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Volumn 23, Issue 2, 2007, Pages 224-242

Membrane perturbing actions of HIV type 1 glycoprotein 41 domains are inhibited by helical C-peptides

Author keywords

[No Author keywords available]

Indexed keywords

C PEPTIDE; ENFUVIRTIDE; GLYCOPROTEIN GP 41; HYBRID PROTEIN; LEUCINE ZIPPER PROTEIN; SYNTHETIC PEPTIDE; TRYPTOPHAN; VIRUS GLYCOPROTEIN;

EID: 33947254649     PISSN: 08892229     EISSN: None     Source Type: Journal    
DOI: 10.1089/aid.2006.0046     Document Type: Article
Times cited : (4)

References (99)
  • 2
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC and Kim PS: HIV entry and its inhibition. Cell 1998;93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 3
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang S, Zhao Q, and Debnath AK: Peptide and non-peptide HIV fusion inhibitors. Curr Pharm Des 2002;8:563-580.
    • (2002) Curr Pharm Des , vol.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 9
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger M, and Kim PS: Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997;89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, M.3    Kim, P.S.4
  • 10
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, and 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
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr CM and Kim PS: A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 1993;73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 12
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, and Kim PS: A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 1995;2:1075-1082.
    • (1995) Nat Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 13
    • 0032934830 scopus 로고    scopus 로고
    • Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs
    • Mobley PW, Waring AJ, Sherman MA, and Gordon LM: Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs. Biochim Biophys Acta 1999;1418:1-18.
    • (1999) Biochim Biophys Acta , vol.1418 , pp. 1-18
    • Mobley, P.W.1    Waring, A.J.2    Sherman, M.A.3    Gordon, L.M.4
  • 16
    • 0035839477 scopus 로고    scopus 로고
    • Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes
    • Dimitrov AS, Xiao X, Dimitrov DS, and Blumenthal R: Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes. J Biol Chem 2001;276:30335-30341.
    • (2001) J Biol Chem , vol.276 , pp. 30335-30341
    • Dimitrov, A.S.1    Xiao, X.2    Dimitrov, D.S.3    Blumenthal, R.4
  • 19
    • 0028934164 scopus 로고
    • Liposome destabilization induced by the HIV-1 fusion peptide: Effect of a single amino acid substitution
    • Pereira FB, Goni FM, and Nieva JL: Liposome destabilization induced by the HIV-1 fusion peptide: Effect of a single amino acid substitution. FEBS Lett 1995;362:243-246.
    • (1995) FEBS Lett , vol.362 , pp. 243-246
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 20
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • Martin I, Schaal H, Scheid A, and Ruysschaert J-M: Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J Virol 1996;70:298-304.
    • (1996) J Virol , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.-M.4
  • 21
    • 0031010455 scopus 로고    scopus 로고
    • Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion
    • Kliger Y, Aharoni A, Rapaport D, Jones P, Blumenthal R, and Shai Y: Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion. J Biol Chem 1997;272:13496-13505.
    • (1997) J Biol Chem , vol.272 , pp. 13496-13505
    • Kliger, Y.1    Aharoni, A.2    Rapaport, D.3    Jones, P.4    Blumenthal, R.5    Shai, Y.6
  • 22
    • 0342506479 scopus 로고    scopus 로고
    • Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects
    • Pereira FB, Goni FM, and Nieva JL: Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects. Biophys J 1997;73:1977-1986.
    • (1997) Biophys J , vol.73 , pp. 1977-1986
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 23
    • 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, and 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;195:533-538.
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 533-538
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 24
    • 0028925008 scopus 로고
    • Two partially overlapping antiviral peptides from the external portion of HIV type 1 glycoprotein 41, adjoining the transmembrane region, affect the glycoprotein 41 fusion domain
    • Neurath AR, Lin K, Strick N, and Jiang S: Two partially overlapping antiviral peptides from the external portion of HIV type 1 glycoprotein 41, adjoining the transmembrane region, affect the glycoprotein 41 fusion domain. AIDS Res Hum Retroviruses 1995;11:189-190.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 189-190
    • Neurath, A.R.1    Lin, K.2    Strick, N.3    Jiang, S.4
  • 26
    • 0030886014 scopus 로고    scopus 로고
    • Membrane fusion induced by the HIV type 1 fusion peptide: Modulation by factors affecting glycoprotein 41 activity and potential anti-HIV compounds
    • Pereira FB, Goni FM, and Nieva JL: Membrane fusion induced by the HIV type 1 fusion peptide: Modulation by factors affecting glycoprotein 41 activity and potential anti-HIV compounds. AIDS Res Hum Retroviruses 1997;13:1203-1211.
    • (1997) AIDS Res Hum Retroviruses , vol.13 , pp. 1203-1211
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 27
    • 0030841309 scopus 로고    scopus 로고
    • The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface
    • Chang D-K, Cheng S-F, and Chien W-J: The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface. J Virol 1997;71:6593-6602.
    • (1997) J Virol , vol.71 , pp. 6593-6602
    • Chang, D.-K.1    Cheng, S.-F.2    Chien, W.-J.3
  • 28
    • 7744231330 scopus 로고    scopus 로고
    • The interactions of HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy
    • Morris KF, Gao X, and Wong TC: The interactions of HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy. Biochim Biophys Acta 2004;1667:67-81.
    • (2004) Biochim Biophys Acta , vol.1667 , pp. 67-81
    • Morris, K.F.1    Gao, X.2    Wong, T.C.3
  • 30
    • 0035838516 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion peptide
    • Yang J, Gabrys CM, and Weliky DP: Solid-state nuclear magnetic resonance evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion peptide. Biochemistry 2001;40:8126-8137.
    • (2001) Biochemistry , vol.40 , pp. 8126-8137
    • Yang, J.1    Gabrys, C.M.2    Weliky, D.P.3
  • 31
    • 3042631195 scopus 로고    scopus 로고
    • Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations
    • Kanyalkar M, Srivastava S, Saran A, and Coutinho E: Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations. J Peptide Sci 2004;10:363-380.
    • (2004) J Peptide Sci , vol.10 , pp. 363-380
    • Kanyalkar, M.1    Srivastava, S.2    Saran, A.3    Coutinho, E.4
  • 32
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay JW, Roberts SJ, Brody B, and Hunter E: Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J Virol 1992;66:4748-4756.
    • (1992) J Virol , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 33
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao J, Bergeron L, Helseth E, Thali M, Repke H, and Sodroski J: Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J Virol 1993;67:2747-2755.
    • (1993) J Virol , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 34
    • 0028107566 scopus 로고
    • Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41
    • Chen SSL: Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41. J Virol 1994;68:2002-2010.
    • (1994) J Virol , vol.68 , pp. 2002-2010
    • Chen, S.S.L.1
  • 35
    • 0027266886 scopus 로고
    • Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein
    • Chen SSL, Lee C-N, Lee W-R, McIntosh K, and Lee T-H: Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J Virol 1993;67:3615-3619.
    • (1993) J Virol , vol.67 , pp. 3615-3619
    • Chen, S.S.L.1    Lee, C.-N.2    Lee, W.-R.3    McIntosh, K.4    Lee, T.-H.5
  • 36
    • 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, and Matthews T: A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition. Proc Natl Acad Sci USA 1992;89:10537-10541.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 37
    • 0029956143 scopus 로고    scopus 로고
    • Inhibitors of human immunodeficiency virus type 1 derived from gp41 transmembrane protein: Structure-activity studies
    • Kazmierski WM, Hazen RJ, Aulabaugh A, and StClair MH: Inhibitors of human immunodeficiency virus type 1 derived from gp41 transmembrane protein: Structure-activity studies. J Med Chem 1996;39:2681-2689.
    • (1996) J Med Chem , vol.39 , pp. 2681-2689
    • Kazmierski, W.M.1    Hazen, R.J.2    Aulabaugh, A.3    StClair, M.H.4
  • 38
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41
    • Lawless MK, Barney S, Guthrie KI, Bucy TB, Petteway SR Jr, and Merutka G: HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41. Biochemistry 1996;35:13697-13708.
    • (1996) Biochemistry , vol.35 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway Jr, S.R.5    Merutka, G.6
  • 39
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein M and Shin Y-K: A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 1995;34:13390-13397.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.-K.2
  • 40
    • 0029904711 scopus 로고    scopus 로고
    • HIV-1 gp41 tertiary structure studied by EPR spectroscopy
    • Rabenstein MD and Shin Y-K: HIV-1 gp41 tertiary structure studied by EPR spectroscopy. Biochemistry 1996;35:13922-13928.
    • (1996) Biochemistry , vol.35 , pp. 13922-13928
    • Rabenstein, M.D.1    Shin, Y.-K.2
  • 41
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure
    • Wild C, Greenwell T, Shugars D, Rimsky-Clarke L, and Matthews T: The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res Hum Retroviruses 1995;11:323-325.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 42
    • 0030040326 scopus 로고    scopus 로고
    • NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41
    • Consonni R, Limiroli R, Longhi R, Manera E, Vecchio G, Ragona L, Siccardi AG, and Zetta L: NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41. Biopolymers 1996;38:423-435.
    • (1996) Biopolymers , vol.38 , pp. 423-435
    • Consonni, R.1    Limiroli, R.2    Longhi, R.3    Manera, E.4    Vecchio, G.5    Ragona, L.6    Siccardi, A.G.7    Zetta, L.8
  • 43
    • 0033619917 scopus 로고    scopus 로고
    • Proline affects oligomerization of a coiled coil by inducing a kink in a long helix
    • Chang D-K, Cheng S-F, Trivedi VD, and Lin K-L: Proline affects oligomerization of a coiled coil by inducing a kink in a long helix. J Struct Biol 1999;128:270-279.
    • (1999) J Struct Biol , vol.128 , pp. 270-279
    • Chang, D.-K.1    Cheng, S.-F.2    Trivedi, V.D.3    Lin, K.-L.4
  • 44
    • 0033605369 scopus 로고    scopus 로고
    • Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1
    • Chang D-K, Cheng S-F, and Trivedi VD: Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. J Biol Chem 1999;274:5299-5309.
    • (1999) J Biol Chem , vol.274 , pp. 5299-5309
    • Chang, D.-K.1    Cheng, S.-F.2    Trivedi, V.D.3
  • 45
    • 0141457555 scopus 로고    scopus 로고
    • How structure correlates to function for membrane associated HIV-1 gp41 constructs corresponding to the N-terminal half of the ectodomain
    • Sackett K and Shai Y: How structure correlates to function for membrane associated HIV-1 gp41 constructs corresponding to the N-terminal half of the ectodomain. J Mol Biol 2003;333:47-58.
    • (2003) J Mol Biol , vol.333 , pp. 47-58
    • Sackett, K.1    Shai, Y.2
  • 46
    • 0032537597 scopus 로고    scopus 로고
    • Interaction of the major epitope region of HIV protein gp41 with membrane model systems. A fluorescence spectroscopy study
    • Santos NC, Prieto M, and Castanho MARB: Interaction of the major epitope region of HIV protein gp41 with membrane model systems. A fluorescence spectroscopy study. Biochemistry 1998;37:8674-8682.
    • (1998) Biochemistry , vol.37 , pp. 8674-8682
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.R.B.3
  • 47
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for env-mediated fusion and virus infectivity
    • Salzwedel K, West JT, and Hunter E: A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for env-mediated fusion and virus infectivity. J Virol 1999;73:2469-2480.
    • (1999) J Virol , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 48
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus mediated cell-cell fusion
    • Wild C, Greenwell T, and Matthews T: A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus mediated cell-cell fusion. AIDS Res Hum Retroviruses 1993;9:1051-1053.
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 50
    • 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, Apella E, and 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;140:315-323.
    • (1998) J Cell Biol , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Apella, E.4    Blumenthal, R.5
  • 51
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring
    • Saez-Cirion A, Nir S, Lorizate M, Agirre A, Cruz A, Perez-Gil J, and Nieva JL: Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring. J Biol Chem 2002;277:21776-21785.
    • (2002) J Biol Chem , vol.277 , pp. 21776-21785
    • Saez-Cirion, A.1    Nir, S.2    Lorizate, M.3    Agirre, A.4    Cruz, A.5    Perez-Gil, J.6    Nieva, J.L.7
  • 52
    • 3142779320 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 baseline susceptibility to the fusion inhibitors enfuvirtide and T-649 reside outside the peptide interaction site
    • Heil ML, Decker JM, Sfakianos JN, Shaw GM, Hunter E, and Derdeyn CA: Determinants of human immunodeficiency virus type 1 baseline susceptibility to the fusion inhibitors enfuvirtide and T-649 reside outside the peptide interaction site. J Virol 2004;78:7582-7589.
    • (2004) J Virol , vol.78 , pp. 7582-7589
    • Heil, M.L.1    Decker, J.M.2    Sfakianos, J.N.3    Shaw, G.M.4    Hunter, E.5    Derdeyn, C.A.6
  • 53
    • 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, and Jiang S: Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120. J Biol Chem 2005;280:11259-11273.
    • (2005) J Biol Chem , vol.280 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 55
    • 0037195784 scopus 로고    scopus 로고
    • Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP-178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro: Implications for vaccine design
    • Joyce JG, Hurni WM, Bogusky MJ, Garsky VM, Liang X, Citron MP, Danzeisen RC, Miller MD, Shiver JW, and Keller PM: Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP-178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro: Implications for vaccine design. J Biol Chem 2002;277:45811-45820.
    • (2002) J Biol Chem , vol.277 , pp. 45811-45820
    • Joyce, J.G.1    Hurni, W.M.2    Bogusky, M.J.3    Garsky, V.M.4    Liang, X.5    Citron, M.P.6    Danzeisen, R.C.7    Miller, M.D.8    Shiver, J.W.9    Keller, P.M.10
  • 58
    • 0038418536 scopus 로고    scopus 로고
    • The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: A novel fusogenic sequence
    • Suarez T, Nir S, Goni FM, Saez-Cirion A, and Nieva JL: The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: A novel fusogenic sequence. FEBS Lett 2000;477:145-149.
    • (2000) FEBS Lett , vol.477 , pp. 145-149
    • Suarez, T.1    Nir, S.2    Goni, F.M.3    Saez-Cirion, A.4    Nieva, J.L.5
  • 59
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez T, Gallaher WR, Agirre A, Goni FM, and Nieva JL: Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion. J Virol 2000;74:8038-8047.
    • (2000) J Virol , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 61
    • 2442559243 scopus 로고    scopus 로고
    • The C- and N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively
    • Shnaper S, Sackett K, Gallo SA, Blumenthal R, and Shai Y: The C- and N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively. J Biol Chem 2004;279:18526-18534.
    • (2004) J Biol Chem , vol.279 , pp. 18526-18534
    • Shnaper, S.1    Sackett, K.2    Gallo, S.A.3    Blumenthal, R.4    Shai, Y.5
  • 62
    • 1042298782 scopus 로고    scopus 로고
    • Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan
    • Moreno MR, Pascual R, and Villalain I: Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan. Biochim Biophys Acta 2004;1661:97-105.
    • (2004) Biochim Biophys Acta , vol.1661 , pp. 97-105
    • Moreno, M.R.1    Pascual, R.2    Villalain, I.3
  • 63
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli DJ, Montelaro RC, and Vogel HJ: The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 2001;40:9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 64
    • 0345060499 scopus 로고    scopus 로고
    • Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion
    • Dimitrov AS, Rawat SS, Jiang S, and Blumenthal R: Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion. Biochemistry 2003;42:14150-14158.
    • (2003) Biochemistry , vol.42 , pp. 14150-14158
    • Dimitrov, A.S.1    Rawat, S.S.2    Jiang, S.3    Blumenthal, R.4
  • 66
    • 0026743982 scopus 로고
    • The amino terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation
    • Gordon LM, Curtain CC, Zhong YC, Kirkpatrick A, Mobley PW, and Waring AJ: The amino terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation. Biochim Biophys Acta 1992;1139:257-274.
    • (1992) Biochim Biophys Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 68
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson WCJ: Protein secondary structure and circular dichroism: A practical guide. Proteins Struct Funct Genet 1990;7:205-214.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 205-214
    • Johnson, W.C.J.1
  • 69
    • 0022691315 scopus 로고
    • Examination of the secondary structure of protein by deconvolved FTIR spectra
    • Byler DM and Susi H: Examination of the secondary structure of protein by deconvolved FTIR spectra. Biopolymers 1986;25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 70
    • 0025055304 scopus 로고
    • The most highly amphipathic alpha helices include two amino acid segments in human immunodeficiency virus glycoprotein gp41
    • Eisenberg D and Wesson M: The most highly amphipathic alpha helices include two amino acid segments in human immunodeficiency virus glycoprotein gp41. Biopolymers 1990;29:171-177.
    • (1990) Biopolymers , vol.29 , pp. 171-177
    • Eisenberg, D.1    Wesson, M.2
  • 71
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody RW: Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J 1994;23:253-262.
    • (1994) Eur Biophys J , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 72
    • 16844383101 scopus 로고    scopus 로고
    • The tryptophan-rich region of HIV gp41 and the promotion of cholesterol-rich domains
    • Epand RF, Sayer BG, and Epand RM: The tryptophan-rich region of HIV gp41 and the promotion of cholesterol-rich domains. Biochemistry 2005;44:5525-5531.
    • (2005) Biochemistry , vol.44 , pp. 5525-5531
    • Epand, R.F.1    Sayer, B.G.2    Epand, R.M.3
  • 73
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N and Woody RW: Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 2000;287:252-260.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 74
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo JLR and Goni FM: Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 1999;72:367-405.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 75
    • 0034701058 scopus 로고    scopus 로고
    • Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
    • Shu W, Liu J, Radigen L, Jiang S, and Lu M: Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides. Biochemistry 2000;39:1634-1642.
    • (2000) Biochemistry , vol.39 , pp. 1634-1642
    • Shu, W.1    Liu, J.2    Radigen, L.3    Jiang, S.4    Lu, M.5
  • 76
    • 0035078486 scopus 로고    scopus 로고
    • The leucine zipper motif of the envelope glycoprotein ectodomain of human immunodeficiency virus type 1 contains conformationally flexible regions as revealed by NMR and circular dichroism studies in different media
    • Chang D-K, Trivedi VD, Cheng S-F, and Francis S: The leucine zipper motif of the envelope glycoprotein ectodomain of human immunodeficiency virus type 1 contains conformationally flexible regions as revealed by NMR and circular dichroism studies in different media. J Peptide Res 2001;57:234-239.
    • (2001) J Peptide Res , vol.57 , pp. 234-239
    • Chang, D.-K.1    Trivedi, V.D.2    Cheng, S.-F.3    Francis, S.4
  • 77
    • 0034645796 scopus 로고    scopus 로고
    • Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation
    • Kliger Y and Shai Y: Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation. J Mol Biol 2000;295:163-168.
    • (2000) J Mol Biol , vol.295 , pp. 163-168
    • Kliger, Y.1    Shai, Y.2
  • 79
    • 0034755554 scopus 로고    scopus 로고
    • Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing antibody 2F5
    • Parker CE, Deterding LJ, Hager-Braun C, Binley JM, Schulke N, Katinger H, Moore JP, and Tomer KB: Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing antibody 2F5. J Virol 2001;75:10906-10911.
    • (2001) J Virol , vol.75 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-Braun, C.3    Binley, J.M.4    Schulke, N.5    Katinger, H.6    Moore, J.P.7    Tomer, K.B.8
  • 80
    • 0037159248 scopus 로고    scopus 로고
    • 10-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41
    • 10-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41. Biochemistry 2002;41:12687-12696.
    • (2002) Biochemistry , vol.41 , pp. 12687-12696
    • Biron, Z.1    Khare, S.2    Samson, A.O.3    Hayek, Y.4    Naider, F.5    Anglister, J.6
  • 82
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A, Katinger H, Mascola JR, Wyatt R, and Kwong PD: Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J Virol 2004;78:10724-10737.
    • (2004) J Virol , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5    Wyatt, R.6    Kwong, P.D.7
  • 84
    • 0037136052 scopus 로고    scopus 로고
    • Conformational transitions of membrane-bound HIV-1 fusion peptide
    • Saez-Cirion A and Nieva JL: Conformational transitions of membrane-bound HIV-1 fusion peptide. Biochim Biophys Acta 2002;1564:57-65.
    • (2002) Biochim Biophys Acta , vol.1564 , pp. 57-65
    • Saez-Cirion, A.1    Nieva, J.L.2
  • 85
    • 0027056047 scopus 로고
    • A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41
    • Fujii G, Horvath S, Woodward S, Eiserling F, and Eisenberg D: A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41. Protein Sci 1992;1:1454-1464.
    • (1992) Protein Sci , vol.1 , pp. 1454-1464
    • Fujii, G.1    Horvath, S.2    Woodward, S.3    Eiserling, F.4    Eisenberg, D.5
  • 86
    • 1642494594 scopus 로고    scopus 로고
    • Putative role of membrane in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level
    • Veiga S, Henriques S, Santos NC, and Castanho M: Putative role of membrane in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level. Biochem J 2004;377:107-110.
    • (2004) Biochem J , vol.377 , pp. 107-110
    • Veiga, S.1    Henriques, S.2    Santos, N.C.3    Castanho, M.4
  • 87
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta RA, Wild CT, Weng Y, and Weiss CD: Capture of an early fusion-active conformation of HIV-1 gp41. Nat Struct Biol 1998;5:276-279.
    • (1998) Nat Struct Biol , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 88
    • 20744446731 scopus 로고    scopus 로고
    • Design, expression and immunogenicity of a soluble HIV trimeric envelope fragment adopting a prefusion gp41 configuration
    • Qiao ZS, Kim M, Reinhold B, Montefiori D, Wang JH, and Reinheit EL: Design, expression and immunogenicity of a soluble HIV trimeric envelope fragment adopting a prefusion gp41 configuration. J Biol Chem 2005;280:23138-23146.
    • (2005) J Biol Chem , vol.280 , pp. 23138-23146
    • Qiao, Z.S.1    Kim, M.2    Reinhold, B.3    Montefiori, D.4    Wang, J.H.5    Reinheit, E.L.6
  • 89
    • 0029040825 scopus 로고
    • Multifaceted consequences of anti-gp41 monoclonal antibody 2F5 binding to HIV type 1 virions
    • Neurath AR, Strick N, Lin K, and Jiang S: Multifaceted consequences of anti-gp41 monoclonal antibody 2F5 binding to HIV type 1 virions. AIDS Res Hum Retroviruses 1995;11:687-696.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 687-696
    • Neurath, A.R.1    Strick, N.2    Lin, K.3    Jiang, S.4
  • 90
    • 0034695596 scopus 로고    scopus 로고
    • Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion
    • Shu W, Ji H, and Lu M: Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion. J Biol Chem 2000;275:1839-1845.
    • (2000) J Biol Chem , vol.275 , pp. 1839-1845
    • Shu, W.1    Ji, H.2    Lu, M.3
  • 91
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Munoz-Barroso I, Salzwedel K, Hunter E, and Blumenthal R: Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J Virol 1999;73:6089-6092.
    • (1999) J Virol , vol.73 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 92
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia RC, Tian H, and Jensen FC: Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Acad Sei USA 1993;90:5181-5185.
    • (1993) Proc Natl Acad Sei USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 93
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • Vincent N, Genin C, and Malvoisin E: Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups. Biochim Biophys Acta 2003;1567:157-164.
    • (2003) Biochim Biophys Acta , vol.1567 , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 94
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, and Matthews TJ: Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 1998;72:986-993.
    • (1998) J Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 95
    • 0038425042 scopus 로고    scopus 로고
    • Proteins with H-bond packing defects are highly interactive with lipids bilayers: Implications for amyloidogenesis
    • Fernandez A and Berry RS: Proteins with H-bond packing defects are highly interactive with lipids bilayers: Implications for amyloidogenesis. Proc Natl Acad Sci USA 2003;100:2391-2396.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2391-2396
    • Fernandez, A.1    Berry, R.S.2


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