메뉴 건너뛰기




Volumn 21, Issue 4, 1996, Pages 787-797

DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; PILIN; UNCLASSIFIED DRUG; DSBA PROTEIN;

EID: 0029774730     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.431403.x     Document Type: Article
Times cited : (119)

References (55)
  • 1
    • 0026625932 scopus 로고
    • icsB: A Shigella flexneri virulence gene necessary for the lysis of protrusions during intercellular spread
    • Allaoui, A., Mounier, J., Prévost, M.-C., Sansonetti, P.J., and Parsot, C. (1992) icsB: a Shigella flexneri virulence gene necessary for the lysis of protrusions during intercellular spread. Mol Microbiol 6: 1605-1616.
    • (1992) Mol Microbiol , vol.6 , pp. 1605-1616
    • Allaoui, A.1    Mounier, J.2    Prévost, M.-C.3    Sansonetti, P.J.4    Parsot, C.5
  • 2
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C., McGovern, K., and Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 3
    • 0028282814 scopus 로고
    • Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi
    • Bortoli-German, I., Brun, E., Py, B., Chippaux, M., and Barras, F. (1994) Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi. Mol Microbiol 11: 545-553.
    • (1994) Mol Microbiol , vol.11 , pp. 545-553
    • Bortoli-German, I.1    Brun, E.2    Py, B.3    Chippaux, M.4    Barras, F.5
  • 4
    • 0021943866 scopus 로고
    • Supercoil sequencing: A fast and simple method for sequencing plasmid DNA
    • Chen, E.Y., and Seeburg, P.H. (1985) Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA 4: 165-170.
    • (1985) DNA , vol.4 , pp. 165-170
    • Chen, E.Y.1    Seeburg, P.H.2
  • 5
    • 0022357999 scopus 로고
    • Plasmid-mediated virulence in Salmonella dublin demonstrated by use of a Tn5-oriT construct
    • Chikami, G.K., Fierer, J., and Guiney, D.G. (1985) Plasmid-mediated virulence in Salmonella dublin demonstrated by use of a Tn5-oriT construct. Infect Immun 50: 420-424.
    • (1985) Infect Immun , vol.50 , pp. 420-424
    • Chikami, G.K.1    Fierer, J.2    Guiney, D.G.3
  • 6
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey, F.E., and Berg, H.C. (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc Natl Acad Sci USA 90: 1043-1047.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1043-1047
    • Dailey, F.E.1    Berg, H.C.2
  • 7
    • 0027483426 scopus 로고
    • Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperonepilus subunit complexes
    • Dodson, K.W., Jacob-Dubuisson, F., Striker, R.T., and Hultgren, S.J. (1993) Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperonepilus subunit complexes. Proc Natl Acad Sci USA 90: 3670-3674.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3670-3674
    • Dodson, K.W.1    Jacob-Dubuisson, F.2    Striker, R.T.3    Hultgren, S.J.4
  • 8
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A.J., and Williams, D.H. (1991) Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J Mol Biol 217: 389-398.
    • (1991) J Mol Biol , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 9
    • 0001102041 scopus 로고
    • Enteropathogenic Escherichia coli
    • Blaser, M.J., Smith, P.D., Ravdin, J.I., Greenberg, H.B., and Guerrant, R.L. (eds). New York: Raven Press Ltd
    • Donnenberg, M.S. (1995) Enteropathogenic Escherichia coli. In Infections of the Gastrointestinal Tract. Blaser, M.J., Smith, P.D., Ravdin, J.I., Greenberg, H.B., and Guerrant, R.L. (eds). New York: Raven Press Ltd, pp. 709-726.
    • (1995) Infections of the Gastrointestinal Tract , pp. 709-726
    • Donnenberg, M.S.1
  • 10
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg, M.S., and Kaper, J.B. (1991) Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect Immun 59:4310-4317.
    • (1991) Infect Immun , vol.59 , pp. 4310-4317
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 11
    • 0025285812 scopus 로고
    • Construction and analysis of TnphoA mutants of enteropathogenic Escherichia coli unable to invade HEp-2 cells
    • Donnenberg, M.S., Calderwood, S.B., Donohue-Rolfe, A., Keusch, G.T., and Kaper, J.B. (1990) Construction and analysis of TnphoA mutants of enteropathogenic Escherichia coli unable to invade HEp-2 cells. Infect Immun 58: 1565-1571.
    • (1990) Infect Immun , vol.58 , pp. 1565-1571
    • Donnenberg, M.S.1    Calderwood, S.B.2    Donohue-Rolfe, A.3    Keusch, G.T.4    Kaper, J.B.5
  • 12
    • 0026482190 scopus 로고
    • A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence
    • Donnenberg, M.S., Girön, J.A., Nataro, J.P., and Kaper, J.B. (1992) A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence. Mol Microbiol 6: 3427-3437.
    • (1992) Mol Microbiol , vol.6 , pp. 3427-3437
    • Donnenberg, M.S.1    Girön, J.A.2    Nataro, J.P.3    Kaper, J.B.4
  • 13
    • 0027250343 scopus 로고
    • A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells
    • Donnenberg, M.S., Yu, J., and Kaper, J.B. (1993) A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells. J Bacteriol 175: 4670-4680.
    • (1993) J Bacteriol , vol.175 , pp. 4670-4680
    • Donnenberg, M.S.1    Yu, J.2    Kaper, J.B.3
  • 14
    • 0028182415 scopus 로고
    • Molecular analysis of archaeal flagellins: Similarity to the type IV pilin-transport superfamily widespread in bacteria
    • Faguy, D.M., Jarrell, K.F., Kuzio, J., and Kalmokoff, M.L. (1994) Molecular analysis of archaeal flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria. Can J Microbiol 40: 67-71.
    • (1994) Can J Microbiol , vol.40 , pp. 67-71
    • Faguy, D.M.1    Jarrell, K.F.2    Kuzio, J.3    Kalmokoff, M.L.4
  • 15
    • 0028100375 scopus 로고
    • Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in mice
    • Farinha, M.A., Conway, B.D., Glasier, L.M.G., Ellert, N.W., Irvin, R.T., Sherburne, R., and Paranchych, W. (1994) Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in mice. Infect Immun 62: 4118-4123.
    • (1994) Infect Immun , vol.62 , pp. 4118-4123
    • Farinha, M.A.1    Conway, B.D.2    Glasier, L.M.G.3    Ellert, N.W.4    Irvin, R.T.5    Sherburne, R.6    Paranchych, W.7
  • 16
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.P., and Vogelstein, B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6-13.
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 17
    • 0026330896 scopus 로고
    • An inducible bundle-forming pilus of enteropathogenic Escherichia coli
    • Girón, J.A., Ho, A.S.Y., and Schoolnik, G.K. (1991) An inducible bundle-forming pilus of enteropathogenic Escherichia coli. Science 254: 710-713.
    • (1991) Science , vol.254 , pp. 710-713
    • Girón, J.A.1    Ho, A.S.Y.2    Schoolnik, G.K.3
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Harlow, D.H., and Lane, D. (1988) Antibodies, a Laboratory Manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1988) Antibodies, a Laboratory Manual
    • Harlow, D.H.1    Lane, D.2
  • 19
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: A general system for the formation of surface-associated protein complexes
    • Hobbs, M., and Mattick, J.S. (1993) Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol Microbiol 10: 233-243.
    • (1993) Mol Microbiol , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 20
  • 21
    • 0025047435 scopus 로고
    • A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells
    • Jerse, A.E., Yu, J., Tall, B.D., and Kaper, J.B. (1990) A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc Natl Acad Sci USA 87: 7839-7843.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7839-7843
    • Jerse, A.E.1    Yu, J.2    Tall, B.D.3    Kaper, J.B.4
  • 23
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Akiyama, Y., and Ito, K. (1992) Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J 11: 57-62.
    • (1992) EMBO J , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 24
    • 0025944413 scopus 로고
    • Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by Gram-negative bacteria
    • Kaufman, M.R., Seyer, J.M., and Taylor, R.K. (1991) Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by Gram-negative bacteria. Genes Dev5: 1834-1846.
    • (1991) Genes Dev , vol.5 , pp. 1834-1846
    • Kaufman, M.R.1    Seyer, J.M.2    Taylor, R.K.3
  • 25
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 26
    • 0026509588 scopus 로고
    • P pili in uropathogenic E coli are composite fibres with distinct fibrillar adhesive tips
    • Kuehn, M.J., Heuser, J., Normark, S., and Hultgren, S.J. (1992) P pili in uropathogenic E coli are composite fibres with distinct fibrillar adhesive tips. Nature 356: 252-255.
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 27
    • 0028365476 scopus 로고
    • The binding of Pseudomonas aeruginosa pili to glycosphingolipids is a tip-associated event involving the C-terminal region of the structural pilin subunit
    • Lee, K.K., Sheth, H.B., Wong, W.Y., Sherburne, R., Paranchych, W., Hodges, R.S., Lingwood, C.A., Krivan, H., and Irvin, R.T. (1994) The binding of Pseudomonas aeruginosa pili to glycosphingolipids is a tip-associated event involving the C-terminal region of the structural pilin subunit. Mol Microbiol 11: 705-713.
    • (1994) Mol Microbiol , vol.11 , pp. 705-713
    • Lee, K.K.1    Sheth, H.B.2    Wong, W.Y.3    Sherburne, R.4    Paranchych, W.5    Hodges, R.S.6    Lingwood, C.A.7    Krivan, H.8    Irvin, R.T.9
  • 28
    • 0021825282 scopus 로고
    • The diarrheal response of humans to some classic serotypes of enteropathogenic Escherichia coli is dependent on a plasmid encoding an enteroadhesiveness factor
    • Levine, M.M., Nataro, J.P., Karch, H., Baldini, M.M., Kaper, J.B., Black, R.E., Clements, M.L., and O'Brien, A.D. (1985) The diarrheal response of humans to some classic serotypes of enteropathogenic Escherichia coli is dependent on a plasmid encoding an enteroadhesiveness factor. J Infect Dis 152: 550-559.
    • (1985) J Infect Dis , vol.152 , pp. 550-559
    • Levine, M.M.1    Nataro, J.P.2    Karch, H.3    Baldini, M.M.4    Kaper, J.B.5    Black, R.E.6    Clements, M.L.7    O'Brien, A.D.8
  • 29
  • 30
    • 0027244956 scopus 로고
    • Non-polar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells
    • Ménard, R., Sansonetti, P.J., and Parsot, C. (1993) Non-polar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J Bacteriol 175: 5899-5906.
    • (1993) J Bacteriol , vol.175 , pp. 5899-5906
    • Ménard, R.1    Sansonetti, P.J.2    Parsot, C.3
  • 31
    • 0003842951 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1992) A Short Course in Bacterial Genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 32
    • 0023227547 scopus 로고
    • Characterization of plasmids encoding the adherence factor of enteropathogenic Escherichia coli
    • Nataro, J.P., Maher, K.O., Mackie, P., and Kaper, J.B. (1987) Characterization of plasmids encoding the adherence factor of enteropathogenic Escherichia coli. Infect Immun 55: 2370-2377.
    • (1987) Infect Immun , vol.55 , pp. 2370-2377
    • Nataro, J.P.1    Maher, K.O.2    Mackie, P.3    Kaper, J.B.4
  • 33
    • 0023721293 scopus 로고
    • The physiology and biochemistry of pili
    • Paranchych, W., and Frost, L.S. (1988) The physiology and biochemistry of pili. Adv Microb Physiol 29: 53-114.
    • (1988) Adv Microb Physiol , vol.29 , pp. 53-114
    • Paranchych, W.1    Frost, L.S.2
  • 35
    • 0024041477 scopus 로고
    • The expression of mutant pilins in Pseudomonas aeruginosa: Fifth postion glutamate affects pilin methylation
    • Pasloske, B.L., and Paranchych, W. (1988) The expression of mutant pilins in Pseudomonas aeruginosa: fifth postion glutamate affects pilin methylation. Mol Microbiol 2: 489-495.
    • (1988) Mol Microbiol , vol.2 , pp. 489-495
    • Pasloske, B.L.1    Paranchych, W.2
  • 36
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
    • Peek, J.A., and Taylor, R.K. (1992) Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc Natl Acad Sci USA 89: 6210-6214.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 37
    • 0027535103 scopus 로고
    • A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF gene
    • Pugsley, A.P. (1993) A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF gene. Mol Gen Genet 237: 407-411.
    • (1993) Mol Gen Genet , vol.237 , pp. 407-411
    • Pugsley, A.P.1
  • 38
    • 0028306098 scopus 로고
    • Beta-lactamase topology probe analysis of the OutO NMePhe peptidase, and six other Out protein components of the Erwinia carotovora general secretion pathway apparatus
    • Reeves, P.J., Douglas, P., and Salmond, G.P.C. (1994) Beta-lactamase topology probe analysis of the OutO NMePhe peptidase, and six other Out protein components of the Erwinia carotovora general secretion pathway apparatus. Mol Microbiol 12: 445-457.
    • (1994) Mol Microbiol , vol.12 , pp. 445-457
    • Reeves, P.J.1    Douglas, P.2    Salmond, G.P.C.3
  • 39
    • 0027428606 scopus 로고
    • Pseudomonas aeruginosa pili bind to asialoGM1 which is increased on the surface of cystic fibrosis epithelial cells
    • Saiman, L., and Prince, A. (1993) Pseudomonas aeruginosa pili bind to asialoGM1 which is increased on the surface of cystic fibrosis epithelial cells. J Clin Invest 92: 1875-1880.
    • (1993) J Clin Invest , vol.92 , pp. 1875-1880
    • Saiman, L.1    Prince, A.2
  • 41
    • 0021274267 scopus 로고
    • Distinctive patterns of adherence of enteropathogenic Escherichia coli to HeLa cells
    • Scaletsky, I.C.A., Silva, M.L.M., and Trabulsi, L.R. (1984) Distinctive patterns of adherence of enteropathogenic Escherichia coli to HeLa cells. Infect Immun 45: 534-536.
    • (1984) Infect Immun , vol.45 , pp. 534-536
    • Scaletsky, I.C.A.1    Silva, M.L.M.2    Trabulsi, L.R.3
  • 42
    • 0028342695 scopus 로고
    • Multiple gonococcal pilin antigenic variants are produced during experimental human infections
    • Seifert, H.S., Wright, C.J., Jerse, A.E., Cohen, M.S., and Cannon, J.G. (1994) Multiple gonococcal pilin antigenic variants are produced during experimental human infections. J Clin Invest 93: 2744-2749.
    • (1994) J Clin Invest , vol.93 , pp. 2744-2749
    • Seifert, H.S.1    Wright, C.J.2    Jerse, A.E.3    Cohen, M.S.4    Cannon, J.G.5
  • 43
    • 0029975939 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli: Identification of a gene cluster coding for Bundle-Forming Pilus morphogenesis
    • Sohel, I., Puente, J.L., Ramer, S.W., Bieber, D., Wu, C.-Y., and Schoolnik, G.K. (1996) Enteropathogenic Escherichia coli: identification of a gene cluster coding for Bundle-Forming Pilus morphogenesis. J Bacteriol 178: 2613-2628.
    • (1996) J Bacteriol , vol.178 , pp. 2613-2628
    • Sohel, I.1    Puente, J.L.2    Ramer, S.W.3    Bieber, D.4    Wu, C.-Y.5    Schoolnik, G.K.6
  • 44
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus
    • Stone, K.D., Zhang, H.-Z., Carlson, L.K., and Donnenberg, M.S. (1996) A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus. Mol Microbiol 20: 325-337.
    • (1996) Mol Microbiol , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.-Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 45
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • Strauch, K.L., and Beckwith, J. (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc Natl Acad Sci USA 85: 1576-1580.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 46
    • 0025978598 scopus 로고
    • Amino acid substitutions in pilin of Pseudomona aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly
    • Strom, M.S., and Lory, S. (1991) Amino acid substitutions in pilin of Pseudomona aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly. J Biol Chem 266: 1656-1664.
    • (1991) J Biol Chem , vol.266 , pp. 1656-1664
    • Strom, M.S.1    Lory, S.2
  • 47
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of the type IV pili
    • Strom, M.S., and Lory, S. (1993) Structure-function and biogenesis of the type IV pili. Ann Rev Microbiol 47: 565-596.
    • (1993) Ann Rev Microbiol , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 48
    • 0027528605 scopus 로고
    • A single bifunctional enzyme, PilD, catalyses cleavage and N-methylation of proteins belonging to the type IV pilin family
    • Strom, M.S., Nunn, D.N., and Lory, S. (1993) A single bifunctional enzyme, PilD, catalyses cleavage and N-methylation of proteins belonging to the type IV pilin family. Proc Natl Acad Sci USA 90: 2404-2408.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2404-2408
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 49
    • 0026034189 scopus 로고
    • Localization of protective epitopes within the pilin subunit of the Vibrio cholerae toxin-coregulated pilus
    • Sun, D., Seyer, J.M., Kovari, I., Sumrada, R.A., and Taylor, R.K. (1991) Localization of protective epitopes within the pilin subunit of the Vibrio cholerae toxin-coregulated pilus. Infect Immun 59: 114-118.
    • (1991) Infect Immun , vol.59 , pp. 114-118
    • Sun, D.1    Seyer, J.M.2    Kovari, I.3    Sumrada, R.A.4    Taylor, R.K.5
  • 50
    • 0025806533 scopus 로고
    • Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme
    • Taniyama, Y., Kuroki, R., Omura, F., Seko, C., and Kikuchi, M. (1991) Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. J Biol Chem 266: 6456-6461.
    • (1991) J Biol Chem , vol.266 , pp. 6456-6461
    • Taniyama, Y.1    Kuroki, R.2    Omura, F.3    Seko, C.4    Kikuchi, M.5
  • 51
    • 0026459569 scopus 로고
    • A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd
    • Tomb, J.-F. (1992) A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd. Proc Natl Acad Sci USA 89: 10252-10256.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10252-10256
    • Tomb, J.-F.1
  • 52
    • 0027366752 scopus 로고
    • The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains
    • Whitley, P., and Von Heijne, G. (1993) The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains. FEBS Lett 332: 49-51.
    • (1993) FEBS Lett , vol.332 , pp. 49-51
    • Whitley, P.1    Von Heijne, G.2
  • 53
    • 0028356277 scopus 로고
    • Maturation pathway of Escherichia coli heat-stable enterotoxin I: Requirement of DsbA for disulfide bond formation
    • Yamanaka, H., Kameyama, M., Baba, T., Fujii, Y., and Okamoto, K. (1994) Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation. J Bacteriol 176: 2906-2913.
    • (1994) J Bacteriol , vol.176 , pp. 2906-2913
    • Yamanaka, H.1    Kameyama, M.2    Baba, T.3    Fujii, Y.4    Okamoto, K.5
  • 54
    • 0026633141 scopus 로고
    • A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae
    • Yu, J., Webb, H., and Hirst, T.R. (1992) A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae. Mol Microbiol 6: 1949-1958.
    • (1992) Mol Microbiol , vol.6 , pp. 1949-1958
    • Yu, J.1    Webb, H.2    Hirst, T.R.3
  • 55
    • 0028117722 scopus 로고
    • A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli
    • Zhang, H.-Z., Lory, S., and Donnenberg, M.S. (1994) A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli. J Bacteriol 176: 6885-6891.
    • (1994) J Bacteriol , vol.176 , pp. 6885-6891
    • Zhang, H.-Z.1    Lory, S.2    Donnenberg, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.