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Volumn 48, Issue 23, 2009, Pages 5320-5331

Distinct mechanisms of lipid bilayer perturbation induced by peptides derived from the membrane-proximal external region of HIV-1 gp41

Author keywords

[No Author keywords available]

Indexed keywords

BI-LAYER; ENVELOPE GLYCOPROTEINS; HUMAN IMMUNODEFICIENCY VIRUS TYPE-1; HYDROCARBON CORES; MELITTIN; MEMBRANE PERMEABILIZATION; MEMBRANE-BOUND; MOLECULAR MECHANISM; NEUTRALIZING ANTIBODIES; NEUTRALIZING EPITOPE; PERMEABILIZATION; SDS-PAGE; SUB-DOMAINS; WATER PHASE;

EID: 67049119439     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900504t     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 0034675998 scopus 로고    scopus 로고
    • HIV-1 membrane fusion: Targets of opportunity
    • Doms, R. W., and Moore, J. P. (2000) HIV-1 membrane fusion: targets of opportunity. J. Cell Biol. 151, F9-14.
    • (2000) J. Cell Biol. , vol.151
    • Doms, R.W.1    Moore, J.P.2
  • 2
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70, 777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 4
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher, W. R. (1987) Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell 50, 327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 5
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • Epand, R. M. (2003) Fusion peptides and the mechanism of viral fusion. Biochim. Biophys. Acta 1614, 116-121.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 116-121
    • Epand, R.M.1
  • 6
    • 0038487379 scopus 로고    scopus 로고
    • Are fusion peptides a good model to study viral cell fusion?
    • Nieva, J. L., and Agirre, A. (2003) Are fusion peptides a good model to study viral cell fusion?. Biochim. Biophys. Acta 1614, 104-115.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 104-115
    • Nieva, J.L.1    Agirre, A.2
  • 8
    • 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, J. T., and Hunter, E. (1999) 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. 73, 2469-2480. (Pubitemid 29098154)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 9
    • 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. (1999) Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J. Virol. 73, 6089-6092. (Pubitemid 29274898)
    • (1999) Journal of Virology , vol.73 , Issue.7 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 10
    • 43949135190 scopus 로고    scopus 로고
    • Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion
    • DOI 10.1128/JVI.00305-08
    • Vishwanathan, S. A., and Hunter, E. (2008) Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion. J. Virol. 82, 5118-5126. (Pubitemid 351705220)
    • (2008) Journal of Virology , vol.82 , Issue.11 , pp. 5118-5126
    • Vishwanathan, S.A.1    Hunter, E.2
  • 11
    • 37849019272 scopus 로고    scopus 로고
    • Hydrophobic substitutions in the first residue of the CRAC segment of the gp41 protein of HIV
    • Vishwanathan, S. A., Thomas, A., Brasseur, R., Epand, R. F., Hunter, E., and Epand, R. M. (2008) Hydrophobic substitutions in the first residue of the CRAC segment of the gp41 protein of HIV. Biochemistry 47, 124-130.
    • (2008) Biochemistry , vol.47 , pp. 124-130
    • Vishwanathan, S.A.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4    Hunter, E.5    Epand, R.M.6
  • 12
    • 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
    • DOI 10.1128/JVI.74.17.8038-8047.2000
    • Suarez, T., Gallaher, W. R., Agirre, A., Goni, F. M., and Nieva, J. L. (2000) Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Virol. 74, 8038-8047. (Pubitemid 30641649)
    • (2000) Journal of Virology , vol.74 , Issue.17 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 14
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • DOI 10.1021/bi010640u
    • Schibli, D. J., Montelaro, R. C., and Vogel, H. J. (2001) The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 40, 9570-9578. (Pubitemid 32757895)
    • (2001) Biochemistry , vol.40 , Issue.32 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 15
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun, Z. Y., Oh, K. J., Kim, M., Yu, J., Brusic, V., Song, L., Qiao, Z., Wang, J. H., Wagner, G., and Reinherz, E. L. (2008) HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 28, 52-63.
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1    Oh, K.J.2    Kim, M.3    Yu, J.4    Brusic, V.5    Song, L.6    Qiao, Z.7    Wang, J.H.8    Wagner, G.9    Reinherz, E.L.10
  • 16
    • 34147104516 scopus 로고    scopus 로고
    • AIDS virus envelope spike structure
    • Roux, K. H., and Taylor, K. A. (2007) AIDS virus envelope spike structure. Curr. Opin. Struct. Biol. 17, 244-252.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 244-252
    • Roux, K.H.1    Taylor, K.A.2
  • 17
    • 2442559243 scopus 로고    scopus 로고
    • The C- And the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively
    • Shnaper, S., Sackett, K., Gallo, S. A., Blumenthal, R., and Shai, Y. (2004) The C- and the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively. J. Biol. Chem. 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
  • 18
    • 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, J. L. (2002) Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring. J. Biol. Chem. 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
  • 20
    • 45449105978 scopus 로고    scopus 로고
    • Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission
    • Lorizate, M., Huarte, N., Saez-Cirion, A., and Nieva, J. L. (2008) Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission. Biochim. Biophys. Acta 1778, 1624-1639.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1624-1639
    • Lorizate, M.1    Huarte, N.2    Saez-Cirion, A.3    Nieva, J.L.4
  • 21
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- And arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • Chan, D. I., Prenner, E. J., and Vogel, H. J. (2006) Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta 1758, 1184-1202.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 22
    • 50949104097 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5
    • Huarte, N., Lorizate, M., Maeso, R., Kunert, R., Arranz, R., Valpuesta, J. M., and Nieva, J. L. (2008) The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5. J. Virol. 82, 8986-8996.
    • (2008) J. Virol. , vol.82 , pp. 8986-8996
    • Huarte, N.1    Lorizate, M.2    Maeso, R.3    Kunert, R.4    Arranz, R.5    Valpuesta, J.M.6    Nieva, J.L.7
  • 23
    • 33845987097 scopus 로고    scopus 로고
    • Recognition and blocking of HIV-1 gp41 pretransmembrane sequence by monoclonal 4E10 antibody in a Raft-like membrane environment
    • Lorizate, M., Cruz, A., Huarte, N., Kunert, R., Perez-Gil, J., and Nieva, J. L. (2006) Recognition and blocking of HIV-1 gp41 pretransmembrane sequence by monoclonal 4E10 antibody in a Raft-like membrane environment. J. Biol. Chem. 281, 39598-39606.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39598-39606
    • Lorizate, M.1    Cruz, A.2    Huarte, N.3    Kunert, R.4    Perez-Gil, J.5    Nieva, J.L.6
  • 24
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: Dominant site of antibody neutralization and target for vaccine design
    • Montero, M., van Houten, N. E., Wang, X., and Scott, J. K. (2008) The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol. Mol. Biol. Rev. 72, 54-84.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 54-84
    • Montero, M.1    Van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 25
    • 33845978962 scopus 로고    scopus 로고
    • Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies
    • Sanchez-Martinez, S., Lorizate, M., Katinger, H., Kunert, R., and Nieva, J. L. (2006) Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies. AIDS Res. Hum. Retroviruses 22, 998-1006.
    • (2006) AIDS Res. Hum. Retroviruses , vol.22 , pp. 998-1006
    • Sanchez-Martinez, S.1    Lorizate, M.2    Katinger, H.3    Kunert, R.4    Nieva, J.L.5
  • 26
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining energetics of peptide-bilayer interactions
    • DOI 10.1016/S0076-6879(98)95035-2
    • White, S. H., Wimley, W. C., Ladokhin, A. S., and Hristova, K. (1998) Protein folding in membranes: determining energetics of peptide-bilayer interactions. Methods Enzymol. 295, 62-87. (Pubitemid 29349909)
    • (1998) Methods in Enzymology , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 27
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J., and Holloway, P. W. (1990) Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry 29, 9638-9643. (Pubitemid 20355212)
    • (1990) Biochemistry , vol.29 , Issue.41 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 28
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon, A. I., Soekarjo, M. W., De Gier, J., and De Kruijff, B. (1990) The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 29, 8229-8240. (Pubitemid 20307796)
    • (1990) Biochemistry , vol.29 , Issue.36 , pp. 8229-8240
    • De Kroon, A.I.P.M.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 29
    • 0021890825 scopus 로고
    • H+- and Ca2+-induced fusion and destabilization of liposomes
    • Ellens, H., Bentz, J., and Szoka, F. C. (1985) H+- and Ca2+-induced fusion and destabilization of liposomes. Biochemistry 24, 3099-3106.
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 31
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., Selsted, M. E., and White, S. H. (1994) Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 3, 1362-1373. (Pubitemid 24314455)
    • (1994) Protein Science , vol.3 , Issue.9 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 32
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • Ladokhin, A. S., Wimley, W. C., and White, S. H. (1995) Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching. Biophys. J. 69, 1964-1971.
    • (1995) Biophys. J. , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 33
    • 0031008251 scopus 로고    scopus 로고
    • Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching
    • DOI 10.1016/S0076-6879(97)78025-X
    • Ladokhin, A. S., Wimley, W. C., Hristova, K., and White, S. H. (1997) Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching. Methods Enzymol. 278, 474-486. (Pubitemid 27229934)
    • (1997) Methods in Enzymology , vol.278 , pp. 474-487
    • Ladokhin, A.S.1    Wimley, W.C.2    Hristova, K.3    White, S.H.4
  • 34
    • 35649005895 scopus 로고    scopus 로고
    • β-Sheet pore-forming peptides selected from a rational combinatorial library: Mechanism of pore formation in lipid vesicles and activity in biological membranes
    • DOI 10.1021/bi700978h
    • Rausch, J. M., Marks, J. R., Rathinakumar, R., and Wimley, W. C. (2007) Beta-sheet pore-forming peptides selected from a rational combinatorial library: mechanism of pore formation in lipid vesicles and activity in biological membranes. Biochemistry 46, 12124-12139. (Pubitemid 350022368)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12124-12139
    • Rausch, J.M.1    Marks, J.R.2    Rathinakumar, R.3    Wimley, W.C.4
  • 35
    • 0029731358 scopus 로고    scopus 로고
    • Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide
    • Nicol, F., Nir, S., and Szoka, F. C.Jr. (1996) Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide. Biophys. J. 71, 3288-3301. (Pubitemid 26422370)
    • (1996) Biophysical Journal , vol.71 , Issue.6 , pp. 3288-3301
    • Nicol, F.1    Nir, S.2    Szoka Jr., F.C.3
  • 36
    • 0034164025 scopus 로고    scopus 로고
    • Interactions of peptides with liposomes: Pore formation and fusion
    • Nir, S., and Nieva, J. L. (2000) Interactions of peptides with liposomes: pore formation and fusion. Prog. Lipid Res. 39, 181-206.
    • (2000) Prog. Lipid Res. , vol.39 , pp. 181-206
    • Nir, S.1    Nieva, J.L.2
  • 37
    • 0037687909 scopus 로고    scopus 로고
    • Effects of sphingomyelin on melittin pore formation
    • Gomara, M. J., Nir, S., and Nieva, J. L. (2003) Effects of sphingomyelin on melittin pore formation. Biochim. Biophys. Acta 1612, 83-89.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 83-89
    • Gomara, M.J.1    Nir, S.2    Nieva, J.L.3
  • 38
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • DOI 10.1128/JVI.02666-07
    • Shang, L., Yue, L., and Hunter, E. (2008) Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. J. Virol. 82, 5417-5428. (Pubitemid 351705249)
    • (2008) Journal of Virology , vol.82 , Issue.11 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 39
    • 0242488929 scopus 로고    scopus 로고
    • Translocons, thermodynamics, and the folding of membrane proteins
    • DOI 10.1016/S0014-5793(03)01153-0
    • White, S. H. (2003) Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett. 555, 116-121. (Pubitemid 37431107)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 116-121
    • White, S.H.1
  • 40
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • DOI 10.1021/bi00380a042
    • McIntosh, T. J., and Holloway, P. W. (1987) Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry 26, 1783-1788. (Pubitemid 17047651)
    • (1987) Biochemistry , vol.26 , Issue.6 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 41
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • DOI 10.1128/JVI.79.2.1252-1261.2005
    • Zwick, M. B., Jensen, R., Church, S., Wang, M., Stiegler, G., Kunert, R., Katinger, H., and Burton, D. R. (2005) Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J. Virol. 79, 1252-1261. (Pubitemid 40053907)
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 1252-1261
    • Zwick, M.B.1    Jensen, R.2    Church, S.3    Wang, M.4    Stiegler, G.5    Kunert, R.6    Katinger, H.7    Burton, D.R.8
  • 42
    • 0035909890 scopus 로고    scopus 로고
    • Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils
    • Keating, A. E., Malashkevich, V. N., Tidor, B., and Kim, P. S. (2001) Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils. Proc. Natl. Acad. Sci. U.S.A. 98, 14825-14830.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14825-14830
    • Keating, A.E.1    Malashkevich, V.N.2    Tidor, B.3    Kim, P.S.4
  • 43
    • 0037020082 scopus 로고    scopus 로고
    • Designing heterodimeric two-stranded R-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity
    • Litowski, J. R., and Hodges, R. S. (2002) Designing heterodimeric two-stranded R-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity. J. Biol. Chem. 277, 37272-37279.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37272-37279
    • Litowski, R.J.1    Hodges, R.S.2
  • 45
    • 0030971376 scopus 로고    scopus 로고
    • Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin
    • Ladokhin, A. S., Selsted, M. E., and White, S. H. (1997) Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin. Biophys. J. 72, 1762-1766. (Pubitemid 27133115)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1762-1766
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 46
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin, A. S., and White, S. H. (2001) 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim. Biophys. Acta 1514, 253-260.
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, S.A.1    White, S.H.2
  • 47
    • 0029042292 scopus 로고
    • Study of vesicle leakage induced by melittin
    • Benachir, T., and Lafleur, M. (1995) Study of vesicle leakage induced by melittin. Biochim. Biophys. Acta 1235, 452-460.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 452-460
    • Benachir, T.1    Lafleur, M.2
  • 48
    • 0034117591 scopus 로고    scopus 로고
    • Effect of phospholipid composition on an amphipathic peptide-mediated pore formation in bilayer vesicles
    • Nicol, F., Nir, S., and Szoka, F. C.Jr. (2000) Effect of phospholipid composition on an amphipathic peptide-mediated pore formation in bilayer vesicles. Biophys. J. 78, 818-829. (Pubitemid 30211839)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 818-829
    • Nicol, F.1    Nir, N.2    Szoka Jr., F.C.3
  • 49
    • 0030025781 scopus 로고    scopus 로고
    • Reversible surface aggregation in pore formation by pardaxin
    • Rapaport, D., Peled, R., Nir, S., and Shai, Y. (1996) Reversible surface aggregation in pore formation by pardaxin. Biophys. J. 70, 2502-2512. (Pubitemid 26000951)
    • (1996) Biophysical Journal , vol.70 , Issue.6 , pp. 2502-2512
    • Rapaport, D.1    Peled, R.2    Nir, S.3    Shai, Y.4
  • 50
    • 0029070927 scopus 로고
    • Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41
    • Arroyo, J., Boceta, M., Gonzalez, M. E., Michel, M., and Carrasco, L. (1995) Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41. J. Virol. 69, 4095-4102.
    • (1995) J. Virol. , vol.69 , pp. 4095-4102
    • Arroyo, J.1    Boceta, M.2    Gonzalez, M.E.3    Michel, M.4    Carrasco, L.5
  • 51
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • DOI 10.1371/journal.ppat.0020083
    • Zanetti, G., Briggs, J. A., Grunewald, K., Sattentau, Q. J., and Fuller, S. D. (2006) Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog. 2, e83. (Pubitemid 44299887)
    • (2006) PLoS Pathogens , vol.2 , Issue.8 , pp. 790-797
    • Zanetti, G.1    Briggs, J.A.G.2    Grunewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 52
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • DOI 10.1038/nature04817, PII N04817
    • Zhu, P., Liu, J., Bess, J.Jr., Chertova, E., Lifson, J. D., Grise, H., Ofek, G. A., Taylor, K. A., and Roux, K. H. (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441, 847-852. (Pubitemid 43910414)
    • (2006) Nature , vol.441 , Issue.7095 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess Jr., J.3    Chertova, E.4    Lifson, J.D.5    Grise, H.6    Ofek, G.A.7    Taylor, K.A.8    Roux, K.H.9
  • 53
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: Further evidence for tripod-like legs
    • Zhu, P., Winkler, H., Chertova, E., Taylor, K. A., and Roux, K. H. (2008) Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog. 4, e1000203.
    • (2008) PLoS Pathog. , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5
  • 54
    • 0041320883 scopus 로고    scopus 로고
    • A new mechanism of model membrane fusion determined from Monte Carlo simulation
    • Muller, M., Katsov, K., and Schick, M. (2003) A new mechanism of model membrane fusion determined from Monte Carlo simulation. Biophys. J. 85, 1611-1623. (Pubitemid 37052246)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1611-1623
    • Muller, M.1    Katsov, K.2    Schick, M.3
  • 55
    • 55949137911 scopus 로고    scopus 로고
    • Membrane lysis during biological membrane fusion: Collateral damage by misregulated fusion machines
    • Engel, A., and Walter, P. (2008) Membrane lysis during biological membrane fusion: collateral damage by misregulated fusion machines. J. Cell Biol. 183, 181-186.
    • (2008) J. Cell Biol. , vol.183 , pp. 181-186
    • Engel, A.1    Walter, P.2
  • 56
    • 33846847940 scopus 로고    scopus 로고
    • Exposure of the membrane-proximal external region of HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion
    • DOI 10.1021/bi062245f
    • Dimitrov, A. S., Jacobs, A., Finnegan, C. M., Stiegler, G., Katinger, H., and Blumenthal, R. (2007) Exposure of the membrane-proximal external region of HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion. Biochemistry 46, 1398-1401. (Pubitemid 46208487)
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1398-1401
    • Dimitrov, A.S.1    Jacobs, A.2    Finnegan, C.M.3    Stiegler, G.4    Katinger, H.5    Blumenthal, R.6
  • 57
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 58
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


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