메뉴 건너뛰기




Volumn 16, Issue 7, 2009, Pages 743-750

Antimicrobial peptides and viral fusion peptides : How different they are?

Author keywords

Antimicrobial peptides; GXXXG motif; Hydrophobicity; Membrane disruptive properties; Structural plasticity; Viral fusion peptides

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; PEPTIDE; VIRUS FUSION PROTEIN;

EID: 67849131062     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609788681814     Document Type: Article
Times cited : (24)

References (82)
  • 1
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M.R.; Yount, N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev., 2003, 55(1), 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 3
    • 1042267410 scopus 로고    scopus 로고
    • Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?
    • Papo, N.; Shai, Y. Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes? Peptides, 2003, 24(11), 1693-1703.
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 4
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta, 1999, 1462(1-2), 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , Issue.1-2 , pp. 55-70
    • Shai, Y.1
  • 5
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang, H.W. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta, 2006, 1758(9), 1292-1302.
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1292-1302
    • Huang, H.W.1
  • 6
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B.; Lohner, K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta, 2006, 1758(9), 1529-1539.
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 7
    • 28044443162 scopus 로고    scopus 로고
    • Antibacterial peptides and proteins with multiple cellular targets
    • Otvos, L., Jr. Antibacterial peptides and proteins with multiple cellular targets. J. Pept. Sci., 2005, 11(11), 697-706.
    • (2005) J. Pept. Sci. , vol.11 , Issue.11 , pp. 697-706
    • Otvos Jr., L.1
  • 8
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D.M.; Kim, P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem., 2001, 70, 777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 9
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review)
    • Durell, S.R.; Martin, I.; Ruysschaert, J.M.; Shai, Y.; Blumenthal, R. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review). Mol. Membr. Biol., 1997, 14(3), 97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , Issue.3 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.M.3    Shai, Y.4    Blumenthal, R.5
  • 10
  • 11
    • 0034442295 scopus 로고    scopus 로고
    • Functional domains within fusion proteins: Prospectives for development of peptide inhibitors of viral cell fusion
    • Shai, Y. Functional domains within fusion proteins: prospectives for development of peptide inhibitors of viral cell fusion. Biosci. Rep., 2000, 20(6), 535-555.
    • (2000) Biosci. Rep. , vol.20 , Issue.6 , pp. 535-555
    • Shai, Y.1
  • 12
    • 34547128385 scopus 로고    scopus 로고
    • Mode of membrane interaction and fusogenic properties of a de novo transmembrane model peptide depend on the length of the hydrophobic core.
    • Lorin, A.; Charloteaux, B.; Fridmann-Sirkis, Y.; Thomas, A.; Shai, Y.; Brasseur, R. Mode of membrane interaction and fusogenic properties of a de novo transmembrane model peptide depend on the length of the hydrophobic core. J. Biol. Chem., 2007, 282(25), 18388-18396.
    • (2007) J. Biol. Chem. , vol.282 , Issue.25 , pp. 18388-18396
    • Lorin, A.1    Charloteaux, B.2    Fridmann-Sirkis, Y.3    Thomas, A.4    Shai, Y.5    Brasseur, R.6
  • 13
    • 0038487379 scopus 로고    scopus 로고
    • Are fusion peptides a good model to study viral cell fusion?
    • Nieva, J.L.; Agirre, A. Are fusion peptides a good model to study viral cell fusion? Biochim. Biophys. Acta, 2003, 1614(1), 104-115.
    • (2003) Biochim. Biophys. Acta , vol.1614 , Issue.1 , pp. 104-115
    • Nieva, J.L.1    Agirre, A.2
  • 14
    • 0345276642 scopus 로고    scopus 로고
    • Interaction of a synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: A biophysical study
    • Aranda, F.J.; Teruel, J.A.; Ortiz, A. Interaction of a synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: a biophysical study. Biochim. Biophys. Acta, 2003, 1618(1), 51-58.
    • (2003) Biochim. Biophys. Acta , vol.1618 , Issue.1 , pp. 51-58
    • Aranda, F.J.1    Teruel, J.A.2    Ortiz, A.3
  • 15
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • Epand, R.M. Fusion peptides and the mechanism of viral fusion. Biochim. Biophys. Acta, 2003, 1614(1), 116-121.
    • (2003) Biochim. Biophys. Acta , vol.1614 , Issue.1 , pp. 116-121
    • Epand, R.M.1
  • 16
    • 0033696634 scopus 로고    scopus 로고
    • Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions
    • DOI 10.1016/S0196-9781(00)00316-8, PII S0196978100003168
    • Mangoni, M.L.; Grovale, N.; Giorgi, A.; Mignogna, G.; Simmaco, M.; Barra, D. Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions. Peptides, 2000, 21(11), 1673-1679. (Pubitemid 30945691)
    • (2000) Peptides , vol.21 , Issue.11 , pp. 1673-1679
    • Mangoni M.Luisa1    Grovale, N.2    Giorgi, A.3    Mignogna, G.4    Simmaco, M.5    Barra, D.6
  • 17
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan-and argininerich antimicrobial peptides: Structures and mechanisms of action
    • Chan, D.I.; Prenner, E.J.; Vogel, H.J. Tryptophan-and argininerich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta, 2006, 1758(9), 1184-1202.
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 19
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas, P.; Mor, A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbiol., 1995, 49, 277-304.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 20
    • 64349096490 scopus 로고    scopus 로고
    • The dermaseptin superfamily: A genebased combinatorial library of antimicrobial peptides
    • in press
    • Nicolas, P.; El Amri, C. The dermaseptin superfamily: a genebased combinatorial library of antimicrobial peptides. Biochim. Biophys. Acta, 2008, in press.
    • (2008) Biochim. Biophys. Acta
    • Nicolas, P.1    El Amri, C.2
  • 21
    • 27744577746 scopus 로고    scopus 로고
    • Properties and structures of the influenza and HIV fusion peptides on lipid membranes: Implications for a role in fusion
    • Haque, M.E.; Koppaka, V.; Axelsen, P.H.; Lentz, B.R. Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusion. Biophys. J., 2005, 89(5), 3183-3194.
    • (2005) Biophys. J. , vol.89 , Issue.5 , pp. 3183-3194
    • Haque, M.E.1    Koppaka, V.2    Axelsen, P.H.3    Lentz, B.R.4
  • 23
    • 0036707998 scopus 로고    scopus 로고
    • Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin
    • Nagpal, S.; Kaur, K.J.; Jain, D.; Salunke, D.M. Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin. Protein Sci., 2002, 11(9), 2158-2167.
    • (2002) Protein Sci. , vol.11 , Issue.9 , pp. 2158-2167
    • Nagpal, S.1    Kaur, K.J.2    Jain, D.3    Salunke, D.M.4
  • 24
    • 33646570880 scopus 로고    scopus 로고
    • Lipiddestabilising properties of a peptide with structural plasticity
    • Lorin, A.; Thomas, A.; Stroobant, V.; Brasseur, R.; Lins, L. Lipiddestabilising properties of a peptide with structural plasticity. Chem. Phys. Lipids, 2006, 141(1-2), 185-196.
    • (2006) Chem. Phys. Lipids , vol.141 , Issue.1-2 , pp. 185-196
    • Lorin, A.1    Thomas, A.2    Stroobant, V.3    Brasseur, R.4    Lins, L.5
  • 25
    • 34547652634 scopus 로고    scopus 로고
    • Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers
    • Li, Y.; Tamm, L.K. Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers. Biophys. J., 2007, 93(3), 876-885.
    • (2007) Biophys. J. , vol.93 , Issue.3 , pp. 876-885
    • Li, Y.1    Tamm, L.K.2
  • 26
    • 43049084716 scopus 로고    scopus 로고
    • Structural polymorphism of two CPP: An important parameter of activity
    • Deshayes, S.; Decaffmeyer, M.; Brasseur, R.; Thomas, A. Structural polymorphism of two CPP: an important parameter of activity. Biochim. Biophys. Acta, 2008, 1778(5), 1197-1205.
    • (2008) Biochim. Biophys. Acta , vol.1778 , Issue.5 , pp. 1197-1205
    • Deshayes, S.1    Decaffmeyer, M.2    Brasseur, R.3    Thomas, A.4
  • 27
    • 43249103254 scopus 로고    scopus 로고
    • Plasticins: membrane-damaging peptides with,chameleon-like' properties
    • El Amri, C.; Nicolas, P. Plasticins: membrane-damaging peptides with,chameleon-like' properties. Cell. Mol. Life Sci., 2008, 65(6), 895-909.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.6 , pp. 895-909
    • El Amri, C.1    Nicolas, P.2
  • 29
    • 33746655724 scopus 로고    scopus 로고
    • The SIV tilted peptide induces cylindrical reverse micelles in supported lipid bilayers
    • El Kirat, K.; Dufrene, Y.F.; Lins, L.; Brasseur, R. The SIV tilted peptide induces cylindrical reverse micelles in supported lipid bilayers. Biochemistry, 2006, 45(30), 9336-9341.
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9336-9341
    • El Kirat, K.1    Dufrene, Y.F.2    Lins, L.3    Brasseur, R.4
  • 30
    • 42149130277 scopus 로고    scopus 로고
    • Tilted peptides: A structural motif involved in protein membrane insertion?
    • Lins, L.; Brasseur, R. Tilted peptides: a structural motif involved in protein membrane insertion? J. Pept. Sci., 2008, 14(4), 416-422.
    • (2008) J. Pept. Sci. , vol.14 , Issue.4 , pp. 416-422
    • Lins, L.1    Brasseur, R.2
  • 31
    • 0034456592 scopus 로고    scopus 로고
    • Use of hydrophobic moment plot methodology to aid the identification of oblique orientated alpha-helices
    • Harris, F.; Wallace, J.; Phoenix, D.A. Use of hydrophobic moment plot methodology to aid the identification of oblique orientated alpha-helices. Mol. Membr. Biol., 2000, 17(4), 201-207.
    • (2000) Mol. Membr. Biol. , vol.17 , Issue.4 , pp. 201-207
    • Harris, F.1    Wallace, J.2    Phoenix, D.A.3
  • 32
    • 11244352103 scopus 로고    scopus 로고
    • Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?
    • Dennison, S.R.; Harris, F.; Phoenix, D.A. Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion? Protein Pept. Lett., 2005, 12(1), 27-29.
    • (2005) Protein Pept. Lett. , vol.12 , Issue.1 , pp. 27-29
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 33
    • 44049096050 scopus 로고    scopus 로고
    • Fusion peptides and transmembrane domains of fusion proteins are characterized by different but specific structural properties
    • Weise, K.; Reed, J. Fusion peptides and transmembrane domains of fusion proteins are characterized by different but specific structural properties. Chembiochem, 2008, 9(6), 934-943.
    • (2008) Chembiochem , vol.9 , Issue.6 , pp. 934-943
    • Weise, K.1    Reed, J.2
  • 34
    • 26444584944 scopus 로고    scopus 로고
    • Interaction of fusion peptides from HIV gp41 with membranes: A time-resolved membrane binding, lipid mixing, and structural study
    • Buzon, V.; Padros, E.; Cladera, J. Interaction of fusion peptides from HIV gp41 with membranes: a time-resolved membrane binding, lipid mixing, and structural study. Biochemistry, 2005, 44(40), 13354-13364.
    • (2005) Biochemistry , vol.44 , Issue.40 , pp. 13354-13364
    • Buzon, V.1    Padros, E.2    Cladera, J.3
  • 35
    • 24044479637 scopus 로고    scopus 로고
    • Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi-and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy
    • Castano, S.; Desbat, B. Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi-and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy. Biochim. Biophys. Acta, 2005, 1715(2), 81-95.
    • (2005) Biochim. Biophys. Acta , vol.1715 , Issue.2 , pp. 81-95
    • Castano, S.1    Desbat, B.2
  • 36
    • 34247209161 scopus 로고    scopus 로고
    • A critical evaluation of the conformational requirements of fusogenic peptides in membranes
    • Reichert, J.; Grasnick, D.; Afonin, S.; Buerck, J.; Wadhwani, P.; Ulrich, A.S. A critical evaluation of the conformational requirements of fusogenic peptides in membranes. Eur. Biophys. J., 2007, 36(4-5), 405-413.
    • (2007) Eur. Biophys. J. , vol.36 , Issue.4-5 , pp. 405-413
    • Reichert, J.1    Grasnick, D.2    Afonin, S.3    Buerck, J.4    Wadhwani, P.5    Ulrich, A.S.6
  • 37
    • 34248153097 scopus 로고    scopus 로고
    • Structural malleability of plasticins: Preorganized conformations in solution and relevance for antimicrobial activity
    • Bruston, F.; Lacombe, C.; Zimmermann, K.; Piesse, C.; Nicolas, P.; El Amri, C. Structural malleability of plasticins: preorganized conformations in solution and relevance for antimicrobial activity. Biopolymers, 2007, 86(1), 42-56.
    • (2007) Biopolymers , vol.86 , Issue.1 , pp. 42-56
    • Bruston, F.1    Lacombe, C.2    Zimmermann, K.3    Piesse, C.4    Nicolas, P.5    El Amri, C.6
  • 38
    • 35748933858 scopus 로고    scopus 로고
    • Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility
    • El Amri, C.; Bruston, F.; Joanne, P.; Lacombe, C.; Nicolas, P. Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility. Eur. Biophys. J., 2007, 36(8), 901-909.
    • (2007) Eur. Biophys. J. , vol.36 , Issue.8 , pp. 901-909
    • El Amri, C.1    Bruston, F.2    Joanne, P.3    Lacombe, C.4    Nicolas, P.5
  • 39
    • 0037472811 scopus 로고    scopus 로고
    • Antibacterial activity of peptides derived from envelope glycoproteins of HIV-1
    • Cole, A.M.; Liao, H.I.; Ganz, T.; Yang, O.O. Antibacterial activity of peptides derived from envelope glycoproteins of HIV-1. FEBS Lett., 2003, 535(1-3), 195-199.
    • (2003) FEBS Lett. , vol.535 , Issue.1-3 , pp. 195-199
    • Cole, A.M.1    Liao, H.I.2    Ganz, T.3    Yang, O.O.4
  • 41
    • 34249988514 scopus 로고    scopus 로고
    • Aggregation and hemi-fusion of anionic vesicles induced by the antimicrobial peptide cryptdin-4
    • Cummings, J.E.; Vanderlick, T.K. Aggregation and hemi-fusion of anionic vesicles induced by the antimicrobial peptide cryptdin-4. Biochim. Biophys. Acta, 2007, 1768(7), 1796-1804.
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.7 , pp. 1796-1804
    • Cummings, J.E.1    Vanderlick, T.K.2
  • 42
    • 11244292022 scopus 로고    scopus 로고
    • Immunocontinuum: Perspectives in antimicrobial peptide mechanisms of action and resistance
    • Yount, N.Y.; Yeaman, M.R. Immunocontinuum: perspectives in antimicrobial peptide mechanisms of action and resistance. Protein Pept. Lett., 2005, 12(1), 49-67.
    • (2005) Protein Pept. Lett. , vol.12 , Issue.1 , pp. 49-67
    • Yount, N.Y.1    Yeaman, M.R.2
  • 43
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z.; Lerman, J.C.; Gudmundsson, G.H.; Agerberth, B.; Shai, Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J., 1999, 341(Pt. 3), 501-513.
    • (1999) Biochem. J. , vol.341 , Issue.PT. 3 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 44
    • 0346057944 scopus 로고    scopus 로고
    • Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization
    • Lau, W.L.; Ege, D.S.; Lear, J.D.; Hammer, D.A.; DeGrado, W.F. Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization. Biophys. J., 2004, 86(1Pt 1), 272-284.
    • (2004) Biophys. J. , vol.86 , Issue.1 PT 1 , pp. 272-284
    • Lau, W.L.1    Ege, D.S.2    Lear, J.D.3    Hammer, D.A.4    DeGrado, W.F.5
  • 45
    • 33845480990 scopus 로고    scopus 로고
    • Configuration of influenza hemagglutinin fusion peptide monomers and oligomers in membranes
    • Sammalkorpi, M.; Lazaridis, T. Configuration of influenza hemagglutinin fusion peptide monomers and oligomers in membranes. Biochim. Biophys. Acta, 2007, 1768(1), 30-38.
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.1 , pp. 30-38
    • Sammalkorpi, M.1    Lazaridis, T.2
  • 46
  • 48
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • Glukhov, E.; Stark, M.; Burrows, L.L.; Deber, C.M. Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. J. Biol. Chem., 2005, 280(40), 33960-33967.
    • (2005) J. Biol. Chem. , vol.280 , Issue.40 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 49
    • 17844363968 scopus 로고    scopus 로고
    • Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR
    • Glaser, R.W.; Sachse, C.; Durr, U.H.; Wadhwani, P.; Afonin, S.; Strandberg, E.; Ulrich, A.S. Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR. Biophys. J., 2005, 88(5), 3392-3397.
    • (2005) Biophys. J. , vol.88 , Issue.5 , pp. 3392-3397
    • Glaser, R.W.1    Sachse, C.2    Durr, U.H.3    Wadhwani, P.4    Afonin, S.5    Strandberg, E.6    Ulrich, A.S.7
  • 50
    • 42949144745 scopus 로고    scopus 로고
    • Threedimensional structure of the two peptides that constitute the twopeptide bacteriocin lactococcin G
    • Rogne, P.; Fimland, G.; Nissen-Meyer, J.; Kristiansen, P.E. Threedimensional structure of the two peptides that constitute the twopeptide bacteriocin lactococcin G. Biochim. Biophys. Acta, 2008, 1784(3), 543-554.
    • (2008) Biochim. Biophys. Acta , vol.1784 , Issue.3 , pp. 543-554
    • Rogne, P.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 51
    • 33646176601 scopus 로고    scopus 로고
    • Mutations of conserved glycine residues within the membrane-spanning domain of human immunodeficiency virus type 1 gp41 can inhibit membrane fusion and incorporation of Env onto virions
    • Miyauchi, K.; Curran, R.; Matthews, E.; Komano, J.; Hoshino, T.; Engelman, D.M.; Matsuda, Z. Mutations of conserved glycine residues within the membrane-spanning domain of human immunodeficiency virus type 1 gp41 can inhibit membrane fusion and incorporation of Env onto virions. Jpn. J. Infect. Dis., 2006, 59(2), 77-84.
    • (2006) Jpn. J. Infect. Dis. , vol.59 , Issue.2 , pp. 77-84
    • Miyauchi, K.1    Curran, R.2    Matthews, E.3    Komano, J.4    Hoshino, T.5    Engelman, D.M.6    Matsuda, Z.7
  • 52
    • 33749001207 scopus 로고    scopus 로고
    • A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain
    • Arbely, E.; Granot, Z.; Kass, I.; Orly, J.; Arkin, I.T. A trimerizing GxxxG motif is uniquely inserted in the severe acute respiratory syndrome (SARS) coronavirus spike protein transmembrane domain. Biochemistry, 2006, 45(38), 11349-11356.
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11349-11356
    • Arbely, E.1    Granot, Z.2    Kass, I.3    Orly, J.4    Arkin, I.T.5
  • 53
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley, D.Z.; Lenard, J. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. USA, 1998, 95(7), 3425-3430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.7 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 54
    • 36549031235 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in the study of lipid phase transitions in model and biological membranes: Practical considerations
    • Lewis, R.N.; McElhaney, R.N. Fourier transform infrared spectroscopy in the study of lipid phase transitions in model and biological membranes: practical considerations. Methods Mol. Biol., 2007, 400, 207-226.
    • (2007) Methods Mol. Biol. , vol.400 , pp. 207-226
    • Lewis, R.N.1    McElhaney, R.N.2
  • 56
    • 36549019514 scopus 로고    scopus 로고
    • Differential scanning calorimetry in the study of lipid phase transitions in model and biological membranes: Practical considerations
    • Lewis, R.N.; Mannock, D.A.; McElhaney, R.N. Differential scanning calorimetry in the study of lipid phase transitions in model and biological membranes: practical considerations. Methods Mol. Biol., 2007, 400, 171-195.
    • (2007) Methods Mol. Biol. , vol.400 , pp. 171-195
    • Lewis, R.N.1    Mannock, D.A.2    McElhaney, R.N.3
  • 57
    • 0022872025 scopus 로고
    • Parameters affecting fusion between Sendai virus and liposomes. Role of viral proteins, liposome composition, and pH
    • Klappe, K.; Wilschut, J.; Nir, S.; Hoekstra, D. Parameters affecting fusion between Sendai virus and liposomes. Role of viral proteins, liposome composition, and pH. Biochemistry, 1986, 25(25), 8252-8260.
    • (1986) Biochemistry , vol.25 , Issue.25 , pp. 8252-8260
    • Klappe, K.1    Wilschut, J.2    Nir, S.3    Hoekstra, D.4
  • 58
    • 0021199076 scopus 로고
    • Effect of lipid composition upon fusion of liposomes with Sendai virus membranes
    • Haywood, A.M.; Boyer, B.P. Effect of lipid composition upon fusion of liposomes with Sendai virus membranes. Biochemistry, 1984, 23(18), 4161-4166.
    • (1984) Biochemistry , vol.23 , Issue.18 , pp. 4161-4166
    • Haywood, A.M.1    Boyer, B.P.2
  • 59
    • 0026758906 scopus 로고
    • Asymmetric fusion between synthetic di-n-dodecylphosphate vesicles and virus membranes
    • Fonteijn, T.A.; Engberts, J.B.; Nir, S.; Hoekstra, D. Asymmetric fusion between synthetic di-n-dodecylphosphate vesicles and virus membranes. Biochim. Biophys. Acta, 1992, 1110(2), 185-192.
    • (1992) Biochim. Biophys. Acta , vol.1110 , Issue.2 , pp. 185-192
    • Fonteijn, T.A.1    Engberts, J.B.2    Nir, S.3    Hoekstra, D.4
  • 60
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as modulators of membrane fusion mediated by viral fusion proteins
    • Teissier, E.; Pecheur, E.I. Lipids as modulators of membrane fusion mediated by viral fusion proteins. Eur. Biophys. J., 2007, 36(8), 887-899.
    • (2007) Eur. Biophys. J. , vol.36 , Issue.8 , pp. 887-899
    • Teissier, E.1    Pecheur, E.I.2
  • 62
    • 33845929560 scopus 로고    scopus 로고
    • Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. importance of the membrane dipole potential
    • Buzon, V.; Cladera, J. Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. importance of the membrane dipole potential. Biochemistry, 2006, 45(51), 15768-15775.
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15768-15775
    • Buzon, V.1    Cladera, J.2
  • 63
    • 8844228894 scopus 로고    scopus 로고
    • HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers: Putative correlation with improved efficiency
    • Veiga, A.S.; Santos, N.C.; Loura, L.M.; Fedorov, A.; Castanho, M.A. HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers: putative correlation with improved efficiency. J. Am. Chem. Soc., 2004, 126(45), 14758-14763.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.45 , pp. 14758-14763
    • Veiga, A.S.1    Santos, N.C.2    Loura, L.M.3    Fedorov, A.4    Castanho, M.A.5
  • 64
    • 0034462310 scopus 로고    scopus 로고
    • Modulation of membrane curvature by peptides
    • Epand, R.M.; Epand, R.F. Modulation of membrane curvature by peptides. Biopolymers., 2000, 55(5), 358-363.
    • (2000) Biopolymers. , vol.55 , Issue.5 , pp. 358-363
    • Epand, R.M.1    Epand, R.F.2
  • 65
    • 0034730436 scopus 로고    scopus 로고
    • Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms
    • Siegel, D.P.; Epand, R.M. Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms. Biochim. Biophys. Acta, 2000, 1468(1-2), 87-98.
    • (2000) Biochim. Biophys. Acta , vol.1468 , Issue.1-2 , pp. 87-98
    • Siegel, D.P.1    Epand, R.M.2
  • 67
    • 0035881708 scopus 로고    scopus 로고
    • Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    • Cross, K.J.; Wharton, S.A.; Skehel, J.J.; Wiley, D.C.; Steinhauer, D.A. Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics. EMBO J., 2001, 20(16), 4432-4442.
    • (2001) EMBO J. , vol.20 , Issue.16 , pp. 4432-4442
    • Cross, K.J.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Steinhauer, D.A.5
  • 68
    • 0028023386 scopus 로고
    • Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers
    • Epand, R.M.; Epand, R.F. Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochem. Biophys. Res. Commun., 1994, 202(3), 1420-1425.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , Issue.3 , pp. 1420-1425
    • Epand, R.M.1    Epand, R.F.2
  • 69
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K.A.; Lee, D.K.; Ramamoorthy, A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry, 2003, 42(21), 6545-6558.
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 70
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock, K.J.; Lee, D.K.; Ramamoorthy, A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J., 2003, 84(5), 3052-3060.
    • (2003) Biophys. J. , vol.84 , Issue.5 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 72
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang, S.; Zhao, Q.; Debnath, A.K. Peptide and non-peptide HIV fusion inhibitors. Curr. Pharm. Des., 2002, 8(8), 563-580.
    • (2002) Curr. Pharm. Des. , vol.8 , Issue.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 73
    • 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.; Qi, Z.; Lu, H.; Dong, M.; Jiang, S.; Dai, Q. 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(13), 6349-6358.
    • (2008) J. Virol. , vol.82 , Issue.13 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3    Qi, Z.4    Lu, H.5    Dong, M.6    Jiang, S.7    Dai, Q.8
  • 74
    • 0032560463 scopus 로고    scopus 로고
    • A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion
    • Pritsker, M.; Jones, P.; Blumenthal, R.; Shai, Y. A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion. Proc. Natl. Acad. Sci. USA, 1998, 95(13), 7287-7292.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.13 , pp. 7287-7292
    • Pritsker, M.1    Jones, P.2    Blumenthal, R.3    Shai, Y.4
  • 76
    • 34347378496 scopus 로고    scopus 로고
    • HIV entry inhibitors
    • Este, J.A.; Telenti, A. HIV entry inhibitors. Lancet, 2007, 370(9581), 81-88.
    • (2007) Lancet , vol.370 , Issue.9581 , pp. 81-88
    • Este, J.A.1    Telenti, A.2
  • 78
    • 27144491977 scopus 로고    scopus 로고
    • Frog skin yields antiviral peptides
    • Thomas, C. Frog skin yields antiviral peptides. Nat. Med., 2005, 11(10), 1046.
    • (2005) Nat. Med. , vol.11 , Issue.10 , pp. 1046
    • Thomas, C.1
  • 79
    • 0036137074 scopus 로고    scopus 로고
    • In. vitro antiviral activity of dermaseptins against herpes simplex virus type 1
    • Belaid, A.; Aouni, M.; Khelifa, R.; Trabelsi, A.; Jemmali, M.; Hani, K. In. vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol., 2002, 66(2), 229-234.
    • (2002) J. Med. Virol. , vol.66 , Issue.2 , pp. 229-234
    • Belaid, A.1    Aouni, M.2    Khelifa, R.3    Trabelsi, A.4    Jemmali, M.5    Hani, K.6
  • 81
    • 34548138936 scopus 로고    scopus 로고
    • Apolipoprotein Ederived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity
    • Kelly, B.A.; Neil, S.J.; McKnight, A.; Santos, J.M.; Sinnis, P.; Jack, E.R.; Middleton, D.A.; Dobson, C.B. Apolipoprotein Ederived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity. FEBS J., 2007, 274(17), 4511-4525.
    • (2007) FEBS J. , vol.274 , Issue.17 , pp. 4511-4525
    • Kelly, B.A.1    Neil, S.J.2    McKnight, A.3    Santos, J.M.4    Sinnis, P.5    Jack, E.R.6    Middleton, D.A.7    Dobson, C.B.8
  • 82
    • 25444466265 scopus 로고    scopus 로고
    • Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition
    • Abrunhosa, F.; Faria, S.; Gomes, P.; Tomaz, I.; Pessoa, J.C.; Andreu, D.; Bastos, M. Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition. J. Phys. Chem. B, 2005, 109(36), 17311-17319.
    • (2005) J. Phys. Chem. B , vol.109 , Issue.36 , pp. 17311-17319
    • Abrunhosa, F.1    Faria, S.2    Gomes, P.3    Tomaz, I.4    Pessoa, J.C.5    Andreu, D.6    Bastos, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.