메뉴 건너뛰기




Volumn 1464, Issue 2, 2000, Pages 284-298

Biochemical and biophysical characterization of in vitro folded outer membrane porin PorA of Neisseria meningitidis

Author keywords

Black lipid membrane; Membrane protein; Neisseria meningitidis; PorA; Porin; RmpM

Indexed keywords

OUTER MEMBRANE PROTEIN; PORIN;

EID: 0034607359     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(00)00155-3     Document Type: Article
Times cited : (56)

References (63)
  • 1
    • 0000744655 scopus 로고
    • Studies of porins: Spontaneously transferred from whole cells and reconstituted from purified proteins of Neisseria gonorrhoeae and Neisseria meningitidis
    • Lynch E.C., Blake M.S., Gotschlich E.C., Mauro A. Studies of porins: spontaneously transferred from whole cells and reconstituted from purified proteins of Neisseria gonorrhoeae and Neisseria meningitidis. Biophys. J. 45:1984;104-107.
    • (1984) Biophys. J. , vol.45 , pp. 104-107
    • Lynch, E.C.1    Blake, M.S.2    Gotschlich, E.C.3    Mauro, A.4
  • 2
    • 0032513175 scopus 로고    scopus 로고
    • Successful recovery of the normal electrophysiological properties of PorB (Class 3) porin from Neisseria meningitidis after expression in Escherichia coli and renaturation
    • Song J., Minetti C.A.S.A., Blake M.S., Colombini M. Successful recovery of the normal electrophysiological properties of PorB (Class 3) porin from Neisseria meningitidis after expression in Escherichia coli and renaturation. Biochim. Biophys. Acta. 1370:1998;289-298.
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 289-298
    • Song, J.1    Minetti, C.A.S.A.2    Blake, M.S.3    Colombini, M.4
  • 3
    • 0025347045 scopus 로고
    • Isolation of Neisseria meningitidis mutants deficient in class 1 (PorA) and class 3 (PorB) outer membrane proteins
    • Tommassen J., Vermey P., Struyvé M., Benz R., Poolman J.T. Isolation of Neisseria meningitidis mutants deficient in class 1 (PorA) and class 3 (PorB) outer membrane proteins. Infect. Immun. 58:1990;1355-1359.
    • (1990) Infect. Immun. , vol.58 , pp. 1355-1359
    • Tommassen, J.1    Vermey, P.2    Struyvé, M.3    Benz, R.4    Poolman, J.T.5
  • 6
    • 0030888166 scopus 로고    scopus 로고
    • Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis
    • Minetti C.A.S.A., Tai J.Y., Blake M.S., Pullen J.K., Liang S.M., Remeta D.P. Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. J. Biol. Chem. 272:1997;10710-10720.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10710-10720
    • Minetti, C.A.S.A.1    Tai, J.Y.2    Blake, M.S.3    Pullen, J.K.4    Liang, S.M.5    Remeta, D.P.6
  • 7
    • 0023628634 scopus 로고
    • Molecular cloning and expression of Neisseria meningitidis class I outer membrane protein in Escherichia coli K-12
    • Barlow A.K., Heckels J.E., Clarke I.N. Molecular cloning and expression of Neisseria meningitidis class I outer membrane protein in Escherichia coli K-12. Infect. Immun. 55:1987;2734-2740.
    • (1987) Infect. Immun. , vol.55 , pp. 2734-2740
    • Barlow, A.K.1    Heckels, J.E.2    Clarke, I.N.3
  • 8
    • 0025346393 scopus 로고
    • Stable expression of meningococcal class 1 protein in an antigenically reactive form in outer membranes of Escherichia coli
    • White D.A., Barlow A.K., Clarke I.N., Heckels J.E. Stable expression of meningococcal class 1 protein in an antigenically reactive form in outer membranes of Escherichia coli. Mol. Microbiol. 4:1990;769-776.
    • (1990) Mol. Microbiol. , vol.4 , pp. 769-776
    • White, D.A.1    Barlow, A.K.2    Clarke, I.N.3    Heckels, J.E.4
  • 9
    • 0028306035 scopus 로고
    • Expression of large amounts of neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers
    • Qi H.L., Tai J.Y., Blake M.S. Expression of large amounts of neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers. Infect. Immun. 62:1994;2432-2439.
    • (1994) Infect. Immun. , vol.62 , pp. 2432-2439
    • Qi, H.L.1    Tai, J.Y.2    Blake, M.S.3
  • 10
    • 0030174312 scopus 로고    scopus 로고
    • Immunization with meningococcal class 1 outer membrane protein produced in Bacillus subtilis and reconstituted in the presence of Zwittergent or Triton X-100
    • Idänpään-Heikkilä I., Wahlström E., Muttilainen S., Nurminen M., Käyhty H., Sarvas M., Mäkelä P.H. Immunization with meningococcal class 1 outer membrane protein produced in Bacillus subtilis and reconstituted in the presence of Zwittergent or Triton X-100. Vaccine. 14:1996;886-891.
    • (1996) Vaccine , vol.14 , pp. 886-891
    • Idänpään-Heikkilä, I.1    Wahlström, E.2    Muttilainen, S.3    Nurminen, M.4    Käyhty, H.5    Sarvas, M.6    Mäkelä, P.H.7
  • 11
    • 0024453090 scopus 로고
    • The class 1 outer membrane protein of Neisseria meningitidis: Gene sequence and structural and immunological similarities to gonococcal porins
    • Barlow A.K., Heckels J.E., Clarke I.N. The class 1 outer membrane protein of Neisseria meningitidis: gene sequence and structural and immunological similarities to gonococcal porins. Mol. Microbiol. 3:1989;131-139.
    • (1989) Mol. Microbiol. , vol.3 , pp. 131-139
    • Barlow, A.K.1    Heckels, J.E.2    Clarke, I.N.3
  • 13
    • 0023042283 scopus 로고
    • Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffatt B.A. Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 14
    • 0025963805 scopus 로고
    • Comparison of the class I outer membrane proteins of eight serological reference strains of Neisseria meningitidis
    • Maiden M.C.J., Suker J., McKenna A.J., Bygraves J.A., Feavers I.M. Comparison of the class I outer membrane proteins of eight serological reference strains of Neisseria meningitidis. Mol. Microbiol. 5:1991;727-736.
    • (1991) Mol. Microbiol. , vol.5 , pp. 727-736
    • Maiden, M.C.J.1    Suker, J.2    McKenna, A.J.3    Bygraves, J.A.4    Feavers, I.M.5
  • 15
    • 0018377442 scopus 로고
    • Serotypes of Neisseria meningitidis isolated from patients in Norway during the first six months of 1987
    • Holten E. Serotypes of Neisseria meningitidis isolated from patients in Norway during the first six months of 1987. J. Clin. Microbiol. 9:1979;186-188.
    • (1979) J. Clin. Microbiol. , vol.9 , pp. 186-188
    • Holten, E.1
  • 17
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels
    • Tsai C.M., Frasch C.E. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal. Biochem. 119:1982;115-119.
    • (1982) Anal. Biochem. , vol.119 , pp. 115-119
    • Tsai, C.M.1    Frasch, C.E.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0029101182 scopus 로고
    • In vitro folding of Escherichia coli outer-membrane phospholipase A
    • Dekker N., Merck K., Tommassen J., Verheij H.M. In vitro folding of Escherichia coli outer-membrane phospholipase A. Eur. J. Biochem. 232:1995;214-219.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 214-219
    • Dekker, N.1    Merck, K.2    Tommassen, J.3    Verheij, H.M.4
  • 20
    • 0030759550 scopus 로고    scopus 로고
    • Pore functioning of outer membrane protein PhoE of Escherichia coli: Mutagenesis of the constriction loop L3
    • Van Gelder P., Saint N., van Boxtel R., Rosenbusch J.P., Tommassen J. Pore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3. Protein Eng. 10:1997;699-706.
    • (1997) Protein Eng. , vol.10 , pp. 699-706
    • Van Gelder, P.1    Saint, N.2    Van Boxtel, R.3    Rosenbusch, J.P.4    Tommassen, J.5
  • 21
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K-12 into four bands
    • Lugtenberg B., Meijers J., Peters R., van der Hoek P., van Alphen L. Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K-12 into four bands. FEBS Lett. 58:1975;254-258.
    • (1975) FEBS Lett. , vol.58 , pp. 254-258
    • Lugtenberg, B.1    Meijers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 22
    • 0025271965 scopus 로고
    • Outer membrane PhoE protein of Escherichia coli as a carrier for foreign antigenic determinants: Immunogenicity of epitopes of foot-and-mouth disease virus
    • Agterberg M., Adriaanse H., Lankhof H., Meloen R., Tommassen J. Outer membrane PhoE protein of Escherichia coli as a carrier for foreign antigenic determinants: immunogenicity of epitopes of foot-and-mouth disease virus. Vaccine. 8:1990;85-91.
    • (1990) Vaccine , vol.8 , pp. 85-91
    • Agterberg, M.1    Adriaanse, H.2    Lankhof, H.3    Meloen, R.4    Tommassen, J.5
  • 23
    • 0029618716 scopus 로고
    • A conserved histidine residue of Escherichia coli outer-membrane phospholipase A is important for activity
    • Brok R.G.P.M., Dekker N., Gerrits N., Verheij H.M., Tommassen J. A conserved histidine residue of Escherichia coli outer-membrane phospholipase A is important for activity. Eur. J. Biochem. 234:1995;934-938.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 934-938
    • Brok, R.G.P.M.1    Dekker, N.2    Gerrits, N.3    Verheij, H.M.4    Tommassen, J.5
  • 24
    • 0003025310 scopus 로고
    • Influence of the length of lipopolysaccharide molecules on the surface exposure of class 1 and 2 outer membrane proteins of Neisseria meningitidis strain 2996 (B:2b:P1.2)
    • in: G.K. Schoolnik (Ed.), American Society for Microbiology, Washington, DC
    • J.T. Poolman, F.B. Wientjes, C.T.P. Hopman, H.C. Zanen, Influence of the length of lipopolysaccharide molecules on the surface exposure of class 1 and 2 outer membrane proteins of Neisseria meningitidis strain 2996 (B:2b:P1.2), in: G.K. Schoolnik (Ed.), The Pathogenic Neisseriae, American Society for Microbiology, Washington, DC, 1985, pp. 562-570.
    • (1985) The Pathogenic Neisseriae , pp. 562-570
    • Poolman, J.T.1    Wientjes, F.B.2    Hopman, C.T.P.3    Zanen, H.C.4
  • 25
    • 0018081614 scopus 로고
    • Immunochemical characterization of outer membrane complexes from Neisseria meningitidis by the SDS-polyacrylamide-gel-electrophoresis-immunoperoxidase technique (SGIP)
    • Poolman J.T., Hopman C.T.P., Zanen H.C. Immunochemical characterization of outer membrane complexes from Neisseria meningitidis by the SDS-polyacrylamide-gel-electrophoresis-immunoperoxidase technique (SGIP). FEMS Microbiol. Lett. 4:1978;245-248.
    • (1978) FEMS Microbiol. Lett. , vol.4 , pp. 245-248
    • Poolman, J.T.1    Hopman, C.T.P.2    Zanen, H.C.3
  • 26
    • 0020983948 scopus 로고
    • Proteins forming large channels from bacterial and mitochondrial outer membranes: Porins and phage lambda receptor protein
    • Nikaido H. Proteins forming large channels from bacterial and mitochondrial outer membranes: porins and phage lambda receptor protein. Methods Enzymol. 97:1983;85-100.
    • (1983) Methods Enzymol. , vol.97 , pp. 85-100
    • Nikaido, H.1
  • 27
    • 0002056886 scopus 로고
    • Preparation and use of liposomes as models of biological membranes
    • in: E.D. Korn (Ed.), Plenum, New York
    • A.D. Bangham, M.W. Hill, M.G.A. Miller, Preparation and use of liposomes as models of biological membranes, in: E.D. Korn (Ed.), Methods in Membrane Biology, vol. 1, Plenum, New York, 1974, pp. 1-68.
    • (1974) Methods in Membrane Biology , vol.1 , pp. 1-68
    • Bangham, A.D.1    Hill, M.W.2    Miller, M.G.A.3
  • 28
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal M., 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
  • 29
    • 0028300062 scopus 로고
    • Influence of the lipid matrix on incorporation and function of LPS-free porin from Paracoccus denitrificans
    • Wiese A., Schröder G., Brandenburg K., Hirsch A., Welte W., Seydel U. Influence of the lipid matrix on incorporation and function of LPS-free porin from Paracoccus denitrificans. Biochim. Biophys. Acta. 1190:1994;231-242.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 231-242
    • Wiese, A.1    Schröder, G.2    Brandenburg, K.3    Hirsch, A.4    Welte, W.5    Seydel, U.6
  • 31
    • 0029154784 scopus 로고
    • Heterologous production of the P1 porin of Neisseria meningitidis in Bacillus subtilis: The effect of an N-terminal extension on the presentation of native-like epitopes
    • Muttilainen S., Butcher S.J., Runeberg K., Nurminen M., Idänpään-Heikkilä I., Wahlström E., Sarvas M. Heterologous production of the P1 porin of Neisseria meningitidis in Bacillus subtilis: the effect of an N-terminal extension on the presentation of native-like epitopes. Microb. Pathog. 18:1995;365-371.
    • (1995) Microb. Pathog. , vol.18 , pp. 365-371
    • Muttilainen, S.1    Butcher, S.J.2    Runeberg, K.3    Nurminen, M.4    Idänpään-Heikkilä, I.5    Wahlström, E.6    Sarvas, M.7
  • 32
    • 0030550722 scopus 로고    scopus 로고
    • Expression of Neisseria meningitidis class 1 porin as a fusion protein in Escherichia coli: The influence of liposomes and adjuvants on the production of a bactericidal immune response
    • Ward S.J., Scopes D., Christodoulides M., Clarke I.N., Heckels J.E. Expression of Neisseria meningitidis class 1 porin as a fusion protein in Escherichia coli: the influence of liposomes and adjuvants on the production of a bactericidal immune response. Microb. Pathog. 21:1996;499-512.
    • (1996) Microb. Pathog. , vol.21 , pp. 499-512
    • Ward, S.J.1    Scopes, D.2    Christodoulides, M.3    Clarke, I.N.4    Heckels, J.E.5
  • 33
    • 0025214278 scopus 로고
    • Assembly of an in vitro synthesized E. coli outer membrane porin into its stable trimeric configuration
    • de Cock H., Hendriks R., de Vrije T., Tommassen J. Assembly of an in vitro synthesized E. coli outer membrane porin into its stable trimeric configuration. J. Biol. Chem. 265:1990;4646-4651.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4646-4651
    • De Cock, H.1    Hendriks, R.2    De Vrije, T.3    Tommassen, J.4
  • 34
    • 0021355937 scopus 로고
    • Amino terminus of outer membrane PhoE protein: Localization by use of a bla-phoE hybrid gene
    • Tommassen J., Lugtenberg B. Amino terminus of outer membrane PhoE protein: localization by use of a bla-phoE hybrid gene. J. Bacteriol. 157:1984;327-329.
    • (1984) J. Bacteriol. , vol.157 , pp. 327-329
    • Tommassen, J.1    Lugtenberg, B.2
  • 35
    • 0018888099 scopus 로고
    • Characterization of serologically dominant outer membrane proteins of Neisseria gonorrhoeae
    • McDade R.L., Johnston K.H. Characterization of serologically dominant outer membrane proteins of Neisseria gonorrhoeae. J. Bacteriol. 141:1980;1183-1191.
    • (1980) J. Bacteriol. , vol.141 , pp. 1183-1191
    • McDade, R.L.1    Johnston, K.H.2
  • 36
    • 0018828456 scopus 로고
    • Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae
    • Newhall W.J., Sawyer W.D., Haak R.A. Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae. Infect. Immun. 28:1980;785-791.
    • (1980) Infect. Immun. , vol.28 , pp. 785-791
    • Newhall, W.J.1    Sawyer, W.D.2    Haak, R.A.3
  • 37
    • 0024348145 scopus 로고
    • Sequence of the structural gene (rmpM) for the class 4 outer membrane protein of Neisseria meningitidis, homology of the protein to gonococcal protein III and Escherichia coli OmpA, and construction of meningococcal strains that lack class 4 protein
    • Klugman K.P., Gotschlich E.C., Blake M.S. Sequence of the structural gene (rmpM) for the class 4 outer membrane protein of Neisseria meningitidis, homology of the protein to gonococcal protein III and Escherichia coli OmpA, and construction of meningococcal strains that lack class 4 protein. Infect. Immun. 57:1989;2066-2071.
    • (1989) Infect. Immun. , vol.57 , pp. 2066-2071
    • Klugman, K.P.1    Gotschlich, E.C.2    Blake, M.S.3
  • 38
    • 0018378684 scopus 로고
    • Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli
    • Benz R., Janko R., Läuger P. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta. 551:1979;238-257.
    • (1979) Biochim. Biophys. Acta , vol.551 , pp. 238-257
    • Benz, R.1    Janko, R.2    Läuger, P.3
  • 39
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: Insights from electrophysiology
    • Delcour A. Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol. Lett. 151:1997;115-123.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 115-123
    • Delcour, A.1
  • 40
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a β-barrel membrane protein
    • Surrey T., Jähnig F. Kinetics of folding and membrane insertion of a β-barrel membrane protein. J. Biol. Chem. 270:1995;28199-28203.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jähnig, F.2
  • 41
    • 0030045746 scopus 로고    scopus 로고
    • Folding and membrane insertion of the trimeric β-barrel protein OmpF
    • Surrey T., Schmid A., Jähnig F. Folding and membrane insertion of the trimeric β-barrel protein OmpF. Biochemistry. 35:1996;2283-2288.
    • (1996) Biochemistry , vol.35 , pp. 2283-2288
    • Surrey, T.1    Schmid, A.2    Jähnig, F.3
  • 43
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
    • Kreusch A., Neubüser A., Schiltz E., Weckesser J., Schulz G.E. Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3:1994;58-63.
    • (1994) Protein Sci. , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubüser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 44
    • 0032566609 scopus 로고    scopus 로고
    • Characterization of the structure, function and conformational stability of PorB class 3 protein from Neisseria meningitidis. A porin with unusual physicochemical properties
    • Minetti C.A.S.A., Blake M.S., Remeta D.P. Characterization of the structure, function and conformational stability of PorB class 3 protein from Neisseria meningitidis. A porin with unusual physicochemical properties. J. Biol. Chem. 273:1998;25329-25338.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25329-25338
    • Minetti, C.A.S.A.1    Blake, M.S.2    Remeta, D.P.3
  • 45
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A., Schulz G.E. Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5:1998;1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 47
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16:1995;1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 48
    • 0029984887 scopus 로고    scopus 로고
    • A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1
    • Neumann U., Schiltz E., Stahl B., Hillenkamp F., Weckesser J. A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1. FEMS Microbiol. Lett. 138:1996;55-58.
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 55-58
    • Neumann, U.1    Schiltz, E.2    Stahl, B.3    Hillenkamp, F.4    Weckesser, J.5
  • 50
    • 0031824098 scopus 로고    scopus 로고
    • The cell wall porin of Nocardia farcinica: Biochemical identification of the channel-forming protein and biophysical characterization of the channel properties
    • Rieß F.G., Lichtinger T., Cseh R., Yassin A.F., Schaal K.P., Benz R. The cell wall porin of Nocardia farcinica: biochemical identification of the channel-forming protein and biophysical characterization of the channel properties. Mol. Microbiol. 29:1998;139-150.
    • (1998) Mol. Microbiol. , vol.29 , pp. 139-150
    • Rieß, F.G.1    Lichtinger, T.2    Cseh, R.3    Yassin, A.F.4    Schaal, K.P.5    Benz, R.6
  • 51
    • 9344223315 scopus 로고    scopus 로고
    • X-Ray crystallographic and mass spectrometric structure determination and functional characterization of succinylated porin from Rhodobacter capsulatus: Implications for ion selectivity and single-channel conductance
    • Przybylski M., Glocker M.O., Nestel U., Schnaible V., Blüggel M., Diederichs K., Weckesser J., Schad M., Schmid A., Welte W., Benz R. X-Ray crystallographic and mass spectrometric structure determination and functional characterization of succinylated porin from Rhodobacter capsulatus: implications for ion selectivity and single-channel conductance. Protein Sci. 5:1996;1477-1489.
    • (1996) Protein Sci. , vol.5 , pp. 1477-1489
    • Przybylski, M.1    Glocker, M.O.2    Nestel, U.3    Schnaible, V.4    Blüggel, M.5    Diederichs, K.6    Weckesser, J.7    Schad, M.8    Schmid, A.9    Welte, W.10    Benz, R.11
  • 52
    • 0025815219 scopus 로고
    • The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin
    • Brunen M., Engelhardt H., Schmid A., Benz R. The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin. J. Bacteriol. 173:1991;4182-4187.
    • (1991) J. Bacteriol. , vol.173 , pp. 4182-4187
    • Brunen, M.1    Engelhardt, H.2    Schmid, A.3    Benz, R.4
  • 53
    • 0031658512 scopus 로고    scopus 로고
    • Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes
    • Mathes A., Engelhardt H. Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes. Biophys. J. 75:1998;1255-1262.
    • (1998) Biophys. J. , vol.75 , pp. 1255-1262
    • Mathes, A.1    Engelhardt, H.2
  • 54
    • 0033064921 scopus 로고    scopus 로고
    • Meningococcal PorA/C1, a channel that combines high conductance and high selectivity
    • Song J., Minetti C.A.S.A., Blake M.S., Colombini M. Meningococcal PorA/C1, a channel that combines high conductance and high selectivity. Biophys. J. 76:1999;804-813.
    • (1999) Biophys. J. , vol.76 , pp. 804-813
    • Song, J.1    Minetti, C.A.S.A.2    Blake, M.S.3    Colombini, M.4
  • 55
    • 0025359486 scopus 로고
    • Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity
    • McGuinness B., Barlow A.K., Clarke I.N., Farley J.E., Anilionis A., Poolman J.T., Heckels J.E. Deduced amino acid sequences of class 1 protein (PorA) from three strains of Neisseria meningitidis. Synthetic peptides define the epitopes responsible for serosubtype specificity. J. Exp. Med. 171:1990;1871-1882.
    • (1990) J. Exp. Med. , vol.171 , pp. 1871-1882
    • McGuinness, B.1    Barlow, A.K.2    Clarke, I.N.3    Farley, J.E.4    Anilionis, A.5    Poolman, J.T.6    Heckels, J.E.7
  • 56
    • 0029954217 scopus 로고    scopus 로고
    • Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: Parallels between pathogen accommodation and mitochondrial endosymbiosis
    • Rudel T., Schmid A., Benz R., Kolb H.A., Lang F., Meyer T.F. Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: parallels between pathogen accommodation and mitochondrial endosymbiosis. Cell. 85:1996;391-402.
    • (1996) Cell , vol.85 , pp. 391-402
    • Rudel, T.1    Schmid, A.2    Benz, R.3    Kolb, H.A.4    Lang, F.5    Meyer, T.F.6
  • 57
    • 0020773877 scopus 로고
    • Properties of the outer membrane protein from Neisseria gonorrhoeae incorporated into model lipid membranes
    • Young J.D.E., Blake M., Mauro A., Cohn Z.A. Properties of the outer membrane protein from Neisseria gonorrhoeae incorporated into model lipid membranes. Proc. Natl. Acad. Sci. USA. 80:1983;3831-3835.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3831-3835
    • Young, J.D.E.1    Blake, M.2    Mauro, A.3    Cohn, Z.A.4
  • 58
    • 0342649553 scopus 로고
    • Voltage gating of conductance in lipid bilayers induced by porin from outer membrane of Neisseria gonorrhoeae
    • Mauro A., Blake M., Labarca P. Voltage gating of conductance in lipid bilayers induced by porin from outer membrane of Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. USA. 85:1988;1071-1075.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1071-1075
    • Mauro, A.1    Blake, M.2    Labarca, P.3
  • 59
    • 0024833498 scopus 로고
    • The voltage-dependent activity of Escherichia coli porins in different planar bilayer reconstitutions
    • Lakey J.H., Pattus F. The voltage-dependent activity of Escherichia coli porins in different planar bilayer reconstitutions. Eur. J. Biochem. 186:1989;303-308.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 303-308
    • Lakey, J.H.1    Pattus, F.2
  • 62
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid B., Krömer M., Schulz G.E. Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381:1996;111-114.
    • (1996) FEBS Lett. , vol.381 , pp. 111-114
    • Schmid, B.1    Krömer, M.2    Schulz, G.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.