 120
    • 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
  • 121
    • 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
  • 122
    • 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
  • 123
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn CA, Decker JM, Sfakianos JN, et al. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J Virol 2000; 74: 8358-67.
    • (2000) J Virol , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3
  • 124
    • 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
  • 125
    • 47749156074 scopus 로고    scopus 로고
    • Mechanistic studies of a T20-dependent human immunodeficiency virus type 1 variant
    • Baldwin C, Berkhout B. Mechanistic studies of a T20-dependent human immunodeficiency virus type 1 variant. J Virol 2008; 82: 7735-40.
    • (2008) J Virol , vol.82 , pp. 7735-7740
    • Baldwin, C.1    Berkhout, B.2
  • 126
    • 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
  • 127
    • 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
  • 128
    • 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
  • 129
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt EJ, Durnin JP, Kabat D. Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J Virol 2005; 79: 4347-56.
    • (2005) J Virol , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 130
    • 3042799046 scopus 로고    scopus 로고
    • Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20)
    • Lu J, Sista P, Giguel F, Greenberg M, Kuritzkes DR. Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20). J Virol 2004; 78: 4628-37.
    • (2004) J Virol , vol.78 , pp. 4628-4637
    • Lu, J.1    Sista, P.2    Giguel, F.3    Greenberg, M.4    Kuritzkes, D.R.5
  • 131
    • 11844282741 scopus 로고    scopus 로고
    • Resistance and replicative capacity of HIV-1 strains selected in vivo by long-term enfuvirtide treatment
    • Menzo S, Castagna A, Monachetti A, et al. Resistance and replicative capacity of HIV-1 strains selected in vivo by long-term enfuvirtide treatment. New Microbiol 2004; 27: 51-61.
    • (2004) New Microbiol , vol.27 , pp. 51-61
    • Menzo, S.1    Castagna, A.2    Monachetti, A.3
  • 132
    • 0038078724 scopus 로고    scopus 로고
    • Uncommon mutations at residue positions critical for enfuvirtide (T-20) resistance in enfuvirtide-naive patients infected with subtype B and non-B HIV- 1 strains
    • Roman F, Gonzalez D, Lambert C, et al. Uncommon mutations at residue positions critical for enfuvirtide (T-20) resistance in enfuvirtide-naive patients infected with subtype B and non-B HIV- 1 strains. J Acquir Immune Defic Syndr 2003; 33: 134-9.
    • (2003) J Acquir Immune Defic Syndr , vol.33 , pp. 134-139
    • Roman, F.1    Gonzalez, D.2    Lambert, C.3
  • 133
    • 0037223692 scopus 로고    scopus 로고
    • Baseline susceptibility of primary human immunodeficiency virus type 1 to entry inhibitors
    • Labrosse B, Labernardiere JL, Dam E, et al. Baseline susceptibility of primary human immunodeficiency virus type 1 to entry inhibitors. J Virol 2003; 77: 1610-3.
    • (2003) J Virol , vol.77 , pp. 1610-1613
    • Labrosse, B.1    Labernardiere, J.L.2    Dam, E.3
  • 134
    • 33846081762 scopus 로고    scopus 로고
    • Susceptibility of HIV-1 non-B subtypes and recombinant variants to Enfuvirtide
    • Holguin A, Faudon JL, Labernardiere JL, Soriano V. Susceptibility of HIV-1 non-B subtypes and recombinant variants to Enfuvirtide. J Clin Virol 2007; 38: 176-80.
    • (2007) J Clin Virol , vol.38 , pp. 176-180
    • Holguin, A.1    Faudon, J.L.2    Labernardiere, J.L.3    Soriano, V.4
  • 135
    • 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
  • 136
    • 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
  • 137
    • 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
  • 138
    • 0035141001 scopus 로고    scopus 로고
    • Implications of antiretroviral resistance on viral fitness
    • Nijhuis M, Deeks S, Boucher C. Implications of antiretroviral resistance on viral fitness. Curr Opin Infect Dis 2001; 14: 23-8.
    • (2001) Curr Opin Infect Dis , vol.14 , pp. 23-28
    • Nijhuis, M.1    Deeks, S.2    Boucher, C.3
  • 139
    • 0242354002 scopus 로고    scopus 로고
    • Molecular impact of the M184V mutation in human immunodeficiency virus type 1 reverse transcriptase
    • Diallo K, Gotte M, Wainberg MA. Molecular impact of the M184V mutation in human immunodeficiency virus type 1 reverse transcriptase. Antimicrob Agents Chemother 2003; 47: 3377-83.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3377-3383
    • Diallo, K.1    Gotte, M.2    Wainberg, M.A.3
  • 140
    • 0030512725 scopus 로고    scopus 로고
    • Effectiveness of 3TC in HIV clinical trials may be due in part to the M184V substitution in 3TC-resistant HIV-1 reverse transcriptase
    • Wainberg MA, Hsu M, Gu Z, Borkow G, Parniak MA. Effectiveness of 3TC in HIV clinical trials may be due in part to the M184V substitution in 3TC-resistant HIV-1 reverse transcriptase. AIDS 1996; 10 (Suppl 5): S3-10.
    • (1996) AIDS , vol.10 , Issue.SUPPL. 5
    • Wainberg, M.A.1    Hsu, M.2    Gu, Z.3    Borkow, G.4    Parniak, M.A.5
  • 141
    • 0032869255 scopus 로고    scopus 로고
    • HIV-1 evolution under pressure of protease inhibitors: Climbing the stairs of viral fitness
    • Berkhout B. HIV-1 evolution under pressure of protease inhibitors: climbing the stairs of viral fitness. J Biomed Sci 1999; 6: 298-305.
    • (1999) J Biomed Sci , vol.6 , pp. 298-305
    • Berkhout, B.1
  • 142
    • 0026867263 scopus 로고
    • A survey of patient preference for insulin jet injectors versus needle and syringe
    • Denne JR, Andrews KL, Lees DV, Mook W. A survey of patient preference for insulin jet injectors versus needle and syringe. Diabetes Educ 1992; 18: 223-7.
    • (1992) Diabetes Educ , vol.18 , pp. 223-227
    • Denne, J.R.1    Andrews, K.L.2    Lees, D.V.3    Mook, W.4
  • 143
    • 0025153296 scopus 로고
    • Absorption of peptides and proteins from the respiratory tract and the potential for development of locally administered vaccine
    • O'Hagan DT, Illum L. Absorption of peptides and proteins from the respiratory tract and the potential for development of locally administered vaccine. Crit Rev Ther Drug Carrier Syst 1990; 7: 35-97.
    • (1990) Crit Rev Ther Drug Carrier Syst , vol.7 , pp. 35-97
    • O'Hagan, D.T.1    Illum, L.2
  • 144
    • 70349556669 scopus 로고    scopus 로고
    • Nasal delivery of high molecular weight drugs
    • Ozsoy Y, Gungor S, Cevher E. Nasal delivery of high molecular weight drugs. Molecules 2009; 14: 3754-79.
    • (2009) Molecules , vol.14 , pp. 3754-3779
    • Ozsoy, Y.1    Gungor, S.2    Cevher, E.3
  • 145
    • 34547899919 scopus 로고    scopus 로고
    • Solid lipid nanoparticles as a drug delivery system for peptides and proteins
    • Almeida AJ, Souto E. Solid lipid nanoparticles as a drug delivery system for peptides and proteins. Adv Drug Deliv Rev 2007; 59: 478-90.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 478-490
    • Almeida, A.J.1    Souto, E.2
  • 146
    • 0035067784 scopus 로고    scopus 로고
    • Evaluation of gelatin microspheres for nasal and intramuscular administrations of salmon calcitonin
    • Morimoto K, Katsumata H, Yabuta T, et al. Evaluation of gelatin microspheres for nasal and intramuscular administrations of salmon calcitonin. Eur J Pharm Sci 2001; 13: 179-85.
    • (2001) Eur J Pharm Sci , vol.13 , pp. 179-185
    • Morimoto, K.1    Katsumata, H.2    Yabuta, T.3
  • 147
    • 18844392068 scopus 로고    scopus 로고
    • Effect of chitosan on the intranasal absorption of salmon calcitonin in sheep
    • Hinchcliffe M, Jabbal-Gill I, Smith A. Effect of chitosan on the intranasal absorption of salmon calcitonin in sheep. J Pharm Pharmacol 2005; 57: 681-7.
    • (2005) J Pharm Pharmacol , vol.57 , pp. 681-687
    • Hinchcliffe, M.1    Jabbal-Gill, I.2    Smith, A.3
  • 148
    • 0035120510 scopus 로고    scopus 로고
    • Membraneanchored peptide inhibits human immunodeficiency virus entry
    • Hildinger M, Dittmar MT, Schult-Dietrich P, et al. Membraneanchored peptide inhibits human immunodeficiency virus entry. J Virol 2001; 75: 3038-42.
    • (2001) J Virol , vol.75 , pp. 3038-3042
    • Hildinger, M.1    Dittmar, M.T.2    Schult-Dietrich, P.3
  • 149
    • 9144270207 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 entry in cells expressing gp41-derived peptides
    • Egelhofer M, Brandenburg G, Martinius H, et al. Inhibition of human immunodeficiency virus type 1 entry in cells expressing gp41-derived peptides. J Virol 2004; 78: 568-75.
    • (2004) J Virol , vol.78 , pp. 568-575
    • Egelhofer, M.1    Brandenburg, G.2    Martinius, H.3
  • 150
    • 50049133876 scopus 로고    scopus 로고
    • Efficient entry inhibition of human and nonhuman primate immunodeficiency virus by cell surface-expressed gp41-derived peptides
    • Zahn RC, Hermann FG, Kim EY, et al. Efficient entry inhibition of human and nonhuman primate immunodeficiency virus by cell surface-expressed gp41-derived peptides. Gene Ther 2008; 15: 1210-22.
    • (2008) Gene Ther , vol.15 , pp. 1210-1222
    • Zahn, R.C.1    Hermann, F.G.2    Kim, E.Y.3
  • 151
    • 33750813866 scopus 로고    scopus 로고
    • Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41
    • Gustchina E, Louis JM, Bewley CA, Clore GM. Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41. J Mol Biol 2006; 364: 283-9.
    • (2006) J Mol Biol , vol.364 , pp. 283-289
    • Gustchina, E.1    Louis, J.M.2    Bewley, C.A.3    Clore, G.M.4
  • 152
    • 63149114263 scopus 로고    scopus 로고
    • Synergistic efficacy of combination of enfuvirtide and sifuvirtide, the first- and next-generation HIVfusion inhibitors
    • Pan C, Lu H, Qi Z, Jiang S. Synergistic efficacy of combination of enfuvirtide and sifuvirtide, the first- and next-generation HIVfusion inhibitors. AIDS 2009; 23: 639-41.
    • (2009) AIDS , vol.23 , pp. 639-641
    • Pan, C.1    Lu, H.2    Qi, Z.3    Jiang, S.4
  • 153
    • 0036232981 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro
    • Tremblay CL, Giguel F, Kollmann C, et al. Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro. Antimicrob Agents Chemother 2002; 46: 1336-9.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1336-1339
    • Tremblay, C.L.1    Giguel, F.2    Kollmann, C.3
  • 155
    • 58149116577 scopus 로고    scopus 로고
    • Short communication: In vitro synergy between peptides or neutralizing antibodies targeting the N- and C-terminal heptad repeats of HIV Type 1 gp41
    • Hrin R, Montgomery DL, Wang F, et al. Short communication: In vitro synergy between peptides or neutralizing antibodies targeting the N- and C-terminal heptad repeats of HIV Type 1 gp41. AIDS Res Hum Retroviruses 2008; 24: 1537-44.
    • (2008) AIDS Res Hum Retroviruses , vol.24 , pp. 1537-1544
    • Hrin, R.1    Montgomery, D.L.2    Wang, F.3
  • 156
    • 67749147470 scopus 로고    scopus 로고
    • Combinations of the first and next generations of human immunodeficiency virus (HIV) fusion inhibitors exhibit a highly potent synergistic effect against enfuvirtide- sensitive and -resistant HIV type 1 strains
    • Pan C, Cai L, Lu H, Qi Z, Jiang S. Combinations of the first and next generations of human immunodeficiency virus (HIV) fusion inhibitors exhibit a highly potent synergistic effect against enfuvirtide- sensitive and -resistant HIV type 1 strains. J Virol 2009; 83: 7862-72.
    • (2009) J Virol , vol.83 , pp. 7862-7872
    • Pan, C.1    Cai, L.2    Lu, H.3    Qi, Z.4    Jiang, S.5
  • 157
    • 0035313589 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion
    • Nagashima KA, Thompson DA, Rosenfield SI, Maddon PJ, Dragic T, Olson WC. Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion. J Infect Dis 2001; 183: 1121-5.
    • (2001) J Infect Dis , vol.183 , pp. 1121-1125
    • Nagashima, K.A.1    Thompson, D.A.2    Rosenfield, S.I.3    Maddon, P.J.4    Dragic, T.5    Olson, W.C.6
  • 158
    • 44449125062 scopus 로고    scopus 로고
    • Potent synergistic antihuman immunodeficiency virus (HIV) effects using combinations of the CCR5 inhibitor aplaviroc with other anti-HIV drugs
    • Nakata H, Steinberg SM, Koh Y, et al. Potent synergistic antihuman immunodeficiency virus (HIV) effects using combinations of the CCR5 inhibitor aplaviroc with other anti-HIV drugs. Antimicrob Agents Chemother 2008; 52: 2111-9.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 2111-2119
    • Nakata, H.1    Steinberg, S.M.2    Koh, Y.3
  • 159
    • 44349096289 scopus 로고    scopus 로고
    • Closing two doors of viral entry: Intramolecular combination of a coreceptor- and fusion inhibitor of HIV-1
    • Kopetzki E, Jekle A, Ji C, et al. Closing two doors of viral entry: intramolecular combination of a coreceptor- and fusion inhibitor of HIV-1. Virol J 2008; 5: 56.
    • (2008) Virol J , vol.5 , pp. 56
    • Kopetzki, E.1    Jekle, A.2    Ji, C.3
  • 160
    • 48749094276 scopus 로고    scopus 로고
    • Tropism-independent protection of macaques against vaginal transmission of three SHIVs by the HIV-1 fusion inhibitor T-1249
    • Veazey RS, Ketas TA, Klasse PJ, et al. Tropism-independent protection of macaques against vaginal transmission of three SHIVs by the HIV-1 fusion inhibitor T-1249. Proc Natl Acad Sci USA 2008; 105: 10531-6.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10531-10536
    • Veazey, R.S.1    Ketas, T.A.2    Klasse, P.J.3
  • 161
    • 27744571425 scopus 로고    scopus 로고
    • Protection of macaques from vaginal SHIV challenge by vaginally delivered inhibitors of virus-cell fusion
    • Veazey RS, Klasse PJ, Schader SM, et al. Protection of macaques from vaginal SHIV challenge by vaginally delivered inhibitors of virus-cell fusion. Nature 2005; 438: 99-102.
    • (2005) Nature , vol.438 , pp. 99-102
    • Veazey, R.S.1    Klasse, P.J.2    Schader, S.M.3
  • 162
    • 0042368611 scopus 로고    scopus 로고
    • Cyanovirin-N gel as a topical microbicide prevents rectal transmission of SHIV89.6P in macaques
    • Tsai CC, Emau P, Jiang Y, et al. Cyanovirin-N gel as a topical microbicide prevents rectal transmission of SHIV89.6P in macaques. AIDS Res Hum Retroviruses 2003; 19: 535-41.
    • (2003) AIDS Res Hum Retroviruses , vol.19 , pp. 535-541
    • Tsai, C.C.1    Emau, P.2    Jiang, Y.3
  • 163
    • 33749532310 scopus 로고    scopus 로고
    • Engineered vaginal lactobacillus strain for mucosal delivery of the human immunodeficiency virus inhibitor cyanovirin-N
    • Liu X, Lagenaur LA, Simpson DA, et al. Engineered vaginal lactobacillus strain for mucosal delivery of the human immunodeficiency virus inhibitor cyanovirin-N. Antimicrob Agents Chemother 2006; 50: 3250-9.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 3250-3259
    • Liu, X.1    Lagenaur, L.A.2    Simpson, D.A.3
  • 164
    • 65549099593 scopus 로고    scopus 로고
    • Scaleable manufacture of HIV-1 entry inhibitor griffithsin and validation of its safety and efficacy as a topical microbicide component
    • O'Keefe BR, Vojdani F, Buffa V, et al. Scaleable manufacture of HIV-1 entry inhibitor griffithsin and validation of its safety and efficacy as a topical microbicide component. Proc Natl Acad Sci USA 2009; 106: 6099-104.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6099-6104
    • O'Keefe, B.R.1    Vojdani, F.2    Buffa, V.3
  • 165
    • 0027757544 scopus 로고
    • Structure, function, and regulation of the enzyme activity of prostate-specific antigen
    • Lilja H. Structure, function, and regulation of the enzyme activity of prostate-specific antigen. World J Urol 1993; 11: 188-91.
    • (1993) World J Urol , vol.11 , pp. 188-191
    • Lilja, H.1
  • 166
    • 12144287276 scopus 로고    scopus 로고
    • Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: Implications for virus fusogenic mechanism and identification of fusion inhibitors
    • Liu S, Xiao G, Chen Y, et al. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet 2004; 363: 938-47.
    • (2004) Lancet , vol.363 , pp. 938-947
    • Liu, S.1    Xiao, G.2    Chen, Y.3
  • 167
    • 33744460794 scopus 로고    scopus 로고
    • Inhibition of human coronavirus NL63 infection at early stages of the replication cycle
    • Pyrc K, Bosch BJ, Berkhout B, et al. Inhibition of human coronavirus NL63 infection at early stages of the replication cycle. Antimicrob Agents Chemother 2006; 50: 2000-8.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2000-2008
    • Pyrc, K.1    Bosch, B.J.2    Berkhout, B.3
  • 168
    • 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
  • 169
    • 34648830863 scopus 로고    scopus 로고
    • Molecular determinants of antiviral potency of paramyxovirus entry inhibitors
    • Porotto M, Carta P, Deng Y, et al. Molecular determinants of antiviral potency of paramyxovirus entry inhibitors. J Virol 2007; 81: 10567-74.
    • (2007) J Virol , vol.81 , pp. 10567-10574
    • Porotto, M.1    Carta, P.2    Deng, Y.3
  • 170
    • 27744533984 scopus 로고    scopus 로고
    • Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion
    • Zhu J, Jiang X, Liu Y, Tien P, Gao GF. Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion. J Mol Biol 2005; 354: 601-13.
    • (2005) J Mol Biol , vol.354 , pp. 601-613
    • Zhu, J.1    Jiang, X.2    Liu, Y.3    Tien, P.4    Gao, G.F.5
  • 171
    • 0345701489 scopus 로고    scopus 로고
    • Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion
    • Wang E, Sun X, Qian Y, Zhao L, Tien P, Gao GF. Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. Biochem Biophys Res Commun 2003; 302: 469-75.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 469-475
    • Wang, E.1    Sun, X.2    Qian, Y.3    Zhao, L.4    Tien, P.5    Gao, G.F.6
  • 172
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild C, Dubay JW, Greenwell T, et al. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc Natl Acad Sci USA 1994; 91: 12676-80.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3
  • 173
    • 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
  • 174
    • 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 AR. Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41. Biochem Biophys Res Commun 1993; 195: 533-8.
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 533-538
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 175
    • 56849129238 scopus 로고    scopus 로고
    • Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, is a potent inhibitor of HIV-1 infection
    • Yu H, Tudor D, Alfsen A, Labrosse B, Clavel F, Bomsel M. Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, is a potent inhibitor of HIV-1 infection. Retrovirology 2008; 5: 93.
    • (2008) Retrovirology , vol.5 , pp. 93
    • Yu, H.1    Tudor, D.2    Alfsen, A.3    Labrosse, B.4    Clavel, F.5    Bomsel, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.