메뉴 건너뛰기




Volumn 39, Issue 2, 2010, Pages 263-276

Biophysical studies of the interactions between the phage φ KZ gp144 lytic transglycosylase and model membranes

Author keywords

Antimicrobials; Endolysins; Fluorescence; Infrared; NMR; Spectroscopy

Indexed keywords

CIRCULAR DICHROISM; DIMYRISTOYLPHOSPHATIDYLCHOLINE; FLUORESCEINS; FLUORESCENCE; GLYCOSYLTRANSFERASES; LIPID BILAYERS; MEMBRANE LIPIDS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHATIDYLGLYCEROLS; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS PHAGES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; UNILAMELLAR LIPOSOMES; VIBRATION;

EID: 73649114944     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0530-1     Document Type: Article
Times cited : (7)

References (76)
  • 1
    • 0038392706 scopus 로고    scopus 로고
    • Bacteriophage observations and evolution
    • DOI 10.1016/S0923-2508(03)00067-6
    • HW Ackermann 2003 Bacteriophage observations and evolution Res Microbiol 154 245 251 10.1016/S0923-2508(03)00067-6 12798228 1:CAS:528: DC%2BD3sXkt1ymur4%3D (Pubitemid 36645270)
    • (2003) Research in Microbiology , vol.154 , Issue.4 , pp. 245-251
    • Ackermann, H.-W.1
  • 2
    • 3042546066 scopus 로고    scopus 로고
    • Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin
    • DOI 10.1016/j.bbamem.2004.03.013, PII S0005273604000938
    • EE Ambroggio F Separovic J Bowie GD Fidelio 2004 Surface behaviour and peptide-lipid interactions of the antibiotic peptides, maculatin and citropin Biochim Biophys Acta 1664 31 37 10.1016/j.bbamem.2004.03.013 15238255 1:CAS:528:DC%2BD2cXlt1Wnsrw%3D (Pubitemid 38829314)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1664 , Issue.1 , pp. 31-37
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.3    Fidelio, G.D.4
  • 3
    • 12144253365 scopus 로고    scopus 로고
    • Temperature and pressure dependent growth and morphology of DMPC/DSPC domains studied by Brewster angle microscopy
    • DOI 10.1016/j.chemphyslip.2004.09.020, PII S0009308404001550
    • A Arnold I Cloutier AM Ritcey M Auger 2005 Temperature and pressure dependent growth and morphology of DMPC/DSPC domains studied by Brewster angle microscopy Chem Phys Lipids 133 165 179 10.1016/j.chemphyslip.2004.09.020 15642585 1:CAS:528:DC%2BD2MXisF2gsA%3D%3D (Pubitemid 40103503)
    • (2005) Chemistry and Physics of Lipids , vol.133 , Issue.2 , pp. 165-179
    • Arnold, A.1    Cloutier, I.2    Ritcey, A.M.3    Auger, M.4
  • 4
    • 0032211895 scopus 로고    scopus 로고
    • Infrared studies of protein-induced perturbation of lipids in lipoproteins and membranes
    • DOI 10.1016/S0009-3084(98)00080-2, PII S0009308498000802
    • JL Arrondo FM Goni 1998 Infrared studies of protein-induced perturbation of lipids in lipoproteins and membranes Chem Phys Lipids 96 53 68 10.1016/S0009-3084(98)00080-2 9871982 1:CAS:528:DyaK1cXntVyhsbk%3D (Pubitemid 28517898)
    • (1998) Chemistry and Physics of Lipids , vol.96 , Issue.1-2 , pp. 53-68
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 5
    • 0024283054 scopus 로고
    • The solution structure of concanavalin A probed by FT-IR spectroscopy
    • 3337827 1:CAS:528:DyaL1cXht1Ojt7o%3D
    • JL Arrondo NM Young HH Mantsch 1988 The solution structure of concanavalin A probed by FT-IR spectroscopy Biochim Biophys Acta 952 261 268 3337827 1:CAS:528:DyaL1cXht1Ojt7o%3D
    • (1988) Biochim Biophys Acta , vol.952 , pp. 261-268
    • Arrondo, J.L.1    Young, N.M.2    Mantsch, H.H.3
  • 6
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • DOI 10.1016/j.bbabio.2007.06.004, PII S0005272807001375
    • A Barth 2007 Infrared spectroscopy of proteins Biochim Biophys Acta 1767 1073 1101 10.1016/j.bbabio.2007.06.004 17692815 1:CAS:528:DC%2BD2sXpvFWmt7Y%3D (Pubitemid 47313388)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.9 , pp. 1073-1101
    • Barth, A.1
  • 7
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • 13641241 1:CAS:528:DyaG1MXmtlWjtg%3D%3D
    • GR Bartlett 1959 Phosphorus assay in column chromatography J Biol Chem 234 466 468 13641241 1:CAS:528:DyaG1MXmtlWjtg%3D%3D
    • (1959) J Biol Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 8
    • 0022339641 scopus 로고
    • Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization
    • DOI 10.1021/bi00346a013
    • AM Batenburg PE Bougis H Rochat AJ Verkleij B de Kruijff 1985 Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization Biochemistry 24 7101 7110 10.1021/bi00346a013 4084565 1:CAS:528:DyaL28XhvFej (Pubitemid 16165322)
    • (1985) Biochemistry , vol.24 , Issue.25 , pp. 7101-7110
    • Batenburg, A.M.1    Bougis, P.E.2    Rochat, H.3
  • 9
    • 3042620560 scopus 로고    scopus 로고
    • Structure and function of membrane-lytic peptides
    • DOI 10.1080/07352680490452825
    • B Bechinger 2004 Structure and function of membrane-lytic peptides Crit Rev Plant Sci 23 271 292 10.1080/07352680490452825 1:CAS:528: DC%2BD2cXlvFWrtLs%3D (Pubitemid 38809962)
    • (2004) Critical Reviews in Plant Sciences , vol.23 , Issue.3 , pp. 271-292
    • Bechinger, B.1
  • 10
    • 20444400818 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy study
    • DOI 10.1016/j.bbamem.2005.03.003, PII S0005273605000659
    • 31P solid-state NMR spectroscopy study Biochim Biophys Acta 1712 101 108 10.1016/j.bbamem.2005.03.003 15869740 1:CAS:528: DC%2BD2MXltFSkurw%3D (Pubitemid 40799285)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1712 , Issue.1 , pp. 101-108
    • Bechinger, B.1
  • 11
    • 33646305152 scopus 로고
    • Heteronuclear decoupling in rotating solids
    • 10.1063/1.470372 1:CAS:528:DyaK2MXovVeqtLs%3D
    • AE Bennett CM Rienstra M Auger KV Lakshmi RG Griffin 1995 Heteronuclear decoupling in rotating solids J Chem Phys 103 6951 6958 10.1063/1.470372 1:CAS:528:DyaK2MXovVeqtLs%3D
    • (1995) J Chem Phys , vol.103 , pp. 6951-6958
    • Bennett, A.E.1    Rienstra, C.M.2    Auger, M.3    Lakshmi, K.V.4    Griffin, R.G.5
  • 13
    • 0024291319 scopus 로고
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups
    • 10.1021/bi00421a038 3233207 1:CAS:528:DyaL1cXls1KjsL0%3D
    • 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups Biochemistry 27 8239 8249 10.1021/bi00421a038 3233207 1:CAS:528: DyaL1cXls1KjsL0%3D
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Hubner, W.2    Messner, G.3
  • 15
    • 33645227952 scopus 로고    scopus 로고
    • Bacteriophage endolysins as a novel class of antibacterial agents
    • 1:CAS:528:DC%2BD28Xjt1SjtLo%3D
    • J Borysowski B Weber-Dabrowska A Gorski 2006 Bacteriophage endolysins as a novel class of antibacterial agents Exp Biol Med 231 366 377 1:CAS:528:DC%2BD28Xjt1SjtLo%3D
    • (2006) Exp Biol Med , vol.231 , pp. 366-377
    • Borysowski, J.1    Weber-Dabrowska, B.2    Gorski, A.3
  • 16
    • 0019816841 scopus 로고
    • Penetration of phospholipid monolayers by cardiotoxins
    • 10.1021/bi00520a017 7295658 1:CAS:528:DyaL3MXkvFaksrg%3D
    • P Bougis H Rochat G Pieroni R Verger 1981 Penetration of phospholipid monolayers by cardiotoxins Biochemistry 20 4915 4920 10.1021/bi00520a017 7295658 1:CAS:528:DyaL3MXkvFaksrg%3D
    • (1981) Biochemistry , vol.20 , pp. 4915-4920
    • Bougis, P.1    Rochat, H.2    Pieroni, G.3    Verger, R.4
  • 17
    • 34547897398 scopus 로고    scopus 로고
    • Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages φKZ and EL
    • DOI 10.1111/j.1365-2958.2007.05870.x
    • Y Briers G Volckaert A Cornelissen S Lagaert CW Michiels K Hertveldt R Lavigne 2007 Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL Mol Microbiol 65 1334 1344 10.1111/j.1365-2958.2007.05870.x 17697255 1:CAS:528:DC%2BD2sXhtVWnurzK (Pubitemid 47262831)
    • (2007) Molecular Microbiology , vol.65 , Issue.5 , pp. 1334-1344
    • Briers, Y.1    Volckaert, G.2    Cornelissen, A.3    Lagaert, S.4    Michiels, C.W.5    Hertveldt, K.6    Lavigne, R.7
  • 18
    • 0033179620 scopus 로고    scopus 로고
    • Lipid monolayers: Why use half a membrane to characterize protein-membrane interactions?
    • DOI 10.1016/S0959-440X(99)80061-X
    • H Brockman 1999 Lipid monolayers: why use half membrane to characterize protein-membrane interactions? Curr Opin Struct Biol 9 438 443 10.1016/S0959-440X(99)80061-X 10449364 1:CAS:528:DyaK1MXlt1Cgsbs%3D (Pubitemid 29377885)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.4 , pp. 438-443
    • Brockman, H.1
  • 19
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • DOI 10.1074/jbc.R000005200
    • DA Brown E London 2000 Structure and function of sphingolipid- and cholesterol-rich membrane rafts J Biol Chem 275 17221 17224 10.1074/jbc. R000005200 10770957 1:CAS:528:DC%2BD3cXktFalu70%3D (Pubitemid 30430750)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 20
    • 0029881913 scopus 로고    scopus 로고
    • 2H NMR spectroscopic evidence
    • DOI 10.1021/bi952349i
    • 2H NMR spectroscopic evidence Biochemistry 35 3368 3378 10.1021/bi952349i 8639486 1:CAS:528:DyaK28XhtlWju7c%3D (Pubitemid 26092559)
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3368-3378
    • Carbone, M.A.1    Macdonald, P.M.2
  • 21
    • 0033634645 scopus 로고    scopus 로고
    • 31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria
    • 1:CAS:528:DC%2BD3MXit1eitA%3D%3D
    • 31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria Lett Peptide Sci 7 151 156 1:CAS:528: DC%2BD3MXit1eitA%3D%3D
    • (2000) Lett Peptide Sci , vol.7 , pp. 151-156
    • Chia, B.C.S.1    Lam, Y.H.2    Dyall-Smith, M.3    Separovic, F.4    Bowie, J.H.5
  • 22
    • 0036431716 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa in cystic fibrosis: Pathogenesis and persistence
    • DOI 10.1016/S1526-0550(02)00003-3
    • JC Davies 2002 Pseudomonas aeruginosa in cystic fibrosis: pathogenesis and persistence Paediatr Respir Rev 3 128 134 10.1016/S1526-0550(02)00003-3 12297059 (Pubitemid 35331506)
    • (2002) Paediatric Respiratory Reviews , vol.3 , Issue.2 , pp. 128-134
    • Davies, J.C.1
  • 23
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • 10.1016/0009-2614(76)80392-2 1:CAS:528:DyaE2sXntFWjuw%3D%3D
    • JH Davis KR Jeffrey M Bloom MI Valic TP Higgs 1976 Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains Chem Phys Lett 42 390 394 10.1016/0009-2614(76)80392-2 1:CAS:528:DyaE2sXntFWjuw%3D%3D
    • (1976) Chem Phys Lett , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 24
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers
    • 10.1016/0005-2736(75)90045-0 1174576 1:CAS:528:DyaE2MXlsF2ms7c%3D
    • RA Demel WSM Geurts Van Kessel RFA Zwall B Roelofsen LM Van Deenen 1975 Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers Biochim Biophys Acta 406 97 107 10.1016/0005-2736(75)90045-0 1174576 1:CAS:528:DyaE2MXlsF2ms7c%3D
    • (1975) Biochim Biophys Acta , vol.406 , pp. 97-107
    • Demel, R.A.1    Geurts Van Kessel, W.S.M.2    Zwall, R.F.A.3    Roelofsen, B.4    Van Deenen, L.M.5
  • 25
    • 0024622619 scopus 로고
    • On the spectral substraction of water from the FT-IR spectra of aqueous solutions of proteins
    • 10.1366/0003702894202814 1:CAS:528:DyaL1MXit1Oqur0%3D
    • F Dousseau M Therrien M Pézolet 1989 On the spectral substraction of water from the FT-IR spectra of aqueous solutions of proteins Appl Spectrosc 43 538 542 10.1366/0003702894202814 1:CAS:528:DyaL1MXit1Oqur0%3D
    • (1989) Appl Spectrosc , vol.43 , pp. 538-542
    • Dousseau, F.1    Therrien, M.2    Pézolet, M.3
  • 26
    • 0001450141 scopus 로고
    • NMR studies of micellar aggregates in 1-acyl-sn-glycerophosphocholine systems. the formation of a cubic liquid crystalline phase
    • 10.1021/j100288a018
    • P-O Ekiksson G Lindblom 1987 NMR studies of micellar aggregates in 1-acyl-sn-glycerophosphocholine systems. The formation of a cubic liquid crystalline phase J Phys Chem 91 846 853 10.1021/j100288a018
    • (1987) J Phys Chem , vol.91 , pp. 846-853
    • Ekiksson, P.-O.1    Lindblom, G.2
  • 27
    • 0001256511 scopus 로고
    • Structure of synthetic polypeptides
    • 10.1038/165921a0 15423537 1:CAS:528:DyaG3MXosFym
    • A Elliott EJ Ambrose 1950 Structure of synthetic polypeptides Nature 165 921 922 10.1038/165921a0 15423537 1:CAS:528:DyaG3MXosFym
    • (1950) Nature , vol.165 , pp. 921-922
    • Elliott, A.1    Ambrose, E.J.2
  • 28
    • 0035433919 scopus 로고    scopus 로고
    • Phage antibacterials make a comeback
    • 10.1038/90777 11479562 1:CAS:528:DC%2BD3MXlsleksbk%3D
    • VA Fischetti 2001 Phage antibacterials make a comeback Nat Biotechnol 19 734 735 10.1038/90777 11479562 1:CAS:528:DC%2BD3MXlsleksbk%3D
    • (2001) Nat Biotechnol , vol.19 , pp. 734-735
    • Fischetti, V.A.1
  • 29
    • 24944587206 scopus 로고    scopus 로고
    • Bacteriophage lytic enzymes: Novel anti-infectives
    • DOI 10.1016/j.tim.2005.08.007, PII S0966842X05002258
    • VA Fischetti 2005 Bacteriophage lytic enzymes: novel anti-infectives Trends Microbiol 13 491 496 10.1016/j.tim.2005.08.007 16125935 1:CAS:528:DC%2BD2MXhtVWnsLvN (Pubitemid 41317527)
    • (2005) Trends in Microbiology , vol.13 , Issue.10 , pp. 491-496
    • Fischetti, V.A.1
  • 30
    • 43749113198 scopus 로고    scopus 로고
    • Structure of the bacteriophage phiKZ lytic transglycosylase, gp144
    • 10.1074/jbc.M709398200 18160394 1:CAS:528:DC%2BD1cXivFyisr8%3D
    • A Fokine KA Miroshnikov MM Shneider VV Mesyanzhinov MG Rossmann 2008 Structure of the bacteriophage phiKZ lytic transglycosylase, gp144 J Biol Chem 283 7242 7250 10.1074/jbc.M709398200 18160394 1:CAS:528:DC%2BD1cXivFyisr8%3D
    • (2008) J Biol Chem , vol.283 , pp. 7242-7250
    • Fokine, A.1    Miroshnikov, K.A.2    Shneider, M.M.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 32
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds
    • 7855877 1:CAS:528:DyaK2MXmvVWlu70%3D
    • E Goormaghtigh V Cabiaux J-M Ruysschaert 1994 Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds Subcell Biochem 23 329 362 7855877 1:CAS:528:DyaK2MXmvVWlu70%3D
    • (1994) Subcell Biochem , vol.23 , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 33
    • 33947416806 scopus 로고
    • Introduction to spectral deconvolution
    • 10.1016/0165-9936(86)80015-2 1:CAS:528:DyaL28XlvF2htL4%3D
    • PR Griffiths GL Pariente 1986 Introduction to spectral deconvolution Trends Anal Chem 5 209 215 10.1016/0165-9936(86)80015-2 1:CAS:528: DyaL28XlvF2htL4%3D
    • (1986) Trends Anal Chem , vol.5 , pp. 209-215
    • Griffiths, P.R.1    Pariente, G.L.2
  • 34
    • 0000516361 scopus 로고
    • Deuterium isotope effect on the stability of molecules: Phospholipids
    • 10.1021/j100255a054 1:CAS:528:DyaL2MXhs1amtL4%3D
    • D Guard-Friar C-H Chen AS Engle 1985 Deuterium isotope effect on the stability of molecules: phospholipids J Phys Chem J Phys Chem 89 1810 1813 10.1021/j100255a054 1:CAS:528:DyaL2MXhs1amtL4%3D
    • (1985) J Phys Chem J Phys Chem , vol.89 , pp. 1810-1813
    • Guard-Friar, D.1    Chen, C.-H.2    Engle, A.S.3
  • 35
    • 33749622370 scopus 로고
    • Spin echoes
    • 10.1103/PhysRev.80.580
    • EL Hahn 1950 Spin echoes Phys Rev 80 580 10.1103/PhysRev.80.580
    • (1950) Phys Rev , vol.80 , pp. 580
    • Hahn, E.L.1
  • 36
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • 10.1016/S0006-3495(02)75226-0 12124282 1:CAS:528:DC%2BD38Xls1Ons70%3D
    • KJ Hallock DK Lee J Omnaas HI Mosberg A Ramamoorthy 2002 Membrane composition determines pardaxin's mechanism of lipid bilayer disruption Biophys J 83 1004 1013 10.1016/S0006-3495(02)75226-0 12124282 1:CAS:528: DC%2BD38Xls1Ons70%3D
    • (2002) Biophys J , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 37
    • 0020858317 scopus 로고
    • The effect of a phase transition on penetration of phospholipid monolayers by melittin and glucagon
    • 10.1016/0003-9861(83)90367-3 6639078 1:CAS:528:DyaL3sXmtVKlu7w%3D
    • HS Hendrickson PC Fan DK Kaufman DE Kleiner 1983 The effect of a phase transition on penetration of phospholipid monolayers by melittin and glucagon Arch Biochem Biophys 227 242 247 10.1016/0003-9861(83)90367-3 6639078 1:CAS:528:DyaL3sXmtVKlu7w%3D
    • (1983) Arch Biochem Biophys , vol.227 , pp. 242-247
    • Hendrickson, H.S.1    Fan, P.C.2    Kaufman, D.K.3    Kleiner, D.E.4
  • 38
    • 25944442748 scopus 로고
    • Microscope at the Brewster angle: Direct observation of first-order phase transitions in monolayers
    • 10.1063/1.1142032
    • S Henon J Meunier 1991 Microscope at the Brewster angle: direct observation of first-order phase transitions in monolayers Rev Sci Instrum 64 936 939 10.1063/1.1142032
    • (1991) Rev Sci Instrum , vol.64 , pp. 936-939
    • Henon, S.1    Meunier, J.2
  • 39
    • 0032813320 scopus 로고    scopus 로고
    • 31P solid state NMR
    • DOI 10.1016/S0014-5793(99)00881-9, PII S0014579399008819
    • 31P solid state NMR FEBS Lett 455 228 232 10.1016/S0014-5793(99)00881-9 10437778 1:CAS:528:DyaK1MXks1OlsLw%3D (Pubitemid 29333041)
    • (1999) FEBS Letters , vol.455 , Issue.3 , pp. 228-232
    • Hori, Y.1    Demura, M.2    Niidome, T.3    Aoyagi, H.4    Asakura, T.5
  • 40
    • 0036089906 scopus 로고    scopus 로고
    • Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers
    • DOI 10.1034/j.1399-3011.2002.21003.x
    • M Jelokhani-Niaraki EJ Prenner CM Kay RN McElhaney RS Hodges 2002 Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers J Peptide Res 60 23 36 10.1034/j.1399-3011.2002.21003.x 1:CAS:528:DC%2BD38XltVyksro%3D (Pubitemid 34680829)
    • (2002) Journal of Peptide Research , vol.60 , Issue.1 , pp. 23-36
    • Jelokhani-Niaraki, M.1    Prenner, E.J.2    Kay, C.M.3    McElhaney, R.N.4    Hodges, R.S.5
  • 41
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • DOI 10.1111/j.1745-7270.2007.00320.x
    • J Kong S Yu 2007 Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim Biophys Sin 39 549 559 10.1111/j.1745-7270.2007.00320.x 17687489 1:CAS:528:DC%2BD2sXhtFSks7bP (Pubitemid 47293710)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 42
    • 0027987329 scopus 로고
    • Components of the carbonyl stretching band in the infrared spectra of hydrated 1, 2-diacylglycerolipid bilayers: A reevaluation
    • 10.1016/S0006-3495(94)80723-4 7696476 1:CAS:528:DyaK2MXisVajuro%3D
    • RNAH Lewis RN McElhaney W Pohle HH Mantsch 1994 Components of the carbonyl stretching band in the infrared spectra of hydrated 1, 2-diacylglycerolipid bilayers: a reevaluation Biophys J 67 2367 2375 10.1016/S0006-3495(94)80723-4 7696476 1:CAS:528:DyaK2MXisVajuro%3D
    • (1994) Biophys J , vol.67 , pp. 2367-2375
    • Rnah, L.1    McElhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 43
    • 0032694324 scopus 로고    scopus 로고
    • The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes
    • 10.1016/S0005-2736(99)00203-5 10590305 1:CAS:528:DyaK1MXnslymu7k%3D
    • R Maget-Dana 1999 The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes Biochim Biophys Acta 1462 109 140 10.1016/S0005-2736(99)00203-5 10590305 1:CAS:528:DyaK1MXnslymu7k%3D
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 109-140
    • Maget-Dana, R.1
  • 44
    • 0026070508 scopus 로고
    • Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy
    • 10.1016/0009-3084(91)90077-O 2054905 1:CAS:528:DyaK3MXit1CksrY%3D
    • HH Mantsch RN McElhaney 1991 Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy Chem Phys Lipids 57 213 226 10.1016/0009-3084(91)90077-O 2054905 1:CAS:528:DyaK3MXit1CksrY%3D
    • (1991) Chem Phys Lipids , vol.57 , pp. 213-226
    • Mantsch, H.H.1    McElhaney, R.N.2
  • 45
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • 8982283 1:CAS:528:DyaK28XmvFals7g%3D
    • D Marsh 1996 Lateral pressure in membranes Biochim Biophys Acta 1286 183 223 8982283 1:CAS:528:DyaK28XmvFals7g%3D
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 46
    • 33644925279 scopus 로고    scopus 로고
    • The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes
    • 16352649 1:CAS:528:DC%2BD28XhsFOksrw%3D
    • AJ Mason A Martinez C Glaubitz O Danos A Kichler B Bechinger 2006 The antibiotic and DNA-transfecting peptide LAH4 selectively associates with, and disorders, anionic lipids in mixed membranes FASEB J 20 320 322 16352649 1:CAS:528:DC%2BD28XhsFOksrw%3D
    • (2006) FASEB J , vol.20 , pp. 320-322
    • Mason, A.J.1    Martinez, A.2    Glaubitz, C.3    Danos, O.4    Kichler, A.5    Bechinger, B.6
  • 48
    • 0035968116 scopus 로고    scopus 로고
    • Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria
    • DOI 10.1016/S0014-5793(01)02587-X, PII S001457930102587X
    • M Morita Y Tanji Y Orito K Mizoguchi A Soejima H Unno 2001 Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria FEBS Lett 500 56 59 10.1016/S0014-5793(01)02587- X 11434926 1:CAS:528:DC%2BD3MXkvVemu7k%3D (Pubitemid 32575318)
    • (2001) FEBS Letters , vol.500 , Issue.1-2 , pp. 56-59
    • Morita, M.1    Tanji, Y.2    Orito, Y.3    Mizoguchi, K.4    Soejima, A.5    Unno, H.6
  • 49
    • 0036360546 scopus 로고    scopus 로고
    • Evolution and spread of antibiotic resistance
    • DOI 10.1046/j.1365-2796.2002.01026.x
    • BH Normark S Normark 2002 Evolution and spread of antibiotic resistance J Intern Med 252 91 106 10.1046/j.1365-2796.2002.01026.x 12190884 1:CAS:528:DC%2BD38XntFGkurY%3D (Pubitemid 34989270)
    • (2002) Journal of Internal Medicine , vol.252 , Issue.2 , pp. 91-106
    • Henriques Normark, B.1    Normark, S.2
  • 50
    • 33845676753 scopus 로고    scopus 로고
    • Peptidoglycan lytic activity of the Pseudomonas aeruginosa phage φKZ gp144 lytic transglycosylase
    • DOI 10.1111/j.1574-6968.2006.00523.x
    • C Paradis-Bleau I Cloutier L Lemieux F Sanschagrin J Laroche M Auger A Garnier RC Levesque 2007 Peptidoglycan lytic activity of the Pseudomonas aeruginosa phage phiKZ gp144 lytic transglycosylase FEMS Microbiol Lett 266 201 209 10.1111/j.1574-6968.2006.00523.x 17233731 1:CAS:528:DC%2BD2sXpsVygsQ%3D%3D (Pubitemid 44952567)
    • (2007) FEMS Microbiology Letters , vol.266 , Issue.2 , pp. 201-209
    • Paradis-Bleau, C.1    Cloutier, I.2    Lemieux, L.3    Sanschagrin, F.4    Laroche, J.5    Auger, M.6    Garnier, A.7    Levesque, R.C.8
  • 51
    • 0029935142 scopus 로고    scopus 로고
    • 31P NMR spectroscopy
    • 10.1016/S0006-3495(96)79736-9 8785332 1:CAS:528:DyaK28XhvVGjsr0%3D
    • 31P NMR spectroscopy Biophys J 70 1737 1744 10.1016/S0006-3495(96) 79736-9 8785332 1:CAS:528:DyaK28XhvVGjsr0%3D
    • (1996) Biophys J , vol.70 , pp. 1737-1744
    • Picard, F.1    Pezolet, M.2    Bougis, P.E.3    Auger, M.4
  • 52
    • 0032586679 scopus 로고    scopus 로고
    • 31P NMR first spectral moment study of the partial magnetic orientation of phospholipid membranes
    • 10.1016/S0006-3495(99)76940-7 10423434 1:CAS:528:DyaK1MXltVyju74%3D
    • 31P NMR first spectral moment study of the partial magnetic orientation of phospholipid membranes Biophys J 77 888 902 10.1016/S0006-3495(99)76940-7 10423434 1:CAS:528:DyaK1MXltVyju74%3D
    • (1999) Biophys J , vol.77 , pp. 888-902
    • Picard, F.1    Paquet, M.-J.2    Levesque, J.3    Belanger, A.4    Auger, M.5
  • 53
    • 0028231733 scopus 로고
    • Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR
    • 10.1021/bi00175a014 8117706 1:CAS:528:DyaK2cXhsFOis7s%3D
    • TJ Pinheiro A Watts 1994 Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR Biochemistry 33 2459 2467 10.1021/bi00175a014 8117706 1:CAS:528:DyaK2cXhsFOis7s%3D
    • (1994) Biochemistry , vol.33 , pp. 2459-2467
    • Pinheiro, T.J.1    Watts, A.2
  • 54
    • 0028024922 scopus 로고
    • Mixing rates can markedly affect the kinetics of peptide-induced leakage from liposomes
    • 7804132 1:CAS:528:DyaK2cXmtVSgt70%3D
    • IV Polozov AI Polozova GM Anantharamaiah JP Segrest RM Epand 1994 Mixing rates can markedly affect the kinetics of peptide-induced leakage from liposomes Biochem Mol Biol Int 33 1073 1079 7804132 1:CAS:528:DyaK2cXmtVSgt70%3D
    • (1994) Biochem Mol Biol Int , vol.33 , pp. 1073-1079
    • Polozov, I.V.1    Polozova, A.I.2    Anantharamaiah, G.M.3    Segrest, J.P.4    Epand, R.M.5
  • 55
    • 0742305687 scopus 로고    scopus 로고
    • Phage-inspired antibiotics?
    • DOI 10.1038/nbt0204-167
    • S Projan 2004 Phage-inspired antibiotics? Nat Biotechnol 22 167 168 10.1038/nbt0204-167 14755287 1:CAS:528:DC%2BD2cXnvFejsA%3D%3D (Pubitemid 38160528)
    • (2004) Nature Biotechnology , vol.22 , Issue.2 , pp. 167-168
    • Projan, S.1
  • 56
    • 33947380145 scopus 로고    scopus 로고
    • Solution structure and interaction of Cupiennin 1a, a spider venom peptide, with phospholipid bilayers
    • DOI 10.1021/bi062306+
    • TL Pukala MP Boland JD Gehman L Kuhn-Nentwig F Separovic JH Bowie 2007 Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers Biochemistry 46 3576 3585 10.1021/bi062306+ 17319697 1:CAS:528:DC%2BD2sXitVKnsr0%3D (Pubitemid 46449174)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3576-3585
    • Pukala, T.L.1    Boland, M.P.2    Gehman, J.D.3    Kuhn-Nentwig, L.4    Separovic, F.5    Bowie, J.H.6
  • 57
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights
    • 10.1016/j.ssnmr.2009.03.003 19386477 1:CAS:528:DC%2BD1MXmvV2rt7o%3D
    • A Ramamoorthy 2009 Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights Solid State Nucl Magn Reson 35 201 207 10.1016/j.ssnmr.2009.03.003 19386477 1:CAS:528: DC%2BD1MXmvV2rt7o%3D
    • (2009) Solid State Nucl Magn Reson , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 58
    • 0035819875 scopus 로고    scopus 로고
    • Genetic analysis of the T4 holin: Timing and topology
    • DOI 10.1016/S0378-1119(01)00365-1, PII S0378111901003651
    • E Ramanculov R Young 2001 Genetic analysis of the phage T4 holin: timing and topology Gene 265 25 36 10.1016/S0378-1119(01)00365-1 11255004 1:CAS:528:DC%2BD3MXhsleksLw%3D (Pubitemid 32209247)
    • (2001) Gene , vol.265 , Issue.1-2 , pp. 25-36
    • Ramanculov, E.1    Young, R.2
  • 59
    • 0036787544 scopus 로고    scopus 로고
    • 31P-NMR and infrared spectroscopic study
    • 10.1016/S0006-3495(02)73968-4 12324425 1:CAS:528:DC%2BD38XnslSrsbg%3D
    • 31P-NMR and infrared spectroscopic study Biophys J 83 2074 2083 10.1016/S0006-3495(02) 73968-4 12324425 1:CAS:528:DC%2BD38XnslSrsbg%3D
    • (2002) Biophys J , vol.83 , pp. 2074-2083
    • Richard, J.-A.1    Kelly, I.2    Marion, D.3    Pezolet, M.4    Auger, M.5
  • 60
    • 0033808851 scopus 로고    scopus 로고
    • The N-terminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells
    • DOI 10.1128/JB.182.20.5823-5831.2000
    • C Sao-José R Parreira G Vieira MA Santos 2000 The N-terminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells J Bacteriol 182 5823 5831 10.1128/JB.182.20.5823-5831.2000 11004183 (Pubitemid 30746531)
    • (2000) Journal of Bacteriology , vol.182 , Issue.20 , pp. 5823-5831
    • Sao-Jose, C.1    Parreira, R.2    Vieira, G.3    Santos, M.A.4
  • 61
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • 10.1021/ac60214a047 1:CAS:528:DyaF2cXksVCjur8%3D
    • A Savitzky MJE Golay 1964 Smoothing and differentiation of data by simplified least squares procedures Anal Chem 36 1627 1639 10.1021/ac60214a047 1:CAS:528:DyaF2cXksVCjur8%3D
    • (1964) Anal Chem , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 62
    • 0017902280 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • 356883 1:CAS:528:DyaE1cXlsVWqsbc%3D
    • J Seelig 1978 Phosphorus-31 nuclear magnetic resonance and the head group structure of phospholipids in membranes Biochim Biophys Acta 515 105 140 356883 1:CAS:528:DyaE1cXlsVWqsbc%3D
    • (1978) Biochim Biophys Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 63
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes and biological membranes
    • 10.1017/S0033583500000305 7220788 1:CAS:528:DyaL3MXhtFKrtA%3D%3D
    • J Seelig A Seelig 1980 Lipid conformation in model membranes and biological membranes Q Rev Biophys 13 19 61 10.1017/S0033583500000305 7220788 1:CAS:528:DyaL3MXhtFKrtA%3D%3D
    • (1980) Q Rev Biophys , vol.13 , pp. 19-61
    • Seelig, J.1    Seelig, A.2
  • 64
    • 0027506087 scopus 로고
    • Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranes
    • 10.1021/bi00063a026 8457573 1:CAS:528:DyaK3sXhtl2gsrk%3D
    • N Sitaram R Nagaraj 1993 Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranes Biochemistry 32 3124 3130 10.1021/bi00063a026 8457573 1:CAS:528:DyaK3sXhtl2gsrk%3D
    • (1993) Biochemistry , vol.32 , pp. 3124-3130
    • Sitaram, N.1    Nagaraj, R.2
  • 66
    • 48449099381 scopus 로고    scopus 로고
    • PBEQ-Solver for online visualization of electrostatic potential of biomolecules
    • 10.1093/nar/gkn314 1:CAS:528:DC%2BD1cXptlKku7g%3D
    • J Sunhwan M Vargyas J Vasko-Szedlar M Roux W Im 2008 PBEQ-Solver for online visualization of electrostatic potential of biomolecules Nucleic Acids Res 36 W270 W275 10.1093/nar/gkn314 1:CAS:528:DC%2BD1cXptlKku7g%3D
    • (2008) Nucleic Acids Res , vol.36
    • Sunhwan, J.1    Vargyas, M.2    Vasko-Szedlar, J.3    Roux, M.4    Im, W.5
  • 67
    • 33847029153 scopus 로고    scopus 로고
    • Interaction of ovalbumin with phospholipids Langmuir-Blodgett film
    • K Tapanendu K Pal GB Talapatra 2007 Interaction of ovalbumin with phospholipids Langmuir-Blodgett film J Phys Chem 111 1199 1205
    • (2007) J Phys Chem , vol.111 , pp. 1199-1205
    • Tapanendu, K.1    Pal, K.2    Talapatra, G.B.3
  • 68
    • 0347356354 scopus 로고    scopus 로고
    • Old dogma, new tricks - 21st Century phage therapy
    • DOI 10.1038/nbt0104-31
    • K Thiel 2004 Old dogma, new tricks-21st century phage therapy Nat Biotechnol 22 31 36 10.1038/nbt0104-31 14704699 1:CAS:528:DC%2BD2cXls1Wm (Pubitemid 38057949)
    • (2004) Nature Biotechnology , vol.22 , Issue.1 , pp. 31-36
    • Thiel, K.1
  • 69
    • 2042527663 scopus 로고    scopus 로고
    • The study of the interaction of a model α-helical peptide with lipid bilayers and monolayers
    • DOI 10.1016/j.bioelechem.2003.12.005, PII S1567539404000313
    • P Vitovic S Kresak R Naumann SM Schiller RN Lewis RN McElhaney T Hianik 2004 The study of the interaction of a model alpha-helical peptide with lipid bilayers and monolayers Bioelectrochemistry 63 169 176 10.1016/j.bioelechem. 2003.12.005 15110268 1:CAS:528:DC%2BD2cXjsVWisLg%3D (Pubitemid 38534215)
    • (2004) Bioelectrochemistry , vol.63 , Issue.1-2 , pp. 169-176
    • Vitovic, P.1    Kresak, S.2    Naumann, R.3    Schiller, S.M.4    Lewis, R.N.A.H.5    McElhaney, R.N.6    Hianik, T.7
  • 70
    • 10444223867 scopus 로고    scopus 로고
    • Microscopic visualization of alamethicin incorporation into model membrane monolayers
    • 10.1021/la0477486 15568861 1:CAS:528:DC%2BD2cXptF2ksbo%3D
    • R Volinsky S Kolusheva A Berman R Jelinek 2004 Microscopic visualization of alamethicin incorporation into model membrane monolayers Langmuir 20 11084 11091 10.1021/la0477486 15568861 1:CAS:528:DC%2BD2cXptF2ksbo%3D
    • (2004) Langmuir , vol.20 , pp. 11084-11091
    • Volinsky, R.1    Kolusheva, S.2    Berman, A.3    Jelinek, R.4
  • 71
    • 33748946590 scopus 로고    scopus 로고
    • Investigations of antimicrobial peptides in planar film systems
    • DOI 10.1016/j.bbamem.2006.03.002, PII S0005273606000861
    • R Volinsky S Kolusheva A Berman R Jelinek 2006 Investigations of antimicrobial peptides in planar film systems Biochim Biophys Acta 1758 1393 1407 10.1016/j.bbamem.2006.03.002 16793000 1:CAS:528:DC%2BD28XhtVanu7bP (Pubitemid 44436077)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1393-1407
    • Volinsky, R.1    Kolusheva, S.2    Berman, A.3    Jelinek, R.4
  • 72
    • 0029332135 scopus 로고
    • Membrane protein structure: The contribution and potential of novel solid state NMR approaches
    • 10.3109/09687689509072423 8520624 1:CAS:528:DyaK2MXnsVOqsr0%3D
    • A Watts AS Ulrich DA Middleton 1995 Membrane protein structure: the contribution and potential of novel solid state NMR approaches Mol Membr Biol 12 233 246 10.3109/09687689509072423 8520624 1:CAS:528:DyaK2MXnsVOqsr0%3D
    • (1995) Mol Membr Biol , vol.12 , pp. 233-246
    • Watts, A.1    Ulrich, A.S.2    Middleton, D.A.3
  • 73
    • 0242576879 scopus 로고    scopus 로고
    • Quantitative Brewster angle microscopy of the surface film of human broncho-alveolar lavage fluid
    • DOI 10.1007/s00249-003-0290-2
    • K Winsel D Honig K Lunkenheimer K Geggel C Witt 2003 Quantitative Brewster angle microscopy of the surface film of human broncho-alveolar lavage fluid Eur Biophys J 32 544 552 10.1007/s00249-003-0290-2 12679861 (Pubitemid 37419921)
    • (2003) European Biophysics Journal , vol.32 , Issue.6 , pp. 544-552
    • Winsel, K.1    Honig, D.2    Lunkenheimer, K.3    Geggel, K.4    Witt, C.5
  • 75
    • 0034162940 scopus 로고    scopus 로고
    • Phages will out: Strategies of host cell lysis
    • DOI 10.1016/S0966-842X(00)01705-4, PII S0966842X00017054
    • R Young I-N Wang WD Roof 2000 Phages will out: strategies of host cell lysis Trends Microbiol 8 120 128 10.1016/S0966-842X(00)01705-4 10707065 1:STN:280:DC%2BD3c7ntlyiuw%3D%3D (Pubitemid 30155487)
    • (2000) Trends in Microbiology , vol.8 , Issue.3 , pp. 120-128
    • Young, R.1    Wang, I.-N.2    Roof, W.D.3
  • 76
    • 0031012862 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1, 2-diacylphosphatidylglycerols
    • 10.1016/S0006-3495(97)78712-5 9017203 1:CAS:528:DyaK2sXnsFGrtw%3D%3D
    • YP Zhang RN Lewis RN McElhaney 1997 Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1, 2-diacylphosphatidylglycerols Biophys J 72 779 793 10.1016/S0006-3495(97)78712-5 9017203 1:CAS:528:DyaK2sXnsFGrtw%3D%3D
    • (1997) Biophys J , vol.72 , pp. 779-793
    • Zhang, Y.P.1    Lewis, R.N.2    McElhaney, R.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.