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Volumn 89, Issue 1, 2010, Pages 11-23

Impact of the glycostructure of amphiphilic membrane components on the function of the outer membrane of Gram-negative bacteria as a matrix for incorporated channels and a target for antimicrobial peptides or proteins

Author keywords

Antimicrobial peptides; Complement; Lipopolysaccharide; Polymyxin B; Porins; Reconstituted membranes

Indexed keywords

BACTERICIDAL PERMEABILITY INCREASING PROTEIN; BACTERIUM LIPOPOLYSACCHARIDE; CATHELICIDIN; GLYCOLIPID; GLYCOSPHINGOLIPID; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PORIN;

EID: 73649107562     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2009.10.011     Document Type: Short Survey
Times cited : (20)

References (74)
  • 1
    • 0029865050 scopus 로고    scopus 로고
    • An N-terminal fragment of bactericidal/permeability-increasing protein protects against hemodynamic and metabolic derangements in Gram-negative sepsis
    • Ammons W.S., and Mallari C. An N-terminal fragment of bactericidal/permeability-increasing protein protects against hemodynamic and metabolic derangements in Gram-negative sepsis. J. Endotoxin Res 3 (1996) 57-66
    • (1996) J. Endotoxin Res , vol.3 , pp. 57-66
    • Ammons, W.S.1    Mallari, C.2
  • 2
    • 0034958947 scopus 로고    scopus 로고
    • Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care
    • Angus D.C., Linde-Zwirble W.T., Lidicker J., Clermont G., Carcillo J., and Pinsky M.R. Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care. Crit. Care Med. 29 (2001) 1303-1310
    • (2001) Crit. Care Med. , vol.29 , pp. 1303-1310
    • Angus, D.C.1    Linde-Zwirble, W.T.2    Lidicker, J.3    Clermont, G.4    Carcillo, J.5    Pinsky, M.R.6
  • 3
    • 0030953625 scopus 로고    scopus 로고
    • Electrophysiological characteristics of the PhoE porin channel from Escherichia coli. Implications for the possible existence of a superfamily of ion channels
    • Berrier C., Besnard M., and Ghazi A. Electrophysiological characteristics of the PhoE porin channel from Escherichia coli. Implications for the possible existence of a superfamily of ion channels. J. Membr. Biol. 156 (1997) 105-115
    • (1997) J. Membr. Biol. , vol.156 , pp. 105-115
    • Berrier, C.1    Besnard, M.2    Ghazi, A.3
  • 5
    • 34848919386 scopus 로고
    • Surface studies by scanning tunneling microscopy
    • Binnig G., Rohrer H., and Gerber C. Surface studies by scanning tunneling microscopy. Phys. Rev. Lett. 49 (1982) 57-61
    • (1982) Phys. Rev. Lett. , vol.49 , pp. 57-61
    • Binnig, G.1    Rohrer, H.2    Gerber, C.3
  • 7
    • 0023152530 scopus 로고
    • Multimeric C9 within C5b-9 is required for inner membrane damage to Escherichia coli J5 during complement killing
    • Bloch E.F., Schmetz M.A., Foulds J., Hammer C.H., Frank M.M., and Joiner K.A. Multimeric C9 within C5b-9 is required for inner membrane damage to Escherichia coli J5 during complement killing. J. Immunol. 138 (1987) 842-848
    • (1987) J. Immunol. , vol.138 , pp. 842-848
    • Bloch, E.F.1    Schmetz, M.A.2    Foulds, J.3    Hammer, C.H.4    Frank, M.M.5    Joiner, K.A.6
  • 8
    • 33847456945 scopus 로고
    • Films built by depositing successive monomolecular layers on a solid surface
    • Blodgett K.B. Films built by depositing successive monomolecular layers on a solid surface. J. Am. Chem. Soc. 57 (1935) 1007-1022
    • (1935) J. Am. Chem. Soc. , vol.57 , pp. 1007-1022
    • Blodgett, K.B.1
  • 9
    • 0018795945 scopus 로고
    • A comparative study of the phase transition of phospholipid bilayers and monolayers
    • Blume A. A comparative study of the phase transition of phospholipid bilayers and monolayers. Biochim. Biophys. Acta 557 (1979) 32-44
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 32-44
    • Blume, A.1
  • 11
    • 0028006169 scopus 로고
    • 2-terminal-fragment with isolated LPS and intact Proteus mirabilis and Escherichia coli. Infect
    • 2-terminal-fragment with isolated LPS and intact Proteus mirabilis and Escherichia coli. Infect. Immunity 62 (1994) 259-265
    • (1994) Immunity , vol.62 , pp. 259-265
    • Capodici, C.1    Chen, S.2    Sidorczyk, Z.3    Elsbach, P.4    Weiss, J.5
  • 12
    • 0029885361 scopus 로고    scopus 로고
    • In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane
    • de Cock H., van Blokland S., and Tommassen J. In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane. J. Biol. Chem. 271 (1996) 12885-12890
    • (1996) J. Biol. Chem. , vol.271 , pp. 12885-12890
    • de Cock, H.1    van Blokland, S.2    Tommassen, J.3
  • 13
    • 0033582497 scopus 로고    scopus 로고
    • Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli
    • de Cock H., Brandenburg K., Wiese A., Holst O., and Seydel U. Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli. J. Biol. Chem. 274 (1999) 5114-5119
    • (1999) J. Biol. Chem. , vol.274 , pp. 5114-5119
    • de Cock, H.1    Brandenburg, K.2    Wiese, A.3    Holst, O.4    Seydel, U.5
  • 15
    • 0027162586 scopus 로고
    • The bactericidal/permeability-increasing protein (BPI), a potent element in host-defense against Gram-negative bacteria and lipopolysaccharide
    • Elsbach P., and Weiss J. The bactericidal/permeability-increasing protein (BPI), a potent element in host-defense against Gram-negative bacteria and lipopolysaccharide. Immunobiology 187 (1993) 417-429
    • (1993) Immunobiology , vol.187 , pp. 417-429
    • Elsbach, P.1    Weiss, J.2
  • 17
    • 0030882451 scopus 로고    scopus 로고
    • Role of the constriction loop in the gating of outer membrane porin PhoE of Escherichia coli
    • Eppens E.F., Saint N., Van Gelder P., van Boxtel R., and Tommassen J. Role of the constriction loop in the gating of outer membrane porin PhoE of Escherichia coli. FEBS Lett. 415 (1997) 317-320
    • (1997) FEBS Lett. , vol.415 , pp. 317-320
    • Eppens, E.F.1    Saint, N.2    Van Gelder, P.3    van Boxtel, R.4    Tommassen, J.5
  • 18
    • 0026497337 scopus 로고
    • High-affinity binding of the bactericidal/permeability-increasing protein and a recombinant amino-terminal fragment to the lipid A region of lipopolysaccharide
    • Gazzano-Santoro H., Parent J.B., Grinna L., Horwitz A., Parsons T., Theofan G., Elsbach P., Weiss J., and Conlon P.J. High-affinity binding of the bactericidal/permeability-increasing protein and a recombinant amino-terminal fragment to the lipid A region of lipopolysaccharide. Infect. Immun. 60 (1992) 4754-4761
    • (1992) Infect. Immun. , vol.60 , pp. 4754-4761
    • Gazzano-Santoro, H.1    Parent, J.B.2    Grinna, L.3    Horwitz, A.4    Parsons, T.5    Theofan, G.6    Elsbach, P.7    Weiss, J.8    Conlon, P.J.9
  • 19
    • 0033550049 scopus 로고    scopus 로고
    • Molecular mechanisms of interaction of rabbit CAP18 with outer membranes of gram-negative bacteria
    • Gutsmann T., Larrick J.W., Seydel U., and Wiese A. Molecular mechanisms of interaction of rabbit CAP18 with outer membranes of gram-negative bacteria. Biochemistry 38 (1999) 13643-13653
    • (1999) Biochemistry , vol.38 , pp. 13643-13653
    • Gutsmann, T.1    Larrick, J.W.2    Seydel, U.3    Wiese, A.4
  • 20
    • 0035007963 scopus 로고    scopus 로고
    • Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids
    • Gutsmann T., Hagge S.O., Larrick J.W., Seydel U., and Wiese A. Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids. Biophys. J. 80 (2001) 2935-2945
    • (2001) Biophys. J. , vol.80 , pp. 2935-2945
    • Gutsmann, T.1    Hagge, S.O.2    Larrick, J.W.3    Seydel, U.4    Wiese, A.5
  • 21
    • 0042026495 scopus 로고    scopus 로고
    • Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers
    • Gutsmann T., Riekens B., Bruhn H., Wiese A., Seydel U., and Leippe M. Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers. Biochemistry 42 (2003) 9804-9812
    • (2003) Biochemistry , vol.42 , pp. 9804-9812
    • Gutsmann, T.1    Riekens, B.2    Bruhn, H.3    Wiese, A.4    Seydel, U.5    Leippe, M.6
  • 22
    • 1142274308 scopus 로고    scopus 로고
    • Inner field compensation as a tool for the characterization of asymmetric membranes and peptide-membrane interactions
    • Hagge S.O., Wiese A., Seydel U., and Gutsmann T. Inner field compensation as a tool for the characterization of asymmetric membranes and peptide-membrane interactions. Biophys. J. 86 (2004) 913-922
    • (2004) Biophys. J. , vol.86 , pp. 913-922
    • Hagge, S.O.1    Wiese, A.2    Seydel, U.3    Gutsmann, T.4
  • 23
    • 33745775471 scopus 로고    scopus 로고
    • Calcium adsorption and displacement: characterization of lipid monolayers and their interaction with membrane-active peptides/proteins
    • Hagge S.O., Hammer M.U., Wiese A., Seydel U., and Gutsmann T. Calcium adsorption and displacement: characterization of lipid monolayers and their interaction with membrane-active peptides/proteins. BMC Biochem. 7 (2006) 15
    • (2006) BMC Biochem. , vol.7 , pp. 15
    • Hagge, S.O.1    Hammer, M.U.2    Wiese, A.3    Seydel, U.4    Gutsmann, T.5
  • 24
    • 0014062013 scopus 로고
    • The binding of calcium at lipid-water interfaces
    • Hauser H., and Dawson R.M. The binding of calcium at lipid-water interfaces. Eur. J. Biochem. 1 (1967) 61-69
    • (1967) Eur. J. Biochem. , vol.1 , pp. 61-69
    • Hauser, H.1    Dawson, R.M.2
  • 25
    • 0029460562 scopus 로고
    • Structure and functions of endotoxin-binding peptides derived from CAP18
    • Hirata M., Zhong J., Wright S.C., and Larrick J.W. Structure and functions of endotoxin-binding peptides derived from CAP18. Prog. Clin. Biol. Res. 392 (1995) 317-326
    • (1995) Prog. Clin. Biol. Res. , vol.392 , pp. 317-326
    • Hirata, M.1    Zhong, J.2    Wright, S.C.3    Larrick, J.W.4
  • 26
    • 0000044612 scopus 로고
    • Chemical structure of the core region of lipopolysaccharides
    • Morrison D.C., and Ryan J.L. (Eds), CRC Press, Boca Raton, FL, USA
    • Holst O., and Brade H. Chemical structure of the core region of lipopolysaccharides. In: Morrison D.C., and Ryan J.L. (Eds). Molecular Biochemistry and Cellular Biology (1992), CRC Press, Boca Raton, FL, USA 135-170
    • (1992) Molecular Biochemistry and Cellular Biology , pp. 135-170
    • Holst, O.1    Brade, H.2
  • 28
    • 0024549593 scopus 로고
    • Molecular design of PhoE porin and its functional consequences
    • Jap B.K. Molecular design of PhoE porin and its functional consequences. J. Mol. Biol. 205 (1989) 407-419
    • (1989) J. Mol. Biol. , vol.205 , pp. 407-419
    • Jap, B.K.1
  • 29
    • 0020061925 scopus 로고
    • Studies on the mechanism of bacterial resistance to complement-mediated killing I. Terminal complement components are deposited and released from Salmonella minnesota S218 without causing bacterial death
    • Joiner K.A., Hammer C.H., Brown E.J., Cole R.J., and Frank M.M. Studies on the mechanism of bacterial resistance to complement-mediated killing I. Terminal complement components are deposited and released from Salmonella minnesota S218 without causing bacterial death. J. Exp. Med. 155 (1982) 797-808
    • (1982) J. Exp. Med. , vol.155 , pp. 797-808
    • Joiner, K.A.1    Hammer, C.H.2    Brown, E.J.3    Cole, R.J.4    Frank, M.M.5
  • 30
    • 0020058726 scopus 로고
    • Studies on the mechanism of bacterial resistance to complement-mediated killing II. C8 and C9 release C5b67 from the surface of Salmonella minnesota S218 because the terminal complex does not insert into the bacterial outer membrane
    • Joiner K.A., Hammer C.H., Brown E.J., and Frank M.M. Studies on the mechanism of bacterial resistance to complement-mediated killing II. C8 and C9 release C5b67 from the surface of Salmonella minnesota S218 because the terminal complex does not insert into the bacterial outer membrane. J. Exp. Med. 155 (1982) 809-819
    • (1982) J. Exp. Med. , vol.155 , pp. 809-819
    • Joiner, K.A.1    Hammer, C.H.2    Brown, E.J.3    Frank, M.M.4
  • 32
    • 0025552762 scopus 로고
    • Chemical structure and biological activity of lipopooligosaccharide isolated from Sphingomonas paucimobilis, a Gram-negative bacterium lacking usual lipopolysaccharide
    • Kawahara, K., Matsuura, M., Danbara, H., 1990. Chemical structure and biological activity of lipopooligosaccharide isolated from Sphingomonas paucimobilis, a Gram-negative bacterium lacking usual lipopolysaccharide. Jpn. J. Med. Sci. Biol. 43, 25.
    • (1990) Jpn. J. Med. Sci. Biol , vol.43 , pp. 25
    • Kawahara, K.1    Matsuura, M.2    Danbara, H.3
  • 33
    • 0034904365 scopus 로고    scopus 로고
    • Lipophilicity and membrane interactions of cationic-amphiphilic compounds: syntheses and structure-property relationships
    • Klein C.D., Tabeteh G.F., Laguna A.V., Holzgrabe U., and Mohr K. Lipophilicity and membrane interactions of cationic-amphiphilic compounds: syntheses and structure-property relationships. Eur. J. Pharm. Sci. 14 (2001) 167-175
    • (2001) Eur. J. Pharm. Sci. , vol.14 , pp. 167-175
    • Klein, C.D.1    Tabeteh, G.F.2    Laguna, A.V.3    Holzgrabe, U.4    Mohr, K.5
  • 34
    • 0029336564 scopus 로고
    • 23 attenuates endotoxin-induced cardiovascular depression in awake rabbits
    • 23 attenuates endotoxin-induced cardiovascular depression in awake rabbits. Shock 4 (1995) 74-78
    • (1995) Shock , vol.4 , pp. 74-78
    • Koyama, S.1    Shibamoto, T.2    Ammons, W.S.3    Saeki, Y.4
  • 35
    • 0000121165 scopus 로고
    • Activities of urease and pepsin monolayers
    • Langmuir I., and Schaefer V.J. Activities of urease and pepsin monolayers. J. Am. Chem. Soc. 60 (1938) 1351-1360
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 1351-1360
    • Langmuir, I.1    Schaefer, V.J.2
  • 36
    • 0019176733 scopus 로고
    • Ca replacement by cationic amphiphilic drugs from lipid monolayers
    • Lüllmann H., Plösch H., and Ziegler A. Ca replacement by cationic amphiphilic drugs from lipid monolayers. Biochem. Pharmacol. 29 (1980) 2969-2974
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 2969-2974
    • Lüllmann, H.1    Plösch, H.2    Ziegler, A.3
  • 37
    • 0016159215 scopus 로고
    • Chain ordering in liquid crystals; II. Structure of bilayer membranes
    • Marcelja S. Chain ordering in liquid crystals; II. Structure of bilayer membranes. Biochim. Biophys. Acta 367 (1974) 165-176
    • (1974) Biochim. Biophys. Acta , vol.367 , pp. 165-176
    • Marcelja, S.1
  • 39
    • 0026650865 scopus 로고
    • Mechanisms of Klebsiella pneumoniae resistance to complement-mediated killing
    • Merino S., Camprubí S., Albertí S., Benedí V.-J., and Tomás J.M. Mechanisms of Klebsiella pneumoniae resistance to complement-mediated killing. Infect. Immun. 60 (1992) 2529-2535
    • (1992) Infect. Immun. , vol.60 , pp. 2529-2535
    • Merino, S.1    Camprubí, S.2    Albertí, S.3    Benedí, V.-J.4    Tomás, J.M.5
  • 40
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal M., and Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA 69 (1972) 3561-3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 41
    • 0029150834 scopus 로고
    • Physiology and pathophysiology of complement: progress and trends
    • Morgan B.P. Physiology and pathophysiology of complement: progress and trends. Crit. Rev. Clin. Lab. Sci. 32 (1995) 265-298
    • (1995) Crit. Rev. Clin. Lab. Sci. , vol.32 , pp. 265-298
    • Morgan, B.P.1
  • 42
    • 0017331146 scopus 로고
    • Activation of the classical and properdin pathways of complement by bacterial lipopolysaccharides (LPS)
    • Morrison D.C., and Kline L.F. Activation of the classical and properdin pathways of complement by bacterial lipopolysaccharides (LPS). J. Immunol. 118 (1977) 362-368
    • (1977) J. Immunol. , vol.118 , pp. 362-368
    • Morrison, D.C.1    Kline, L.F.2
  • 44
    • 0002431489 scopus 로고
    • Outer membrane
    • Neidhardt C., Ingraham J.L., Brooks Low K., Magasnaik B., Schaechter M., and Umbarger H.E. (Eds), American Society for Microbiology, Washington, DC
    • Nikaido H., and Vaara M. Outer membrane. In: Neidhardt C., Ingraham J.L., Brooks Low K., Magasnaik B., Schaechter M., and Umbarger H.E. (Eds). Escherichia coli and Salmonella typhimurium. Cellular and Molecular Biology (1987), American Society for Microbiology, Washington, DC 7-22
    • (1987) Escherichia coli and Salmonella typhimurium. Cellular and Molecular Biology , pp. 7-22
    • Nikaido, H.1    Vaara, M.2
  • 45
    • 0025883775 scopus 로고
    • Endotoxin-neutralizing properties of the 25 kD N-terminal fragment of the 55-60 kD bactericidal/permeability-increasing protein of human neutrophils
    • Ooi C.E., Weiss J., Doerfler M.E., and Elsbach P. Endotoxin-neutralizing properties of the 25 kD N-terminal fragment of the 55-60 kD bactericidal/permeability-increasing protein of human neutrophils. J. Exp. Med. 174 (1991) 649-655
    • (1991) J. Exp. Med. , vol.174 , pp. 649-655
    • Ooi, C.E.1    Weiss, J.2    Doerfler, M.E.3    Elsbach, P.4
  • 46
    • 51149131643 scopus 로고
    • Surface tension
    • Pockels A. Surface tension. Nature 43 (1891) 437-439
    • (1891) Nature , vol.43 , pp. 437-439
    • Pockels, A.1
  • 48
    • 23144458847 scopus 로고    scopus 로고
    • Probing the properties of lipopolysaccharide monolayers and their interaction with the antimicrobial peptide polymyxin B by atomic force microscopy
    • Roes S., Seydel U., and Gutsmann T. Probing the properties of lipopolysaccharide monolayers and their interaction with the antimicrobial peptide polymyxin B by atomic force microscopy. Langmuir 21 (2005) 6970-6978
    • (2005) Langmuir , vol.21 , pp. 6970-6978
    • Roes, S.1    Seydel, U.2    Gutsmann, T.3
  • 49
    • 0018646280 scopus 로고
    • Capacitance and conductance as tools for the measurement of asymmetric surface potentials and energy barriers of lipid bilayer membranes
    • Schoch P., Sargent D.F., and Schwyzer R. Capacitance and conductance as tools for the measurement of asymmetric surface potentials and energy barriers of lipid bilayer membranes. J. Membr. Biol. 46 (1979) 71-89
    • (1979) J. Membr. Biol. , vol.46 , pp. 71-89
    • Schoch, P.1    Sargent, D.F.2    Schwyzer, R.3
  • 50
    • 0025013894 scopus 로고
    • Pore formation by complement in the outer membrane of Gram-negative bacteria studied with asymmetric planar lipopolysaccharide/phospholipid bilayers
    • Schröder G., Brandenburg K., Brade L., and Seydel U. Pore formation by complement in the outer membrane of Gram-negative bacteria studied with asymmetric planar lipopolysaccharide/phospholipid bilayers. J. Membr. Biol. 118 (1990) 161-170
    • (1990) J. Membr. Biol. , vol.118 , pp. 161-170
    • Schröder, G.1    Brandenburg, K.2    Brade, L.3    Seydel, U.4
  • 51
    • 0025970549 scopus 로고
    • Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin
    • Sen K., and Nikaido H. Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin. J. Bacteriol. 173 (1991) 926-928
    • (1991) J. Bacteriol. , vol.173 , pp. 926-928
    • Sen, K.1    Nikaido, H.2
  • 52
    • 0023867105 scopus 로고
    • Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane
    • Sen K., Hellman J., and Nikaido H. Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane. J. Biol. Chem. 263 (1988) 1182-1187
    • (1988) J. Biol. Chem. , vol.263 , pp. 1182-1187
    • Sen, K.1    Hellman, J.2    Nikaido, H.3
  • 53
    • 0024851425 scopus 로고
    • Supramolecular structure of lipopolysaccharide and free lipid A under physiological conditions as determined by synchroton small-angle X-ray diffraction
    • Seydel U., Brandenburg K., Koch M.H.J., and Rietschel E.T. Supramolecular structure of lipopolysaccharide and free lipid A under physiological conditions as determined by synchroton small-angle X-ray diffraction. Eur. J. Biochem. 186 (1989) 325-332
    • (1989) Eur. J. Biochem. , vol.186 , pp. 325-332
    • Seydel, U.1    Brandenburg, K.2    Koch, M.H.J.3    Rietschel, E.T.4
  • 54
    • 0018812824 scopus 로고
    • Study of surface potential difference in bilayer membranes according to the second harmonic response of capacitance current
    • Sokolov V.S., and Kuz'min V.G. Study of surface potential difference in bilayer membranes according to the second harmonic response of capacitance current. Biofizika 25 (1980) 170-172
    • (1980) Biofizika , vol.25 , pp. 170-172
    • Sokolov, V.S.1    Kuz'min, V.G.2
  • 55
    • 0019387949 scopus 로고
    • Localization of phoE, the structural gene for outer membrane protein e in Escherichia coli K-12
    • Tommassen J., and Lugtenberg B. Localization of phoE, the structural gene for outer membrane protein e in Escherichia coli K-12. J. Bacteriol. 147 (1981) 118-123
    • (1981) J. Bacteriol. , vol.147 , pp. 118-123
    • Tommassen, J.1    Lugtenberg, B.2
  • 57
    • 0021264462 scopus 로고
    • Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization
    • Tschopp J. Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization. J. Biol. Chem. 259 (1984) 7857-7863
    • (1984) J. Biol. Chem. , vol.259 , pp. 7857-7863
    • Tschopp, J.1
  • 58
    • 0021320278 scopus 로고
    • Molecular weight of poly C9: 12 to 18 C9 molecules form the transmembrane channel of complement
    • Tschopp J., Engel A., and Podack E.R. Molecular weight of poly C9: 12 to 18 C9 molecules form the transmembrane channel of complement. J. Biol. Chem. 259 (1984) 1922-1928
    • (1984) J. Biol. Chem. , vol.259 , pp. 1922-1928
    • Tschopp, J.1    Engel, A.2    Podack, E.R.3
  • 59
    • 0023911582 scopus 로고
    • pH-dependent influence of membrane-incorporated flunarizine on Ca-binding to phosphatidylserine monolayer membranes
    • Vogelgesang R., Wood G., Peters T., and Scheufler E. pH-dependent influence of membrane-incorporated flunarizine on Ca-binding to phosphatidylserine monolayer membranes. Biochem. Pharmacol. 37 (1988) 1597-1600
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 1597-1600
    • Vogelgesang, R.1    Wood, G.2    Peters, T.3    Scheufler, E.4
  • 60
    • 0022509690 scopus 로고
    • Antibody-independent activation of the classical pathway of human serum complement by lipid A is restricted to Re-chemotype lipopolysaccharide and purified lipid A. Infect
    • Vukajlovich S.W. Antibody-independent activation of the classical pathway of human serum complement by lipid A is restricted to Re-chemotype lipopolysaccharide and purified lipid A. Infect. Immunity 53 (1986) 480-485
    • (1986) Immunity , vol.53 , pp. 480-485
    • Vukajlovich, S.W.1
  • 61
    • 0008916870 scopus 로고
    • Activation of human serum complement by bacterial lipopolysaccharides
    • Vukajlovich S.W., Sinoway P., and Morrison D.C. Activation of human serum complement by bacterial lipopolysaccharides. EOS J. Immunol. Immunopharmacol. 6 Suppl. 3 (1986) 73-75
    • (1986) EOS J. Immunol. Immunopharmacol. , vol.6 , Issue.SUPPL. 3 , pp. 73-75
    • Vukajlovich, S.W.1    Sinoway, P.2    Morrison, D.C.3
  • 62
    • 0023153002 scopus 로고
    • Activation of human serum complement by bacterial lipopolysaccharides: structural requirements for antibody independent activation of the classical and alternative pathway
    • Vukajlovich S.W., Hoffman J., and Morrison D.C. Activation of human serum complement by bacterial lipopolysaccharides: structural requirements for antibody independent activation of the classical and alternative pathway. Mol. Immunol. 24 (1987) 319-331
    • (1987) Mol. Immunol. , vol.24 , pp. 319-331
    • Vukajlovich, S.W.1    Hoffman, J.2    Morrison, D.C.3
  • 63
    • 0028087586 scopus 로고
    • Resistance of Actinobacillus pleuropneumoniae to bactericidal antibody and complement is mediated by capsular polysaccharide and blocking antibody specific for lipopolysaccharide
    • Ward C.K., and Inzana T.J. Resistance of Actinobacillus pleuropneumoniae to bactericidal antibody and complement is mediated by capsular polysaccharide and blocking antibody specific for lipopolysaccharide. J. Immunol. 153 (1994) 2110-2121
    • (1994) J. Immunol. , vol.153 , pp. 2110-2121
    • Ward, C.K.1    Inzana, T.J.2
  • 64
    • 0023123560 scopus 로고
    • Cellular and subcellular localization of the bactericidal/permeability-increasing protein of neutrophils
    • Weiss J., and Olsson I. Cellular and subcellular localization of the bactericidal/permeability-increasing protein of neutrophils. Blood 69 (1987) 652-659
    • (1987) Blood , vol.69 , pp. 652-659
    • Weiss, J.1    Olsson, I.2
  • 65
    • 0017804093 scopus 로고
    • Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes
    • Weiss J., Elsbach P., Olsson I., and Odeberg H. Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes. J. Biol. Chem. 253 (1978) 2664-2672
    • (1978) J. Biol. Chem. , vol.253 , pp. 2664-2672
    • Weiss, J.1    Elsbach, P.2    Olsson, I.3    Odeberg, H.4
  • 66
    • 0026779276 scopus 로고
    • 2-terminal fragment cause killing of serum-resistant Gram-negative bacteria in whole blood and inhibit tumor necrosis factor release induced by the bacteria
    • 2-terminal fragment cause killing of serum-resistant Gram-negative bacteria in whole blood and inhibit tumor necrosis factor release induced by the bacteria. J. Clin. Invest. 90 (1992) 1122-1130
    • (1992) J. Clin. Invest. , vol.90 , pp. 1122-1130
    • Weiss, J.1    Elsbach, P.2    Shu, C.3    Castillo, J.4    Grinna, L.5    Horwitz, A.6    Theofan, G.7
  • 67
    • 0033656562 scopus 로고    scopus 로고
    • Electrophysiological measurements on reconstituted outer membranes
    • Wiese A., and Seydel U. Electrophysiological measurements on reconstituted outer membranes. Methods Mol. Biol. 145 (1999) 355-370
    • (1999) Methods Mol. Biol. , vol.145 , pp. 355-370
    • Wiese, A.1    Seydel, U.2
  • 68
    • 0030052635 scopus 로고    scopus 로고
    • Planar asymmetric lipid bilayers of glycosphingolipid or lipopolysaccharide on one side and phospholipids on the other: membrane potential, porin function, and complement activation
    • Wiese A., Reiners J.O., Brandenburg K., Kawahara K., Zähringer U., and Seydel U. Planar asymmetric lipid bilayers of glycosphingolipid or lipopolysaccharide on one side and phospholipids on the other: membrane potential, porin function, and complement activation. Biophys. J. 70 (1996) 321-329
    • (1996) Biophys. J. , vol.70 , pp. 321-329
    • Wiese, A.1    Reiners, J.O.2    Brandenburg, K.3    Kawahara, K.4    Zähringer, U.5    Seydel, U.6
  • 69
    • 0030739226 scopus 로고    scopus 로고
    • Mechanisms of action of the bactericidal/permeability-increasing protein BPI on reconstituted outer membranes of Gram-negative bacteria
    • Wiese A., Brandenburg K., Carroll S.F., Rietschel E.T., and Seydel U. Mechanisms of action of the bactericidal/permeability-increasing protein BPI on reconstituted outer membranes of Gram-negative bacteria. Biochemistry 36 (1997) 10311-10319
    • (1997) Biochemistry , vol.36 , pp. 10311-10319
    • Wiese, A.1    Brandenburg, K.2    Carroll, S.F.3    Rietschel, E.T.4    Seydel, U.5
  • 70
    • 0030829350 scopus 로고    scopus 로고
    • Mechanisms of action of the bactericidal/permeability-increasing protein BPI on endotoxin and phospholipid monolayers and aggregates
    • Wiese A., Brandenburg K., Lindner B., Schromm A.B., Carroll S.F., Rietschel E.T., and Seydel U. Mechanisms of action of the bactericidal/permeability-increasing protein BPI on endotoxin and phospholipid monolayers and aggregates. Biochemistry 36 (1997) 10301-10310
    • (1997) Biochemistry , vol.36 , pp. 10301-10310
    • Wiese, A.1    Brandenburg, K.2    Lindner, B.3    Schromm, A.B.4    Carroll, S.F.5    Rietschel, E.T.6    Seydel, U.7
  • 71
    • 0032520840 scopus 로고    scopus 로고
    • Molecular mechanisms of polymyxin B-membrane interactions: direct correlation between surface charge density and self-promoted uptake
    • Wiese A., Münstermann M., Gutsmann T., Lindner B., Kawahara K., Zähringer U., and Seydel U. Molecular mechanisms of polymyxin B-membrane interactions: direct correlation between surface charge density and self-promoted uptake. J. Membr. Biol. 162 (1998) 127-138
    • (1998) J. Membr. Biol. , vol.162 , pp. 127-138
    • Wiese, A.1    Münstermann, M.2    Gutsmann, T.3    Lindner, B.4    Kawahara, K.5    Zähringer, U.6    Seydel, U.7
  • 72
    • 0034925803 scopus 로고    scopus 로고
    • Influence of acyl chain fluidity on the lipopolysaccharide-induced activation of complement
    • Wiese A., Grünewald P., Schaper K.J., and Seydel U. Influence of acyl chain fluidity on the lipopolysaccharide-induced activation of complement. J. Endotoxin. Res. 7 (2001) 147-155
    • (2001) J. Endotoxin. Res. , vol.7 , pp. 147-155
    • Wiese, A.1    Grünewald, P.2    Schaper, K.J.3    Seydel, U.4
  • 73
    • 0035208031 scopus 로고    scopus 로고
    • Status of methods for assessing bacterial cell surface charge properties based on zeta potential measurements
    • Wilson W.W., Wade M.M., Holman S.C., and Champlin F.R. Status of methods for assessing bacterial cell surface charge properties based on zeta potential measurements. J. Microbiol. Methods 43 (2001) 153-164
    • (2001) J. Microbiol. Methods , vol.43 , pp. 153-164
    • Wilson, W.W.1    Wade, M.M.2    Holman, S.C.3    Champlin, F.R.4
  • 74
    • 0028844134 scopus 로고
    • Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M., Gennaro R., and Romeo D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374 (1995) 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3


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