메뉴 건너뛰기




Volumn 53, Issue 12, 2013, Pages 3280-3296

Engineering antimicrobial peptides with improved antimicrobial and hemolytic activities

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOACTIVITY; BLOOD; CELLS; FREE ENERGY; HEALTH RISKS; LIPID BILAYERS; MOLECULAR DYNAMICS;

EID: 84896510367     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci400477e     Document Type: Article
Times cited : (89)

References (69)
  • 1
    • 84886709888 scopus 로고    scopus 로고
    • Antimicrobial Peptides
    • In; John Wiley & Sons, Inc. New York - 225
    • Marcos, J. F.; Manzanares, P. Antimicrobial Peptides. In Antimicrobial Polymers; John Wiley & Sons, Inc.: New York, 2011; pp 195-225.
    • (2011) Antimicrobial Polymers , pp. 195
    • Marcos, J.F.1    Manzanares, P.2
  • 2
    • 14944375311 scopus 로고    scopus 로고
    • New targets and screening approaches in antimicrobial drug discovery
    • Brown, E. D.; Wright, G. D. New targets and screening approaches in antimicrobial drug discovery Chem. Rev. 2005, 105, 759-774
    • (2005) Chem. Rev. , vol.105 , pp. 759-774
    • Brown, E.D.1    Wright, G.D.2
  • 3
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley, W. C. Describing the mechanism of antimicrobial peptide action with the interfacial activity model ACS Chem. Biol. 2010, 5, 905-917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 4
    • 0026760182 scopus 로고
    • The crisis in antibiotic-resistance
    • Neu, H. C. The crisis in antibiotic-resistance Science 1992, 257, 1064-1073
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 7
    • 33645505791 scopus 로고    scopus 로고
    • Solid-state NMR studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities
    • Hong, M. Solid-state NMR studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities Acc. Chem. Res. 2006, 39, 176-183
    • (2006) Acc. Chem. Res. , vol.39 , pp. 176-183
    • Hong, M.1
  • 9
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. W.; Sahl, H. G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 2006, 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 10
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E. W.; Lehrer, R. Cationic peptides: a new source of antibiotics Trends Biotechnol. 1998, 16, 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 11
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale, J. D. F.; Hancock, R. E. W. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria Expert Rev. Anti Infect. Ther. 2007, 5, 951-959
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.F.1    Hancock, R.E.W.2
  • 12
    • 77949346087 scopus 로고    scopus 로고
    • Structure-Activity Relationships of Polymyxin Antibiotics
    • Velkov, T.; Thompson, P. E.; Nation, R. L.; Li, J. Structure-Activity Relationships of Polymyxin Antibiotics J. Med. Chem. 2009, 53, 1898-1916
    • (2009) J. Med. Chem. , vol.53 , pp. 1898-1916
    • Velkov, T.1    Thompson, P.E.2    Nation, R.L.3    Li, J.4
  • 13
    • 75449102744 scopus 로고    scopus 로고
    • De Novo design of antimicrobial polymers, foldamers, and small Molecules: From discovery to practical applications
    • Tew, G. N.; Scott, R. W.; Klein, M. L.; DeGrado, W. F. De Novo design of antimicrobial polymers, foldamers, and small Molecules: from discovery to practical applications Acc. Chem. Res. 2009, 43, 30-39
    • (2009) Acc. Chem. Res. , vol.43 , pp. 30-39
    • Tew, G.N.1    Scott, R.W.2    Klein, M.L.3    Degrado, W.F.4
  • 14
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople, V.; Krukemeyer, A.; Ramamoorthy, A. The human beta-defensin-3, an antibacterial peptide with multiple biological functions Biochim. Biophys. Acta, Biomembr. 2006, 1758, 1499-1512
    • (2006) Biochim. Biophys. Acta, Biomembr. , vol.1758 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 15
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F.-Y.; Lee, M.-T.; Huang, H. W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 2003, 84, 3751-3758
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 16
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 2005, 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 17
    • 33745747109 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin
    • Ramamoorthy, A.; Thennarasu, S.; Lee, D.-K.; Tan, A.; Maloy, L. Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin Biophys. J. 2006, 91, 206-216
    • (2006) Biophys. J. , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.-K.3    Tan, A.4    Maloy, L.5
  • 18
    • 70350450689 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Functional and mechanistic insights from NMR structures of potent antimicrobial peptides
    • Bhattacharjya, S.; Ramamoorthy, A. Multifunctional host defense peptides: functional and mechanistic insights from NMR structures of potent antimicrobial peptides FEBS J. 2009, 276, 6465-6473
    • (2009) FEBS J. , vol.276 , pp. 6465-6473
    • Bhattacharjya, S.1    Ramamoorthy, A.2
  • 19
    • 74249106455 scopus 로고    scopus 로고
    • Cholesterol reduces pardaxin's dynamics - A barrel-stave mechanism of membrane disruption investigated by solid-state NMR
    • Ramamoorthy, A.; Lee, D.-K.; Narasimhaswamy, T.; Nanga, R. P. R. Cholesterol reduces pardaxin's dynamics-a barrel-stave mechanism of membrane disruption investigated by solid-state NMR Biochim. Biophys. Acta, Biomembr. 2010, 1798, 223-227
    • (2010) Biochim. Biophys. Acta, Biomembr. , vol.1798 , pp. 223-227
    • Ramamoorthy, A.1    Lee, D.-K.2    Narasimhaswamy, T.3    Nanga, R.P.R.4
  • 20
    • 79953186604 scopus 로고    scopus 로고
    • Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR
    • Hong, M.; Su, Y. Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR Protein Sci. 2011, 20, 641-655
    • (2011) Protein Sci. , vol.20 , pp. 641-655
    • Hong, M.1    Su, Y.2
  • 21
    • 45549085024 scopus 로고    scopus 로고
    • Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy
    • Tang, M.; Waring, A. J.; Lehrer, R. L.; Hong, M. Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy Angew. Chem., Int. Ed. 2008, 47, 3202-3205
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 3202-3205
    • Tang, M.1    Waring, A.J.2    Lehrer, R.L.3    Hong, M.4
  • 22
    • 33748940617 scopus 로고    scopus 로고
    • SFG studies on interactions between antimicrobial peptides and supported lipid bilayers
    • Chen, X.; Chen, Z. SFG studies on interactions between antimicrobial peptides and supported lipid bilayers Biochim. Biophys. Acta, Biomembr. 2006, 1758, 1257-1273
    • (2006) Biochim. Biophys. Acta, Biomembr. , vol.1758 , pp. 1257-1273
    • Chen, X.1    Chen, Z.2
  • 23
    • 70449885926 scopus 로고    scopus 로고
    • Dependence of Antimicrobial Selectivity and Potency on Oligomer Structure Investigated Using Substrate Supported Lipid Bilayers and Sum Frequency Generation Vibrational Spectroscopy
    • Avery, C. W.; Som, A.; Xu, Y.; Tew, G. N.; Chen, Z. Dependence of Antimicrobial Selectivity and Potency on Oligomer Structure Investigated Using Substrate Supported Lipid Bilayers and Sum Frequency Generation Vibrational Spectroscopy Anal. Chem. 2009, 81, 8365-8372
    • (2009) Anal. Chem. , vol.81 , pp. 8365-8372
    • Avery, C.W.1    Som, A.2    Xu, Y.3    Tew, G.N.4    Chen, Z.5
  • 24
    • 0033592458 scopus 로고    scopus 로고
    • CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix
    • Ladokhin, A. S.; Selsted, M. E.; White, S. H. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix Biochemistry (Moscow) 1999, 38, 12313-12319
    • (1999) Biochemistry (Moscow) , vol.38 , pp. 12313-12319
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 25
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner, J.; Cho, Y.; Dinh, N. N.; Waring, A. J.; Lehrer, R. I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils Antimicrob. Agents Chemother. 1998, 42, 2206-2214
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 26
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J.; Gudmundsson, G. H.; Rottenberg, M. E.; Berndt, K. D.; Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37 J. Biol. Chem. 1998, 273, 3718-3724
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 27
    • 0031022395 scopus 로고    scopus 로고
    • Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids
    • Ladokhin, A. S.; Selsted, M. E.; White, S. H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids Biophys. J. 1997, 72, 794-805
    • (1997) Biophys. J. , vol.72 , pp. 794-805
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 28
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C.; White, S. H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 1996, 3, 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 29
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White, S. H.; Wimley, W. C. Membrane protein folding and stability: Physical principles Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 30
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin
    • Ladokhin, A. S.; White, S. H. Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin J. Mol. Biol. 1999, 285, 1363-1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 31
    • 84856725828 scopus 로고    scopus 로고
    • Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants
    • Kyrychenko, A.; Rodnin, M. V.; Posokhov, Y. O.; Holt, A.; Pucci, B.; Killian, J. A.; Ladokhin, A. S. Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants J. Mol. Biol. 2012, 416, 328-334
    • (2012) J. Mol. Biol. , vol.416 , pp. 328-334
    • Kyrychenko, A.1    Rodnin, M.V.2    Posokhov, Y.O.3    Holt, A.4    Pucci, B.5    Killian, J.A.6    Ladokhin, A.S.7
  • 32
    • 58149181485 scopus 로고    scopus 로고
    • Lipids on the move: Simulations of membrane pores, domains, stalks and curves
    • Marrink, S. J.; de Vries, A. H.; Tieleman, D. P. Lipids on the move: Simulations of membrane pores, domains, stalks and curves Biochim. Biophys. Acta, Biomembr. 2009, 1788, 149-168
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , pp. 149-168
    • Marrink, S.J.1    De Vries, A.H.2    Tieleman, D.P.3
  • 34
    • 36248932202 scopus 로고    scopus 로고
    • Computer simulation of antimicrobial peptides
    • Matyus, E.; Kandt, C.; Tieleman, D. P. Computer simulation of antimicrobial peptides Curr. Med. Chem. 2007, 14, 2789-2798
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2789-2798
    • Matyus, E.1    Kandt, C.2    Tieleman, D.P.3
  • 35
    • 58149144259 scopus 로고    scopus 로고
    • Coarse-Grained Simulation Studies of Peptide-Induced Pore Formation
    • Illya, G.; Deserno, M. Coarse-Grained Simulation Studies of Peptide-Induced Pore Formation Biophys. J. 2008, 95, 4163-4173
    • (2008) Biophys. J. , vol.95 , pp. 4163-4173
    • Illya, G.1    Deserno, M.2
  • 36
    • 84865318587 scopus 로고    scopus 로고
    • Binding and reorientation of melittin in a POPC bilayer: Computer simulations
    • Irudayam, S. J.; Berkowitz, M. L. Binding and reorientation of melittin in a POPC bilayer: Computer simulations Biochim. Biophys. Acta, Biomembr. 2012, 1818, 2975-2981
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 2975-2981
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 37
    • 34547653932 scopus 로고    scopus 로고
    • Real-time structural investigation of a lipid bilayer during its interaction with melittin using sum frequency generation vibrational spectroscopy
    • Chen, X.; Wang, J.; Kristalyn, C. B.; Chen, Z. Real-time structural investigation of a lipid bilayer during its interaction with melittin using sum frequency generation vibrational spectroscopy Biophys. J. 2007, 93, 866-875
    • (2007) Biophys. J. , vol.93 , pp. 866-875
    • Chen, X.1    Wang, J.2    Kristalyn, C.B.3    Chen, Z.4
  • 38
    • 34347229452 scopus 로고    scopus 로고
    • De novo design of selective antibiotic peptides by incorporation of unnatural amino acids
    • Hicks, R. P.; Bhonsle, J. B.; Venugopal, D.; Koser, B. W.; Magill, A. J. De novo design of selective antibiotic peptides by incorporation of unnatural amino acids J. Med. Chem. 2007, 50, 3026-3036
    • (2007) J. Med. Chem. , vol.50 , pp. 3026-3036
    • Hicks, R.P.1    Bhonsle, J.B.2    Venugopal, D.3    Koser, B.W.4    Magill, A.J.5
  • 39
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • Dathe, M.; Wieprecht, T.; Nikolenko, H.; Handel, L.; Maloy, W. L.; MacDonald, D. L.; Beyermann, M.; Bienert, M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides FEBS Lett. 1997, 403, 208-212
    • (1997) FEBS Lett. , vol.403 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    Macdonald, D.L.6    Beyermann, M.7    Bienert, M.8
  • 40
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle, S. E.; Houghten, R. A. Design of model amphipathic peptides having potent antimicrobial activities Biochemistry (Moscow) 1992, 31, 12688-12694
    • (1992) Biochemistry (Moscow) , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 41
    • 0031005930 scopus 로고    scopus 로고
    • A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity
    • Oren, Z.; Hong, J.; Shai, Y. A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity J. Biol. Chem. 1997, 272, 14643-14649
    • (1997) J. Biol. Chem. , vol.272 , pp. 14643-14649
    • Oren, Z.1    Hong, J.2    Shai, Y.3
  • 42
    • 0029665072 scopus 로고    scopus 로고
    • Diastereomers of cytolysins, a novel class of potent antibacterial peptides
    • Shai, Y.; Oren, Z. Diastereomers of cytolysins, a novel class of potent antibacterial peptides J. Biol. Chem. 1996, 271, 7305-7308
    • (1996) J. Biol. Chem. , vol.271 , pp. 7305-7308
    • Shai, Y.1    Oren, Z.2
  • 43
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • Oren, Z.; Shai, Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study Biochemistry (Moscow) 1997, 36, 1826-1835
    • (1997) Biochemistry (Moscow) , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 44
    • 34249858459 scopus 로고    scopus 로고
    • AMPer: A database and an automated discovery tool for antimicrobial peptides
    • Fjell, C. D.; Hancock, R. E. W.; Cherkasov, A. AMPer: a database and an automated discovery tool for antimicrobial peptides Bioinformatics 2007, 23, 1148-1155
    • (2007) Bioinformatics , vol.23 , pp. 1148-1155
    • Fjell, C.D.1    Hancock, R.E.W.2    Cherkasov, A.3
  • 45
    • 0347755460 scopus 로고    scopus 로고
    • APD: The Antimicrobial Peptide Database
    • Wang, Z.; Wang, G. S. APD: the Antimicrobial Peptide Database Nucleic Acids Res. 2004, 32, D590-D592
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.S.2
  • 47
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo, D.; Skerlavaj, B.; Bolognesi, M.; Gennaro, R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils J. Biol. Chem. 1988, 263, 9573-9575
    • (1988) J. Biol. Chem. , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 48
    • 0032907969 scopus 로고    scopus 로고
    • Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide
    • Wu, M. H.; Hancock, R. E. W. Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide Antimicrob. Agents Chemother. 1999, 43, 1274-1276
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1274-1276
    • Wu, M.H.1    Hancock, R.E.W.2
  • 49
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert, K.; Volkmer-Engert, R.; Walter, T.; Hancock, R. E. W. High-throughput generation of small antibacterial peptides with improved activity Nat. Biotechnol. 2005, 23, 1008-1012
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 50
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 51
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan, W. Molecular basis for membrane phospholipid diversity: Why are there so many lipids? Annu. Rev. Biochem. 1997, 66, 199-232
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 52
    • 0035879913 scopus 로고    scopus 로고
    • Analysis of phospholipid species in human blood using normal-phase liquid chromatography coupled with electrospray ionization ion-trap tandem mass spectrometry
    • Uran, S.; Larsen, A.; Jacobsen, P. B.; Skotland, T. Analysis of phospholipid species in human blood using normal-phase liquid chromatography coupled with electrospray ionization ion-trap tandem mass spectrometry J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2001, 758, 265-275
    • (2001) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.758 , pp. 265-275
    • Uran, S.1    Larsen, A.2    Jacobsen, P.B.3    Skotland, T.4
  • 54
    • 84878034291 scopus 로고    scopus 로고
    • Molecular interactions of Alzheimer amyloid-beta oligomers with neutral and negatively charged lipid bilayers
    • Yu, X.; Wang, Q.; Pan, Q.; Zhou, F.; Zheng, J. Molecular interactions of Alzheimer amyloid-beta oligomers with neutral and negatively charged lipid bilayers Phys. Chem. Chem. Phys. 2013, 15, 8878-8889
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 8878-8889
    • Yu, X.1    Wang, Q.2    Pan, Q.3    Zhou, F.4    Zheng, J.5
  • 55
    • 34548788549 scopus 로고    scopus 로고
    • Models of {beta}-amyloid ion-channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • Jang, H.; Zheng, J.; Nussinov, R. Models of {beta}-amyloid ion-channels in the membrane suggest that channel formation in the bilayer is a dynamic process Biophys. J. 2007, 93, 1938-1949
    • (2007) Biophys. J. , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 56
    • 84864281394 scopus 로고    scopus 로고
    • Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer
    • Yu, X.; Zheng, J. Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer J. Mol. Biol. 2012, 421, 561-571
    • (2012) J. Mol. Biol. , vol.421 , pp. 561-571
    • Yu, X.1    Zheng, J.2
  • 57
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • Nugent, T.; Jones, D. Transmembrane protein topology prediction using support vector machines BMC Bioinf. 2009, 10, 159
    • (2009) BMC Bioinf. , vol.10 , pp. 159
    • Nugent, T.1    Jones, D.2
  • 58
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • Jones, D. T. Improving the accuracy of transmembrane protein topology prediction using evolutionary information Bioinformatics 2007, 23, 538-544
    • (2007) Bioinformatics , vol.23 , pp. 538-544
    • Jones, D.T.1
  • 59
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J.; de Vries, A. H.; Mark, A. E. Coarse grained model for semiquantitative lipid simulations J. Phys. Chem. B 2004, 108, 750-760
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 60
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar, S.; Rosenberg, J. M.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method J. Comput. Chem. 1992, 13, 1011-1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 62
    • 78651282170 scopus 로고    scopus 로고
    • G-wham - A free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • Hub, J. S.; de Groot, B. L.; van der Spoel, D. g-wham-A free weighted histogram analysis implementation including robust error and autocorrelation estimates J. Chem. Theory Comput. 2010, 6, 3713-3720
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 3713-3720
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 69
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 1982, 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.