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Volumn 290, Issue 3, 1999, Pages 741-756

Structural predictions of AgfA, the insoluble fimbrial subunit of Salmonella thin aggregative fimbriae

Author keywords

AgfA; Fimbrin; Salmonella; SEF17; Thin aggregative fimbriae

Indexed keywords

METALLOPROTEINASE; MYELIN BASIC PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN SUBUNIT; PROTEINASE; STRUCTURAL PROTEIN;

EID: 0032788736     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2882     Document Type: Article
Times cited : (102)

References (87)
  • 1
    • 0021813667 scopus 로고
    • Protection against Escherichia coli -induced urinary tract infections with hybridoma antibodies directed against type 1 fimbriae or complementary D -mannose receptors
    • Abraham S. N., Babu J. P., Giampapa C. S., Hasty D. L., Simpson W. A., Beachey E. H. Protection against Escherichia coli -induced urinary tract infections with hybridoma antibodies directed against type 1 fimbriae or complementary D -mannose receptors. Infect. Immun. 48:1985;625-628.
    • (1985) Infect. Immun. , vol.48 , pp. 625-628
    • Abraham, S.N.1    Babu, J.P.2    Giampapa, C.S.3    Hasty, D.L.4    Simpson, W.A.5    Beachey, E.H.6
  • 2
    • 0032525168 scopus 로고    scopus 로고
    • Thin aggregative fimbriae enhance Salmonella enteritidis biofilm formation
    • Austin J. W., Sanders G., Kay W. W., Collinson S. K. Thin aggregative fimbriae enhance Salmonella enteritidis biofilm formation. FEMS Microbiol. Letters. 162:1998;295-301.
    • (1998) FEMS Microbiol. Letters , vol.162 , pp. 295-301
    • Austin, J.W.1    Sanders, G.2    Kay, W.W.3    Collinson, S.K.4
  • 3
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo-protease from Serratia mercescens
    • Baumann U. Crystal structure of the 50 kDa metallo-protease from Serratia mercescens. J. Mol. Biol. 242:1994;244-251.
    • (1994) J. Mol. Biol. , vol.242 , pp. 244-251
    • Baumann, U.1
  • 4
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann U., Wu S., Flaherty K. M., McKay D. B. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12:1993;3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 5
    • 0029042476 scopus 로고
    • Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi
    • Baumann U., Bauer M., Létoffé S., Delepelaire P., Wandersman C. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. J. Mol. Biol. 248:1995;653-661.
    • (1995) J. Mol. Biol. , vol.248 , pp. 653-661
    • Baumann, U.1    Bauer, M.2    Létoffé, S.3    Delepelaire, P.4    Wandersman, C.5
  • 6
    • 0028913176 scopus 로고
    • Identification and sequence analysis of lpfABCDE, a putative fimbrial operon of Salmonella typhimurium
    • Bäumler A. J., Heffron F. Identification and sequence analysis of lpfABCDE, a putative fimbrial operon of Salmonella typhimurium. J. Bacteriol. 177:1995;2087-2097.
    • (1995) J. Bacteriol. , vol.177 , pp. 2087-2097
    • Bäumler, A.J.1    Heffron, F.2
  • 7
    • 0031023006 scopus 로고    scopus 로고
    • Contribution of horizontal gene transfer and deletion events to development of distinctive patterns of fimbrial operons during evolution of Salmonella serotypes
    • Bäumler A. J., Gilde A. J., Tsolis R. M., van der Velden A. W. M., Ahmer B. M. M., Heffron F. Contribution of horizontal gene transfer and deletion events to development of distinctive patterns of fimbrial operons during evolution of Salmonella serotypes. J. Bacteriol. 179:1997;317-322.
    • (1997) J. Bacteriol. , vol.179 , pp. 317-322
    • Bäumler, A.J.1    Gilde, A.J.2    Tsolis, R.M.3    Van Der Velden, A.W.M.4    Ahmer, B.M.M.5    Heffron, F.6
  • 9
    • 0025333259 scopus 로고
    • The metalloprotease gene of Serratia marcescens strain SM6
    • Braunagel S. C., Benedik M. J. The metalloprotease gene of Serratia marcescens strain SM6. Mol. Gen. Genet. 222:1990;446-451.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 446-451
    • Braunagel, S.C.1    Benedik, M.J.2
  • 10
    • 0343668561 scopus 로고
    • The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in Gram negative bacteria
    • Brinton C. C. Jr. The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in Gram negative bacteria. Trans. NY Acad. Sci. 27:1965;1003-1054.
    • (1965) Trans. NY Acad. Sci. , vol.27 , pp. 1003-1054
    • Brinton C.C., Jr.1
  • 11
    • 0025833413 scopus 로고
    • Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis
    • Collinson S. K., Emödy L., Müller K.-H., Trust T. J., Kay W. W. Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis. J. Bacteriol. 173:1991;4773-4781.
    • (1991) J. Bacteriol. , vol.173 , pp. 4773-4781
    • Collinson, S.K.1    Emödy, L.2    Müller, K.-H.3    Trust, T.J.4    Kay, W.W.5
  • 12
    • 0026729521 scopus 로고
    • Thin aggregative fimbriae from diarrheagenic Escherichia coli
    • Collinson S. K., Emödy L., Trust T. J., Kay W. W. Thin aggregative fimbriae from diarrheagenic Escherichia coli. J. Bacteriol. 174:1992;4490-4495.
    • (1992) J. Bacteriol. , vol.174 , pp. 4490-4495
    • Collinson, S.K.1    Emödy, L.2    Trust, T.J.3    Kay, W.W.4
  • 15
    • 0029919032 scopus 로고    scopus 로고
    • The location of four fimbrin-encoding genes, agfA, fimA, sefA and sefD, on the Salmonella enteritidis and/or S. typhimurium Xba I- Bln I genomic restriction maps
    • Collinson S. K., Liu S.-L., Clouthier S. C., Banser P. A., Doran J. L., Sanderson K. E., Kay W. W. The location of four fimbrin-encoding genes, agfA, fimA, sefA and sefD, on the Salmonella enteritidis and/or S. typhimurium Xba I- Bln I genomic restriction maps. Gene. 169:1996b;75-80.
    • (1996) Gene , vol.169 , pp. 75-80
    • Collinson, S.K.1    Liu, S.-L.2    Clouthier, S.C.3    Banser, P.A.4    Doran, J.L.5    Sanderson, K.E.6    Kay, W.W.7
  • 16
    • 0027310780 scopus 로고
    • Crystallographic studies on a family of cellular lipophilic transport proteins
    • Cowan S. W., Newcomer M. E., Jones T. A. Crystallographic studies on a family of cellular lipophilic transport proteins. J. Mol. Biol. 230:1993;1225-1246.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1225-1246
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 18
    • 0028046269 scopus 로고
    • Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences
    • Der Vartanian M., Méchin M.-C., Jaffeux B., Bertin Y., Félix I., Gaillard-Martinie B. Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences. Gene. 148:1994;23-32.
    • (1994) Gene , vol.148 , pp. 23-32
    • Der, V.M.1    Méchin, M.-C.2    Jaffeux, B.3    Bertin, Y.4    Félix, I.5    Gaillard-Martinie, B.6
  • 20
    • 0019845835 scopus 로고
    • Dissociation and reassembly of Escherichia coli type 1 pili
    • Eshdat Y., Silverblatt F. J., Sharon N. Dissociation and reassembly of Escherichia coli type 1 pili. J. Bacteriol. 148:1981;308-314.
    • (1981) J. Bacteriol. , vol.148 , pp. 308-314
    • Eshdat, Y.1    Silverblatt, F.J.2    Sharon, N.3
  • 21
    • 0000862044 scopus 로고    scopus 로고
    • Structure and function of the F factor and mechanism of conjugation
    • Neidhardt, F. C. 2401, American Society for Microbiology Press, Washington, DC
    • Firth, N. Ippen-Ihler, K. Skurray, R. A. 1996, Structure and function of the F factor and mechanism of conjugation, Escherichia coli and Salmonella Cellular and Molecular Biology, Neidhardt, F. C. 2377, 2401, American Society for Microbiology Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella Cellular and Molecular Biology , pp. 2377
    • Firth, N.1    Ippen-Ihler, K.2    Skurray, R.A.3
  • 22
    • 0029799766 scopus 로고    scopus 로고
    • Pilus assembly by Agrobacterium T-DNA transfer genes
    • Fullner K. J., Lara J. C., Nester E. W. Pilus assembly by Agrobacterium T-DNA transfer genes. Science. 273:1996;1107-1109.
    • (1996) Science , vol.273 , pp. 1107-1109
    • Fullner, K.J.1    Lara, J.C.2    Nester, E.W.3
  • 23
    • 0020315311 scopus 로고
    • Host-specific fimbrial adhesins of non-invasive enterotoxigenic Escherichia coli strains
    • Gaastra W., de Graaf F. K. Host-specific fimbrial adhesins of non-invasive enterotoxigenic Escherichia coli strains. Microbiol. Rev. 46:1982;129-161.
    • (1982) Microbiol. Rev. , vol.46 , pp. 129-161
    • Gaastra, W.1    De Graaf, F.K.2
  • 24
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 25
    • 0028854718 scopus 로고
    • Pilins of fimbrial adhesins of different member species of Enterobacteriaceae are structurally similar to the C-terminal half of adhesin proteins
    • Girardeau J.-P., Bertin Y. Pilins of fimbrial adhesins of different member species of Enterobacteriaceae are structurally similar to the C-terminal half of adhesin proteins. FEBS Letters. 357:1995;103-108.
    • (1995) FEBS Letters , vol.357 , pp. 103-108
    • Girardeau, J.-P.1    Bertin, Y.2
  • 26
    • 0025718896 scopus 로고
    • Sequence analysis of the clpG gene, which codes for surface antigen CS31A subunit: Evidence of an evolutionary relationship between CS31A, K88 and F41 subunit genes
    • Girardeau J.-P., Bertin Y., Martin C., Der Vartanian M., Boeuf C. Sequence analysis of the clpG gene, which codes for surface antigen CS31A subunit: evidence of an evolutionary relationship between CS31A, K88 and F41 subunit genes. J. Bacteriol. 173:1991;7673-7683.
    • (1991) J. Bacteriol. , vol.173 , pp. 7673-7683
    • Girardeau, J.-P.1    Bertin, Y.2    Martin, C.3    Der, V.M.4    Boeuf, C.5
  • 27
    • 0027049870 scopus 로고
    • Helical structure of P pili from Escherichia coli
    • Gong M., Makowski L. Helical structure of P pili from Escherichia coli. J. Mol. Biol. 228:1992;735-742.
    • (1992) J. Mol. Biol. , vol.228 , pp. 735-742
    • Gong, M.1    Makowski, L.2
  • 28
    • 0029561748 scopus 로고
    • Expression of two csg operons is required for production of fibronectin- And congo red-binding curli polymers in Escherichia coli K-12
    • Hammar M., Arvqvist A., Bian Z., Olsen A., Normark S. Expression of two csg operons is required for production of fibronectin- and congo red-binding curli polymers in Escherichia coli K-12. Mol. Microbiol. 18:1995;661-670.
    • (1995) Mol. Microbiol. , vol.18 , pp. 661-670
    • Hammar, M.1    Arvqvist, A.2    Bian, Z.3    Olsen, A.4    Normark, S.5
  • 29
    • 0030014444 scopus 로고    scopus 로고
    • Nucleator-dependent intercellular assembly of adhesive curli organelles in Escherichia coli
    • Hammar M., Bian Z., Normark S. Nucleator-dependent intercellular assembly of adhesive curli organelles in Escherichia coli. Proc. Natl Acad. Sci. USA. 93:1996;6562-6566.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6562-6566
    • Hammar, M.1    Bian, Z.2    Normark, S.3
  • 30
    • 0029932849 scopus 로고    scopus 로고
    • Three-dimensional structure of Bordetella pertussis fimbriae
    • Heck D. V., Trus B. L., Steven A. C. Three-dimensional structure of Bordetella pertussis fimbriae. J. Struct. Biol. 116:1996;264-269.
    • (1996) J. Struct. Biol. , vol.116 , pp. 264-269
    • Heck, D.V.1    Trus, B.L.2    Steven, A.C.3
  • 31
    • 0025082311 scopus 로고
    • The pili of Aeromonas hydrophila: Identification of an environmentally regulated "mini pilin"
    • Ho A. S. Y., Mietzner T. A., Smith A. J., Schoolnik G. K. The pili of Aeromonas hydrophila: identification of an environmentally regulated "mini pilin" J. Expl. Med. 172:1990;795-806.
    • (1990) J. Expl. Med. , vol.172 , pp. 795-806
    • Ho, A.S.Y.1    Mietzner, T.A.2    Smith, A.J.3    Schoolnik, G.K.4
  • 32
    • 0029115481 scopus 로고
    • A sequence property approach to searching protein databases
    • Hobohm U., Sanders C. A sequence property approach to searching protein databases. J. Mol. Biol. 251:1995;390-399.
    • (1995) J. Mol. Biol. , vol.251 , pp. 390-399
    • Hobohm, U.1    Sanders, C.2
  • 33
    • 0029738256 scopus 로고    scopus 로고
    • Molecular basis of two subfamilies of immunoglobulin-like chaperones
    • Hung D. L., Knight S. D., Woods R. M., Pinkner J. S., Hultgren S. J. Molecular basis of two subfamilies of immunoglobulin-like chaperones. EMBO J. 15:1996;3792-3805.
    • (1996) EMBO J. , vol.15 , pp. 3792-3805
    • Hung, D.L.1    Knight, S.D.2    Woods, R.M.3    Pinkner, J.S.4    Hultgren, S.J.5
  • 34
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones C. H., Danese P. N., Pinkner J. S., Silhavy T. J., Hultgren S. J. The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J. 16:1997;6394-6406.
    • (1997) EMBO J. , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 35
    • 0024027281 scopus 로고
    • The three-dimensional structure of P2 myelin protein
    • Jones T. A., Bergfors T., Sedzik J., Unge T. The three-dimensional structure of P2 myelin protein. EMBO J. 7:1988;1597-1604.
    • (1988) EMBO J. , vol.7 , pp. 1597-1604
    • Jones, T.A.1    Bergfors, T.2    Sedzik, J.3    Unge, T.4
  • 36
    • 0029874435 scopus 로고    scopus 로고
    • A left-handed β-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
    • Kisker C., Schindelin H., Alber B. E., Ferry J. G., Rees D. C. A left-handed β-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 15:1996;2323-2330.
    • (1996) EMBO J. , vol.15 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 37
    • 0021754353 scopus 로고
    • The fimA gene encoding the type-1 fimbrial subunit of Escherichia coli
    • Klemm P. The fimA gene encoding the type-1 fimbrial subunit of Escherichia coli. Eur. J. Biochem. 143:1984;395-399.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 395-399
    • Klemm, P.1
  • 39
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B., Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature. 366:1993;751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 40
    • 0018844838 scopus 로고
    • New method for isolation of immunologically pure pili from Escherichia coli
    • Korhonen T. K., Nurmiaho E.-L., Ranta H., Eden C. S. New method for isolation of immunologically pure pili from Escherichia coli. Infect. Immun. 27:1980;569-575.
    • (1980) Infect. Immun. , vol.27 , pp. 569-575
    • Korhonen, T.K.1    Nurmiaho, E.-L.2    Ranta, H.3    Eden, C.S.4
  • 41
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibers with distinct fibrillar adhesive tips
    • Kuehn M. J., Heuser J., Normark S., Hultgren S. J. P pili in uropathogenic E. coli are composite fibers with distinct fibrillar adhesive tips. Nature. 356:1992;252-255.
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0031923138 scopus 로고    scopus 로고
    • Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens
    • Lai E.-M., Kado C. I. Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens. J. Bacteriol. 180:1998;2711-2717.
    • (1998) J. Bacteriol. , vol.180 , pp. 2711-2717
    • Lai, E.-M.1    Kado, C.I.2
  • 45
    • 0031892333 scopus 로고    scopus 로고
    • Regulation of type 1 fimbrial expression in uropathogenic Escherichia coli: Heterogeneity of expression through sequence changes in the fim switch region
    • Leathart J. B. S., Gally D. L. Regulation of type 1 fimbrial expression in uropathogenic Escherichia coli: heterogeneity of expression through sequence changes in the fim switch region. Mol. Microbiol. 28:1998;371-381.
    • (1998) Mol. Microbiol. , vol.28 , pp. 371-381
    • Leathart, J.B.S.1    Gally, D.L.2
  • 47
    • 0028191528 scopus 로고
    • The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi
    • Lietzke S. E., Yoder M. D., Keen N. T., Jurnak F. The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol. 106:1994;849-862.
    • (1994) Plant Physiol. , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 50
    • 0028808909 scopus 로고
    • High adhesiveness of encapsulated Neisseriameningitidis to epithelial cells is associated with the formation of bundles of pili
    • Marceau M., Beretti J.-L., Nassif X. High adhesiveness of encapsulated Neisseriameningitidis to epithelial cells is associated with the formation of bundles of pili. Mol. Microbiol. 17:1995;855-863.
    • (1995) Mol. Microbiol. , vol.17 , pp. 855-863
    • Marceau, M.1    Beretti, J.-L.2    Nassif, X.3
  • 51
    • 0031914987 scopus 로고    scopus 로고
    • Consequences of the loss of O -linked glycosylation of menningococcal type IV pilin on piliation and pilus-mediated adhesion
    • Marceau M., Forest K., Béretti J.-L., Tainer J., Nassif X. Consequences of the loss of O -linked glycosylation of menningococcal type IV pilin on piliation and pilus-mediated adhesion. Mol. Microbiol. 27:1998;705-715.
    • (1998) Mol. Microbiol. , vol.27 , pp. 705-715
    • Marceau, M.1    Forest, K.2    Béretti, J.-L.3    Tainer, J.4    Nassif, X.5
  • 52
    • 0029039757 scopus 로고
    • Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins of Escherichia coli share a common overall fold and differ structurally from other fimbrial subunits
    • Méchin M.-C., Bertin Y., Girardeau J.-P. Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins of Escherichia coli share a common overall fold and differ structurally from other fimbrial subunits. FEBS Letters. 364:1995;319-324.
    • (1995) FEBS Letters , vol.364 , pp. 319-324
    • Méchin, M.-C.1    Bertin, Y.2    Girardeau, J.-P.3
  • 53
    • 0030273775 scopus 로고    scopus 로고
    • Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli
    • Mol O., Oudega B. Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli. FEMS Microbiol. Rev. 19:1996;25-52.
    • (1996) FEMS Microbiol. Rev. , vol.19 , pp. 25-52
    • Mol, O.1    Oudega, B.2
  • 55
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A. G., Brenner S. E., Hubbard T., Chothia C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 56
    • 0031081390 scopus 로고    scopus 로고
    • Antagonsitic effect of synthetic peptides corresponding to the binding regions within fimbrial subunit protein fromPorphyromonas gingivalis to human gingival fibroblasts
    • Ogawa T., Ogo H., Kinoshita A. Antagonsitic effect of synthetic peptides corresponding to the binding regions within fimbrial subunit protein fromPorphyromonas gingivalis to human gingival fibroblasts. Vaccine. 15:1997;230-236.
    • (1997) Vaccine , vol.15 , pp. 230-236
    • Ogawa, T.1    Ogo, H.2    Kinoshita, A.3
  • 57
    • 0027475041 scopus 로고
    • The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli
    • Olsén A., Arnqvist A., Hammar M., Sukupolvi S., Normark S. The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli. Mol. Microbiol. 7:1993;523-536.
    • (1993) Mol. Microbiol. , vol.7 , pp. 523-536
    • Olsén, A.1    Arnqvist, A.2    Hammar, M.3    Sukupolvi, S.4    Normark, S.5
  • 59
    • 0001804219 scopus 로고
    • Molecular studies on N -methylphenylalanine pili
    • Paranchych W. Molecular studies on N -methylphenylalanine pili. Bacteria. 11:1990;61-78.
    • (1990) Bacteria , vol.11 , pp. 61-78
    • Paranchych, W.1
  • 62
    • 0026246944 scopus 로고
    • Prediction of surface and interior regions in proteins - Part I: Linear tripeptide sequences identify structural boundaries in proteins
    • Parker J. M. R., Hodges R. S. Prediction of surface and interior regions in proteins - Part I: Linear tripeptide sequences identify structural boundaries in proteins. Pept. Res. 4:1991a;347-354.
    • (1991) Pept. Res. , vol.4 , pp. 347-354
    • Parker, J.M.R.1    Hodges, R.S.2
  • 63
    • 0026253189 scopus 로고
    • Prediction of surface and interior regions in proteins - PartII: Predicting secondary structure in regions bound by surface exposed regions
    • Parker J. M. R., Hodges R. S. Prediction of surface and interior regions in proteins - PartII: Predicting secondary structure in regions bound by surface exposed regions. Pept. Res. 4:1991b;355-363.
    • (1991) Pept. Res. , vol.4 , pp. 355-363
    • Parker, J.M.R.1    Hodges, R.S.2
  • 65
    • 0028844306 scopus 로고
    • A left-handed parallel β helix in the structure of UDP- N -acetylglucosamine acyltransferase
    • Raetz C. R. H., Roderick S. L. A left-handed parallel β helix in the structure of UDP- N -acetylglucosamine acyltransferase. Science. 270:1995;997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 66
    • 0031932327 scopus 로고    scopus 로고
    • Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation
    • Römling U., Bian Z., Hammar M., Sierralta W. D., Normark S. Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation. J. Bacteriol. 180:1998;722-731.
    • (1998) J. Bacteriol. , vol.180 , pp. 722-731
    • Römling, U.1    Bian, Z.2    Hammar, M.3    Sierralta, W.D.4    Normark, S.5
  • 68
    • 0028297019 scopus 로고
    • Crystal structure of vitelline membrane outer layer protein I (VMO-I): A folding motif with homologous Greek key structures related by an internal three-fold symmetry
    • Shimizu T., Vassylyev D. G., Kido S., Doi Y., Morikawa K. Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry. EMBO J. 13:1994;1003-1010.
    • (1994) EMBO J. , vol.13 , pp. 1003-1010
    • Shimizu, T.1    Vassylyev, D.G.2    Kido, S.3    Doi, Y.4    Morikawa, K.5
  • 69
    • 0031033180 scopus 로고    scopus 로고
    • Towards a structural biology of bacterial conjugation
    • Silverman P. M. Towards a structural biology of bacterial conjugation. Mol. Microbiol. 23:1997;423-429.
    • (1997) Mol. Microbiol. , vol.23 , pp. 423-429
    • Silverman, P.M.1
  • 70
    • 0025707198 scopus 로고
    • The penultimate tyrosine residue of the K99 fibrillar subunit is essential for stability of the protein and its interaction with the periplasmic carrier protein
    • Simons B. L., Rathman P., Malij C. R., Oudega B., de Graaf F. K. The penultimate tyrosine residue of the K99 fibrillar subunit is essential for stability of the protein and its interaction with the periplasmic carrier protein. FEMS Microbiol. Letters. 67:1990;107-112.
    • (1990) FEMS Microbiol. Letters , vol.67 , pp. 107-112
    • Simons, B.L.1    Rathman, P.2    Malij, C.R.3    Oudega, B.4    De Graaf, F.K.5
  • 71
    • 0028305441 scopus 로고
    • Morphological appearances of K88ab fimbriae and optical diffraction analysis of K88 paracrystalline structures
    • Simons B. L., Mol O., van Breemen J. F. L., Oudega B. Morphological appearances of K88ab fimbriae and optical diffraction analysis of K88 paracrystalline structures. FEMS Microbiol. Letters. 118:1994;83-88.
    • (1994) FEMS Microbiol. Letters , vol.118 , pp. 83-88
    • Simons, B.L.1    Mol, O.2    Van Breemen, J.F.L.3    Oudega, B.4
  • 72
    • 0027942891 scopus 로고
    • Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue-type plasminogen activator (t-PA)
    • Sjöbring U., Pohl G., Olsén A. Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue-type plasminogen activator (t-PA). Mol. Microbiol. 14:1994;443-452.
    • (1994) Mol. Microbiol. , vol.14 , pp. 443-452
    • Sjöbring, U.1    Pohl, G.2    Olsén, A.3
  • 74
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher S., Seckler R., Miller S., Steipe B., Huber R., Reinemer P. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science. 265:1994;383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 75
    • 0025857630 scopus 로고
    • Glycine loops in proteins: Their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins
    • Steinert P. M., Mack J. W., Korge B. P., Gan S.-Q., Haynes S. R., Steven A. C. Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins. Int. J. Biol. 13:1991;130-139.
    • (1991) Int. J. Biol. , vol.13 , pp. 130-139
    • Steinert, P.M.1    MacK, J.W.2    Korge, B.P.3    Gan, S.-Q.4    Haynes, S.R.5    Steven, A.C.6
  • 77
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of the type IV pili
    • Strom M. S., Lory S. Structure-function and biogenesis of the type IV pili. Annu. Rev. Microbiol. 47:1993;565-596.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 79
    • 0030831577 scopus 로고    scopus 로고
    • Expression of thin aggregative fimbriae promotes interaction of Salmonella typhimurium SR-11 with mouse small intestinal epithelial cells
    • Sukupolvi S., Lorenz R. G., Gordon J. I., Bian Z., Pfeifer J. D., Normark S. J., Rhen M. Expression of thin aggregative fimbriae promotes interaction of Salmonella typhimurium SR-11 with mouse small intestinal epithelial cells. Infect. Immun. 65:1997b;5320-5325.
    • (1997) Infect. Immun. , vol.65 , pp. 5320-5325
    • Sukupolvi, S.1    Lorenz, R.G.2    Gordon, J.I.3    Bian, Z.4    Pfeifer, J.D.5    Normark, S.J.6    Rhen, M.7
  • 81
    • 0028329671 scopus 로고
    • The use of latex particle agglutination to specifically detect Salmonella enteritidis
    • Thorns C. J., McLaren I. M., Sojka M. G. The use of latex particle agglutination to specifically detect Salmonella enteritidis. Int. J. Food. Microbiol. 21:1994;47-53.
    • (1994) Int. J. Food. Microbiol. , vol.21 , pp. 47-53
    • Thorns, C.J.1    McLaren, I.M.2    Sojka, M.G.3
  • 82
    • 0031977366 scopus 로고    scopus 로고
    • Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: Involvement of a new ompR allele that increases curli expression
    • Vidal O., Longin R., Prigent-Combaret C., Dorel C., Hooreman M., Lejeune P. Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: involvement of a new ompR allele that increases curli expression. J. Bacteriol. 180:1998;2442-2449.
    • (1998) J. Bacteriol. , vol.180 , pp. 2442-2449
    • Vidal, O.1    Longin, R.2    Prigent-Combaret, C.3    Dorel, C.4    Hooreman, M.5    Lejeune, P.6
  • 83
    • 0344867896 scopus 로고    scopus 로고
    • High efficiency gene replacement in Salmonella enteritidis: Chimeric fimbrins containing a T cell epitope fromLeishmania major
    • White A. P., Collinson S. K., Burian J., Clouthier S. C., Banser P. A., Kay W. W. High efficiency gene replacement in Salmonella enteritidis: chimeric fimbrins containing a T cell epitope fromLeishmania major. Vaccine. 17:1999;2150-2161.
    • (1999) Vaccine , vol.17 , pp. 2150-2161
    • White, A.P.1    Collinson, S.K.2    Burian, J.3    Clouthier, S.C.4    Banser, P.A.5    Kay, W.W.6
  • 85
    • 0028353294 scopus 로고
    • SEQSEE: A comprehensive program suite for protein sequence analysis
    • Wishart D. S., Boyko R. F., Willard L., Richards F. M., Sykes B. D. SEQSEE: a comprehensive program suite for protein sequence analysis. CABIOS. 10:1994;121-132.
    • (1994) CABIOS , vol.10 , pp. 121-132
    • Wishart, D.S.1    Boyko, R.F.2    Willard, L.3    Richards, F.M.4    Sykes, B.D.5
  • 87
    • 0029257535 scopus 로고
    • The parallel β helix and other coiled folds
    • Yoder M. D., Jurnak F. The parallel β helix and other coiled folds. FASEB J. 9:1995;335-342.
    • (1995) FASEB J. , vol.9 , pp. 335-342
    • Yoder, M.D.1    Jurnak, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.