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Volumn 535, Issue , 2002, Pages 33-52

Structural basis for bacterial adhesion in the urinary tract

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL INFECTION; BACTERIUM ADHERENCE; BIOGENESIS; CELL ORGANELLE; CONFERENCE PAPER; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; URINARY TRACT INFECTION;

EID: 1642521976     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (14)

References (125)
  • 1
  • 2
    • 0036039736 scopus 로고    scopus 로고
    • Type 1 fimbriae and extracellular polysaccharides are preeminent uropathogenic Escherichia coli virulence determinants in the murine urinary tract
    • Bahrani-Mougeot, F.K., Buckles, E.L., Lockatell, C.V., Hebel, J.R., Johnson, D.E., Tang, C.M., and Donnenberg, M.S., 2002, Type 1 fimbriae and extracellular polysaccharides are preeminent uropathogenic Escherichia coli virulence determinants in the murine urinary tract, Mol Microbiol. 45:1079-1093.
    • (2002) Mol Microbiol , vol.45 , pp. 1079-1093
    • Bahrani-Mougeot, F.K.1    Buckles, E.L.2    Lockatell, C.V.3    Hebel, J.R.4    Johnson, D.E.5    Tang, C.M.6    Donnenberg, M.S.7
  • 5
    • 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., 1965, The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria, Trans N Y Acad Sci. 27:1003-1054.
    • (1965) Trans N Y Acad Sci , vol.27 , pp. 1003-1054
    • Brinton Jr., C.C.1
  • 7
    • 0028794484 scopus 로고
    • Structural polymorphism of bacterial adhesion pili
    • Bullitt, E. and Makowski, L., 1995, Structural polymorphism of bacterial adhesion pili, Nature. 373:164-167.
    • (1995) Nature , vol.373 , pp. 164-167
    • Bullitt, E.1    Makowski, L.2
  • 8
    • 0031032562 scopus 로고    scopus 로고
    • Mutational analysis of receptor binding mediated by the Dr family of Escherichia coli adhesins
    • Carnoy, C. and Moseley, S.L., 1997, Mutational analysis of receptor binding mediated by the Dr family of Escherichia coli adhesins, Mol Microbiol. 23:365-379.
    • (1997) Mol Microbiol , vol.23 , pp. 365-379
    • Carnoy, C.1    Moseley, S.L.2
  • 13
    • 0027483426 scopus 로고
    • Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson, K.W., Jacob-Dubuisson, F., Striker, R.T., and Hultgren, S.J., 1993, Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes, Proc Natl Acad Sci U S A. 90:3670-3674.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3670-3674
    • Dodson, K.W.1    Jacob-Dubuisson, F.2    Striker, R.T.3    Hultgren, S.J.4
  • 14
    • 0035875099 scopus 로고    scopus 로고
    • Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor
    • Dodson, K.W., Pinkner, J.S., Rose, T., Magnusson, G., Hultgren, S.J., and Waksman, G., 2001, Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor, Cell. 105:733-743.
    • (2001) Cell , vol.105 , pp. 733-743
    • Dodson, K.W.1    Pinkner, J.S.2    Rose, T.3    Magnusson, G.4    Hultgren, S.J.5    Waksman, G.6
  • 15
    • 0023095282 scopus 로고
    • Aromatic alpha-glycosides of mannose are powerful inhibitors of the adherence of type 1 fimbriated Escherichia coli to yeast and intestinal epithelial cells
    • Firon, N., Ashkenazi, S., Mirelman, D., Ofek, I., and Sharon, N., 1987, Aromatic alpha-glycosides of mannose are powerful inhibitors of the adherence of type 1 fimbriated Escherichia coli to yeast and intestinal epithelial cells, Infect Immun. 55:472-476.
    • (1987) Infect Immun , vol.55 , pp. 472-476
    • Firon, N.1    Ashkenazi, S.2    Mirelman, D.3    Ofek, I.4    Sharon, N.5
  • 16
    • 0020336272 scopus 로고
    • Interaction of mannose-containing oligosaccharides with the fimbrial lectins of Escherichia coli
    • Firon, N., Ofek, I., and Sharon, N., 1982, Interaction of mannose-containing oligosaccharides with the fimbrial lectins of Escherichia coli, Biochem Biophys Res Commun. 105:1426-1432.
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 1426-1432
    • Firon, N.1    Ofek, I.2    Sharon, N.3
  • 17
    • 0021106296 scopus 로고
    • Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium
    • Firon, N., Ofek, I., and Sharon, N., 1983, Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium. Carbohydr Res. 120:235-249.
    • (1983) Carbohydr Res , vol.120 , pp. 235-249
    • Firon, N.1    Ofek, I.2    Sharon, N.3
  • 18
    • 0021345727 scopus 로고
    • Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria
    • Firon, N., Ofek, I., and Sharon, N., 1984, Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria, Infect Immun. 43:1088-1090.
    • (1984) Infect Immun , vol.43 , pp. 1088-1090
    • Firon, N.1    Ofek, I.2    Sharon, N.3
  • 19
    • 0037043290 scopus 로고    scopus 로고
    • Epidemiology of urinary tract infections: Incidence, morbidity, and economic costs
    • Foxman, B., 2002, Epidemiology of urinary tract infections: incidence, morbidity, and economic costs. Am J Med. 113 Suppl 1A:5S-13S.
    • (2002) Am J Med , vol.113 , Issue.SUPPL. 1A
    • Foxman, B.1
  • 20
    • 0029021466 scopus 로고
    • Bacterial virulence characteristics of Escherichia coli isolates from first-time urinary tract infection
    • Foxman, B., Zhang, L., Palin, K., Tallman, P., and Marrs, C.F., 1995, Bacterial virulence characteristics of Escherichia coli isolates from first-time urinary tract infection. J Infect Dis. 171:1514-1521.
    • (1995) J Infect Dis , vol.171 , pp. 1514-1521
    • Foxman, B.1    Zhang, L.2    Palin, K.3    Tallman, P.4    Marrs, C.F.5
  • 21
    • 0027049870 scopus 로고
    • Helical structure of P pili from Escherichia coli. Evidence from X-ray fiber diffraction and scanning transmission electron microscopy
    • Gong, M. and Makowski, L., 1992, Helical structure of P pili from Escherichia coli. Evidence from X-ray fiber diffraction and scanning transmission electron microscopy, J Mol Biol. 228:735-742.
    • (1992) J Mol Biol , vol.228 , pp. 735-742
    • Gong, M.1    Makowski, L.2
  • 22
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell, D.S. and Olson, A.J., 1990, Automated docking of substrates to proteins by simulated annealing, Prot Struct Func Genet. 8:1040-1045.
    • (1990) Prot Struct Func Genet , vol.8 , pp. 1040-1045
    • Goodsell, D.S.1    Olson, A.J.2
  • 23
    • 0034991646 scopus 로고    scopus 로고
    • Antimicrobial resistance among uropathogens that cause community-acquired urinary tract infections in women: A nationwide analysis
    • Gupta, K., Sahm, D.F., Mayfield, D., and Stamm, W.E., 2001, Antimicrobial resistance among uropathogens that cause community-acquired urinary tract infections in women: A nationwide analysis, Clin Infect Dis. 33:89-94.
    • (2001) Clin Infect Dis , vol.33 , pp. 89-94
    • Gupta, K.1    Sahm, D.F.2    Mayfield, D.3    Stamm, W.E.4
  • 25
    • 0027156470 scopus 로고
    • Specificity of S fimbriae on recombinant Escherichia coli: Preferential binding to gangliosides expressing NeuGc alpha (2-3)Gal and NeuAc alpha (2-8)NeuAc
    • Hanisch, F.G., Hacker, J., and Schroten, H., 1993, Specificity of S fimbriae on recombinant Escherichia coli: preferential binding to gangliosides expressing NeuGc alpha (2-3)Gal and NeuAc alpha (2-8)NeuAc, Infect Immun. 61:2108-2115.
    • (1993) Infect Immun , vol.61 , pp. 2108-2115
    • Hanisch, F.G.1    Hacker, J.2    Schroten, H.3
  • 26
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren, A. and Branden, C.I., 1989, Crystal structure of chaperone protein PapD reveals an immunoglobulin fold, Nature. 342:248-251.
    • (1989) Nature , vol.342 , pp. 248-251
    • Holmgren, A.1    Branden, C.I.2
  • 29
    • 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., and Hultgren, S.J., 1996, Molecular basis of two subfamilies of immunoglobulin-like chaperones, EMBO J. 15:3792-3805.
    • (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
  • 30
    • 0026060005 scopus 로고
    • Virulence factors in Escherichia coli urinary tract infection
    • Johnson, J.R., 1991, Virulence factors in Escherichia coli urinary tract infection, Clin Microbiol Rev. 4:80-128.
    • (1991) Clin Microbiol Rev , vol.4 , pp. 80-128
    • Johnson, J.R.1
  • 31
    • 0037193805 scopus 로고    scopus 로고
    • A disseminated multidrug-resistant clonal group of uropathogenic Escherichia coli in pyelonephritis
    • Johnson, J.R., Manges, A.R., O'Bryan, T.T., and Riley, L.W., 2002, A disseminated multidrug-resistant clonal group of uropathogenic Escherichia coli in pyelonephritis, Lancet. 359:2249-2251.
    • (2002) Lancet , vol.359 , pp. 2249-2251
    • Johnson, J.R.1    Manges, A.R.2    O'Bryan, T.T.3    Riley, L.W.4
  • 32
    • 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., and Hultgren, S.J., 1997, The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems, EMBO J. 16:6394-6406.
    • (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
  • 36
    • 0024397384 scopus 로고
    • Probing the combining site of the PapG adhesin of uropathogenic Escherichia coli bacteria by synthetic analogs of galabiose
    • Kihlberg, J., Hultgren, S.J., Normark, S., and Magnusson, G., 1989, Probing the combining site of the PapG adhesin of uropathogenic Escherichia coli bacteria by synthetic analogs of galabiose, J Am Chem Soc. 111:6364-6368.
    • (1989) J Am Chem Soc , vol.111 , pp. 6364-6368
    • Kihlberg, J.1    Hultgren, S.J.2    Normark, S.3    Magnusson, G.4
  • 37
    • 0023375497 scopus 로고
    • Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae
    • Klemm, P. and Christiansen, G., 1987, Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae, Mol Gen Genet. 208:439-445.
    • (1987) Mol Gen Genet , vol.208 , pp. 439-445
    • Klemm, P.1    Christiansen, G.2
  • 38
    • 0025069863 scopus 로고
    • The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae
    • Klemm, P. and Christiansen, G., 1990, The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae, Mol Gen Genet. 220:334-338.
    • (1990) Mol Gen Genet , vol.220 , pp. 334-338
    • Klemm, P.1    Christiansen, G.2
  • 39
    • 0028231478 scopus 로고
    • Reciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities
    • Klemm, P., Christiansen, G., Kreft, B., Marre, R., and Bergmans, H., 1994, Reciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities, J Bacteriol. 176:2227-2234.
    • (1994) J Bacteriol , vol.176 , pp. 2227-2234
    • Klemm, P.1    Christiansen, G.2    Kreft, B.3    Marre, R.4    Bergmans, H.5
  • 40
    • 0020064078 scopus 로고
    • F7 and type 1-like fimbriae from three Escherichia coli strains isolated from urinary tract infections: Protein chemical and immunological aspects
    • Klemm, P., Orskov, I., and Orskov, F., 1982, F7 and type 1-like fimbriae from three Escherichia coli strains isolated from urinary tract infections: protein chemical and immunological aspects, Infect Immun. 36:462-468.
    • (1982) Infect Immun , vol.36 , pp. 462-468
    • Klemm, P.1    Orskov, I.2    Orskov, F.3
  • 41
    • 0033636403 scopus 로고    scopus 로고
    • Bacterial adhesins: Structural studies reveal chaperone function and pilus biogenesis
    • Knight, S.D., Berglund, J., and Choudhury, D., 2000, Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis, Curr Opin Chem Biol. 4:653-660.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 653-660
    • Knight, S.D.1    Berglund, J.2    Choudhury, D.3
  • 46
    • 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
  • 47
    • 0025885694 scopus 로고
    • Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits
    • Kuehn, M.J., Normark, S., and Hultgren, S.J., 1991, Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits, Proc Natl Acad Sci U S A. 88:10586-10590.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10586-10590
    • Kuehn, M.J.1    Normark, S.2    Hultgren, S.J.3
  • 49
    • 0027498273 scopus 로고
    • Basement membrane carbohydrate as a target for bacterial adhesion: Binding of type I fimbriae of Salmonella enterica and Escherichia coli to laminin
    • Kukkonen, M., Raunio, T., Virkola, R., Lähteenmäki, K., Mäkelä, P.H., Klemm, P., Clegg, S., and Korhonen, T.K., 1993, Basement membrane carbohydrate as a target for bacterial adhesion: binding of type I fimbriae of Salmonella enterica and Escherichia coli to laminin, Mol Microbiol. 7:229-237.
    • (1993) Mol Microbiol , vol.7 , pp. 229-237
    • Kukkonen, M.1    Raunio, T.2    Virkola, R.3    Lähteenmäki, K.4    Mäkelä, P.H.5    Klemm, P.6    Clegg, S.7    Korhonen, T.K.8
  • 52
    • 0019852815 scopus 로고
    • Glycolipid receptors for uropathogenic Escherichia coli on human erythrocytes and uroepithelial cells
    • Leffler, H. and Svanborg-Eden, C., 1981, Glycolipid receptors for uropathogenic Escherichia coli on human erythrocytes and uroepithelial cells, Infect Immun. 34:920-929.
    • (1981) Infect Immun , vol.34 , pp. 920-929
    • Leffler, H.1    Svanborg-Eden, C.2
  • 53
    • 0019221850 scopus 로고
    • Chemical identification of a glycosphingolipid receptor for Escherichia coli attaching to human urinary tract epithelial cells and agglutinating human erythrocytes
    • Leffler, H. and Svanborg-Edén, C., 1980, Chemical identification of a glycosphingolipid receptor for Escherichia coli attaching to human urinary tract epithelial cells and agglutinating human erythrocytes, FEMS Microbiol Lett. 8:127-134.
    • (1980) FEMS Microbiol Lett , vol.8 , pp. 127-134
    • Leffler, H.1    Svanborg-Edén, C.2
  • 54
    • 0023183146 scopus 로고
    • Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus
    • Lindberg, F., Lund, B., Johansson, L., and Normark, S., 1987, Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus, Nature. 328:84-87.
    • (1987) Nature , vol.328 , pp. 84-87
    • Lindberg, F.1    Lund, B.2    Johansson, L.3    Normark, S.4
  • 55
    • 0000856193 scopus 로고    scopus 로고
    • Artificial multivalent sugar ligands to understand and manipulate carbohydrate-protein interaction
    • Lindhorst, T.K., 2002, Artificial multivalent sugar ligands to understand and manipulate carbohydrate-protein interaction, Topics Curr Chem. 218:201-235.
    • (2002) Topics Curr Chem , vol.218 , pp. 201-235
    • Lindhorst, T.K.1
  • 56
    • 0031824605 scopus 로고    scopus 로고
    • Inhibition of the type 1 fimbriae-mediated adhesion of Escherichia coli to erythrocytes by multiantennary alpha-mannosyl clusters: The effect of multivalency
    • Lindhorst, T.K., Kieburg, C., and Krallmann-Wenzel, U., 1998, Inhibition of the type 1 fimbriae-mediated adhesion of Escherichia coli to erythrocytes by multiantennary alpha-mannosyl clusters: the effect of multivalency, Glycoconj J. 15:605-613.
    • (1998) Glycoconj J , vol.15 , pp. 605-613
    • Lindhorst, T.K.1    Kieburg, C.2    Krallmann-Wenzel, U.3
  • 57
    • 0023389683 scopus 로고
    • The PapG protein is the alpha-D-galactopyranosyl-(1-4)-beta-D- galactopyranose-binding adhesin of uropathogenic Escherichia coli
    • Lund, B., Lindberg, F., Marklund, B.I., and Normark, S., 1987, The PapG protein is the alpha-D-galactopyranosyl-(1-4)-beta-D-galactopyranose-binding adhesin of uropathogenic Escherichia coli, Proc Natl Acad Sci USA. 84:5898-5902.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5898-5902
    • Lund, B.1    Lindberg, F.2    Marklund, B.I.3    Normark, S.4
  • 58
    • 0035181360 scopus 로고    scopus 로고
    • An extended hydrophobic interactive surface of Yersinia pestis Caf1M chaperone is essential for subunit binding and F1 capsule assembly
    • MacIntyre, S., Zyrianova, I.M., Chernovskaya, T.V., Leonard, M., Rudenko, E.G., Zav'Yalov, V.P., and Chapman, D.A., 2001, An extended hydrophobic interactive surface of Yersinia pestis Caf1M chaperone is essential for subunit binding and F1 capsule assembly, Mol Microbiol. 39:12-25.
    • (2001) Mol Microbiol , vol.39 , pp. 12-25
    • MacIntyre, S.1    Zyrianova, I.M.2    Chernovskaya, T.V.3    Leonard, M.4    Rudenko, E.G.5    Zav'Yalov, V.P.6    Chapman, D.A.7
  • 59
    • 0034718167 scopus 로고    scopus 로고
    • Terminal glycosylation of bovine uroplakin III, one of the major integral-membrane glycoproteins of mammalian bladder
    • Malagolini, N., Cavallone, D., Wu, X.-R., and Serafini-Cessi, F., 2000, Terminal glycosylation of bovine uroplakin III, one of the major integral-membrane glycoproteins of mammalian bladder, Biochim Biophys Acta. 1475:231-237.
    • (2000) Biochim Biophys Acta , vol.1475 , pp. 231-237
    • Malagolini, N.1    Cavallone, D.2    Wu, X.-R.3    Serafini-Cessi, F.4
  • 60
    • 0033529313 scopus 로고    scopus 로고
    • The mast cell tumor necrosis factor a response to FimH-expressing Escherichia coli is mediated by the glycosylphosphatidylinosityl-anchored molecule CD48
    • Malaviya, R., Gao, Z., Thankavel, K., van der Merwe, P., and Abraham, S.N., 1999, The mast cell tumor necrosis factor a response to FimH-expressing Escherichia coli is mediated by the glycosylphosphatidylinosityl-anchored molecule CD48, Proc Natl Acad Sci USA. 96:8110-8115.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8110-8115
    • Malaviya, R.1    Gao, Z.2    Thankavel, K.3    Van Der Merwe, P.4    Abraham, S.N.5
  • 61
    • 0022978762 scopus 로고
    • Contribution of cloned virulence factors from uropathogenic Escherichia coli strains to nephropathogenicity in an experimental rat pyelonephritis model
    • Marre, R., Hacker, J., Henkel, W., and Goebel, W., 1986, Contribution of cloned virulence factors from uropathogenic Escherichia coli strains to nephropathogenicity in an experimental rat pyelonephritis model, Infect Immun. 54:761-767.
    • (1986) Infect Immun , vol.54 , pp. 761-767
    • Marre, R.1    Hacker, J.2    Henkel, W.3    Goebel, W.4
  • 62
  • 63
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., and Olson, A.J., 1998, Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, J Comput Chem. 19:1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 64
    • 0027583602 scopus 로고
    • Regulation and binding properties of S fimbriae cloned from E. coli strains causing urinary tract infection and meningitis
    • Morschhauser, J., Vetter, V., Korhonen, T., Uhlin, B.E., and Hacker, J., 1993, Regulation and binding properties of S fimbriae cloned from E. coli strains causing urinary tract infection and meningitis, Zentralbl Bakteriol. 278:165-176.
    • (1993) Zentralbl Bakteriol , vol.278 , pp. 165-176
    • Morschhauser, J.1    Vetter, V.2    Korhonen, T.3    Uhlin, B.E.4    Hacker, J.5
  • 65
    • 0036258843 scopus 로고    scopus 로고
    • Adhesion and entry of uropathogenic Escherichia coli
    • Mulvey, M.A., 2002, Adhesion and entry of uropathogenic Escherichia coli, Cell Microbiol. 4:257-271.
    • (2002) Cell Microbiol , vol.4 , pp. 257-271
    • Mulvey, M.A.1
  • 66
  • 67
    • 0034978222 scopus 로고    scopus 로고
    • Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection
    • Mulvey, M.A., Schilling, J.D., and Hultgren, S.J., 2001, Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection, Infect Immun. 69:4572-4579.
    • (2001) Infect Immun , vol.69 , pp. 4572-4579
    • Mulvey, M.A.1    Schilling, J.D.2    Hultgren, S.J.3
  • 68
    • 12244292949 scopus 로고    scopus 로고
    • Inhibition of adhesion of Type 1 fimbriated Escherichia coli to highly mannosylated ligands
    • Nagahori, N., Lee, R.T., Nishimura, S., Page, D., Roy, R., and Lee, Y.C., 2002, Inhibition of adhesion of Type 1 fimbriated Escherichia coli to highly mannosylated ligands, Chembiochem. 3:836-844.
    • (2002) Chembiochem , vol.3 , pp. 836-844
    • Nagahori, N.1    Lee, R.T.2    Nishimura, S.3    Page, D.4    Roy, R.5    Lee, Y.C.6
  • 69
    • 0022638502 scopus 로고
    • Oligomannoside-type glycopeptides inhibiting adhesion of Escherichia coli strains mediated by type 1 pili: Preparation of potent inhibitors from plant glycoproteins
    • Neeser, J.-R., Koellreutter, B., and Wuersch, P., 1986, Oligomannoside-type glycopeptides inhibiting adhesion of Escherichia coli strains mediated by type 1 pili: Preparation of potent inhibitors from plant glycoproteins, Infect Immun. 52:428-436.
    • (1986) Infect Immun , vol.52 , pp. 428-436
    • Neeser, J.-R.1    Koellreutter, B.2    Wuersch, P.3
  • 70
    • 0036322359 scopus 로고    scopus 로고
    • Resistant pathogens in urinary tract infections
    • Nicolle, L.E., 2002, Resistant pathogens in urinary tract infections, J Am Geriatr Soc. 50:S230-235.
    • (2002) J Am Geriatr Soc , vol.50
    • Nicolle, L.E.1
  • 71
    • 0035282875 scopus 로고    scopus 로고
    • Family of Escherichia coli Dr adhesins: Decay-accelerating factor receptor recognition and invasiveness
    • Nowicki, B., Selvarangan, R., and Nowicki, S., 2001, Family of Escherichia coli Dr adhesins: decay-accelerating factor receptor recognition and invasiveness, J Infect Dis. 183 Suppl 1:S24-27.
    • (2001) J Infect Dis , vol.183 , Issue.1 SUPPL.
    • Nowicki, B.1    Selvarangan, R.2    Nowicki, S.3
  • 72
    • 0024584959 scopus 로고
    • Molecular analysis and epidemiology of the Dr hemagglutinin of uropathogenic Escherichia coli
    • Nowicki, B., Svanborg-Eden, C., Hull, R., and Hull, S., 1989, Molecular analysis and epidemiology of the Dr hemagglutinin of uropathogenic Escherichia coli, Infect Immun. 57:446-451.
    • (1989) Infect Immun , vol.57 , pp. 446-451
    • Nowicki, B.1    Svanborg-Eden, C.2    Hull, R.3    Hull, S.4
  • 73
    • 0036905866 scopus 로고    scopus 로고
    • Discovery of potent inhibitors of PapG adhesins from uropathogenic Escherichia coli through synthesis and evaluation of galabiose derivatives
    • Ohlsson, J., Jass, J., Uhlin, B.E., Kihlberg, J., and Nilsson, U.J., 2002, Discovery of potent inhibitors of PapG adhesins from uropathogenic Escherichia coli through synthesis and evaluation of galabiose derivatives, Chembiochem. 3:772-779.
    • (2002) Chembiochem , vol.3 , pp. 772-779
    • Ohlsson, J.1    Jass, J.2    Uhlin, B.E.3    Kihlberg, J.4    Nilsson, U.J.5
  • 74
    • 0035971077 scopus 로고    scopus 로고
    • Tamm-Horsfall protein binds to type 1 fimbriated Escherichia coli and prevents E. coli from binding to uroplakin Ia and Ib receptors
    • Pak, J., Yongbing, P., Zhang, Z.-T., Hasty, D.L., and Wu, X.-R., 2001, Tamm-Horsfall protein binds to type 1 fimbriated Escherichia coli and prevents E. coli from binding to uroplakin Ia and Ib receptors, J Biol Chem. 276:9924-9930.
    • (2001) J Biol Chem , vol.276 , pp. 9924-9930
    • Pak, J.1    Yongbing, P.2    Zhang, Z.-T.3    Hasty, D.L.4    Wu, X.-R.5
  • 75
    • 0022504387 scopus 로고
    • Identification of the O-linked sialyloligosaccharides of glycophorin A as the erythrocyte receptors for S-fimbriated Escherichia coli
    • Parkkinen, J., Rogers, G.N., Korhonen, T., Dahr, W., and Finne, J., 1986, Identification of the O-linked sialyloligosaccharides of glycophorin A as the erythrocyte receptors for S-fimbriated Escherichia coli, Infect Immun. 54:37-42.
    • (1986) Infect Immun , vol.54 , pp. 37-42
    • Parkkinen, J.1    Rogers, G.N.2    Korhonen, T.3    Dahr, W.4    Finne, J.5
  • 79
    • 0000521344 scopus 로고    scopus 로고
    • Amino acid residue Ala-62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis-associated Escherichia coli to collagens
    • Pouttu, R., Puustinen, T., Virkola, R., Hacker, R., Klemm, P., and Korhonen, T.K., 1999, Amino acid residue Ala-62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis-associated Escherichia coli to collagens, Mol Microbiol. 31:1747-1757.
    • (1999) Mol Microbiol , vol.31 , pp. 1747-1757
    • Pouttu, R.1    Puustinen, T.2    Virkola, R.3    Hacker, R.4    Klemm, P.5    Korhonen, T.K.6
  • 80
    • 0027287638 scopus 로고
    • Adhesion of S-fimbriated Escherichia coli to brain glycolipids mediated by sfaA gene-encoded protein of S-fimbriae
    • Prasadarao, N.V., Wass, C.A., Hacker, J., Jann, K., and Kim, K.S., 1993, Adhesion of S-fimbriated Escherichia coli to brain glycolipids mediated by sfaA gene-encoded protein of S-fimbriae, J Biol Chem. 268:10356-10363.
    • (1993) J Biol Chem , vol.268 , pp. 10356-10363
    • Prasadarao, N.V.1    Wass, C.A.2    Hacker, J.3    Jann, K.4    Kim, K.S.5
  • 81
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: Roles of flagella, motility, chemotaxis and type I pili
    • Pratt, L.A. and Kolter, R., 1998, Genetic analysis of Escherichia coli biofilm formation: roles of flagella, motility, chemotaxis and type I pili, Mol Microbiol. 30:285-293.
    • (1998) Mol Microbiol , vol.30 , pp. 285-293
    • Pratt, L.A.1    Kolter, R.2
  • 82
    • 0025020690 scopus 로고
    • F1C fimbriae of a uropathogenic Escherichia coli strain: Genetic and functional organization of the foc gene cluster and identification of minor subunits
    • Riegman, N., Kusters, R., Van Veggel, H., Bergmans, H., Van Bergen en Henegouwen, P., Hacker, J., and Van Die, I., 1990, F1C fimbriae of a uropathogenic Escherichia coli strain: genetic and functional organization of the foc gene cluster and identification of minor subunits, J Bacteriol. 172:1114-1120.
    • (1990) J Bacteriol , vol.172 , pp. 1114-1120
    • Riegman, N.1    Kusters, R.2    Van Veggel, H.3    Bergmans, H.4    Van Bergen En Henegouwen, P.5    Hacker, J.6    Van Die, I.7
  • 84
    • 0037043277 scopus 로고    scopus 로고
    • The etiology of urinary tract infection: Traditional and emerging pathogens
    • Ronald, A., 2002, The etiology of urinary tract infection: traditional and emerging pathogens, Am J Med. 113:14S-19S.
    • (2002) Am J Med , vol.113
    • Ronald, A.1
  • 85
    • 0024226625 scopus 로고
    • New type of adhesive specificity revealed by oligosaccharide probes in Escherichia coli from patients with urinary tract infections
    • Rosenstein, I.J., Mizuochi, T., Hounsell, E.F., Stoll, M.S., Childs, R.A., and Feizi, T., 1988, New type of adhesive specificity revealed by oligosaccharide probes in Escherichia coli from patients with urinary tract infections, Lancet. 2:1327-1330.
    • (1988) Lancet , vol.2 , pp. 1327-1330
    • Rosenstein, I.J.1    Mizuochi, T.2    Hounsell, E.F.3    Stoll, M.S.4    Childs, R.A.5    Feizi, T.6
  • 89
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer, F.G., Pinkner, J.S., Waksman, G., and Hultgren, S.J., 2002, Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation, Cell. 111:543-551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 90
    • 0034255260 scopus 로고    scopus 로고
    • Snapshots of usher-mediated protein secretion and ordered pilus assembly
    • Saulino, E.T., Bullitt, E., and Hultgren, S.J., 2000, Snapshots of usher-mediated protein secretion and ordered pilus assembly, Proc Natl Acad Sci USA. 97:9240-9245.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9240-9245
    • Saulino, E.T.1    Bullitt, E.2    Hultgren, S.J.3
  • 91
    • 0032522714 scopus 로고    scopus 로고
    • Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
    • Saulino, E.T., Thanassi, D.G., Pinkner, J.S., and Hultgren, S.J., 1998, Ramifications of kinetic partitioning on usher-mediated pilus biogenesis, EMBO J. 17:2177-2185.
    • (1998) EMBO J , vol.17 , pp. 2177-2185
    • Saulino, E.T.1    Thanassi, D.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 92
    • 0035111862 scopus 로고    scopus 로고
    • Biofilm formation in a hydrodynamic environment by novel FimH variants and ramifications for virulence
    • Schembri, M.A. and Klemm, P., 2001, Biofilm formation in a hydrodynamic environment by novel FimH variants and ramifications for virulence. Infect Immun. 69:1322-1328.
    • (2001) Infect Immun , vol.69 , pp. 1322-1328
    • Schembri, M.A.1    Klemm, P.2
  • 93
    • 0034016418 scopus 로고    scopus 로고
    • Functional flexibility of the FimH adhesin: Insights from a random mutant library
    • Schembri, M.A., Sokurenko, E.V., and Klemm, P., 2000, Functional flexibility of the FimH adhesin: insights from a random mutant library, Infect Immun. 68:2638-2646.
    • (2000) Infect Immun , vol.68 , pp. 2638-2646
    • Schembri, M.A.1    Sokurenko, E.V.2    Klemm, P.3
  • 94
    • 0024788794 scopus 로고
    • Analysis of genes coding for the sialic acid-binding adhesin and two other minor fimbrial subunits of the S-fimbrial adhesin determinant of Escherichia coli
    • Schmoll, T., Hoschutzky, H., Morschhauser, J., Lottspeich, F., Jann, K., and Hacker, J., 1989, Analysis of genes coding for the sialic acid-binding adhesin and two other minor fimbrial subunits of the S-fimbrial adhesin determinant of Escherichia coli, Mol Microbiol. 3:1735-1744.
    • (1989) Mol Microbiol , vol.3 , pp. 1735-1744
    • Schmoll, T.1    Hoschutzky, H.2    Morschhauser, J.3    Lottspeich, F.4    Jann, K.5    Hacker, J.6
  • 95
    • 0025688642 scopus 로고
    • Complete genetic organization and functional aspects of the Escherichia coli S fimbrial adhesion determinant: Nucleotide sequence of the genes sfa B, C, D, E, F
    • Schmoll, T., Morschhauser, J., Ott, M., Ludwig, B., van Die, I., and Hacker, J., 1990, Complete genetic organization and functional aspects of the Escherichia coli S fimbrial adhesion determinant: nucleotide sequence of the genes sfa B, C, D, E, F, Microb Pathog. 9:331-343.
    • (1990) Microb Pathog , vol.9 , pp. 331-343
    • Schmoll, T.1    Morschhauser, J.2    Ott, M.3    Ludwig, B.4    Van Die, I.5    Hacker, J.6
  • 96
    • 0033015018 scopus 로고    scopus 로고
    • S-fimbriae from Escherichia coli bind to soluble glycoproteins from human milk
    • Schwertmann, A., Schroten, H., Hacker, J., and Kunz, C., 1999, S-fimbriae from Escherichia coli bind to soluble glycoproteins from human milk, J Pediatr Gastroenterol Nutr. 28:257-263.
    • (1999) J Pediatr Gastroenterol Nutr , vol.28 , pp. 257-263
    • Schwertmann, A.1    Schroten, H.2    Hacker, J.3    Kunz, C.4
  • 97
    • 0023191455 scopus 로고
    • Bacterial lectins, cell-cell recognition and infectious disease
    • Sharon, N., 1987, Bacterial lectins, cell-cell recognition and infectious disease, FEBS Lett. 217:145-157.
    • (1987) FEBS Lett , vol.217 , pp. 145-157
    • Sharon, N.1
  • 98
    • 0027085578 scopus 로고
    • Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly
    • Slonim, L.N., Pinkner, J.S., Branden, C.I., and Hultgren, S.J., 1992, Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly, EMBO J. 11:4747-4756.
    • (1992) EMBO J , vol.11 , pp. 4747-4756
    • Slonim, L.N.1    Pinkner, J.S.2    Branden, C.I.3    Hultgren, S.J.4
  • 100
    • 0029063295 scopus 로고
    • Quantitative differences in adhesiveness of type 1 fimbriated Escherichia coli due to structural differences in fimH genes
    • Sokurenko, E.V., Courtney, H.S., Maslow, J., Siitonen, A., and Hasty, D.L., 1995, Quantitative differences in adhesiveness of type 1 fimbriated Escherichia coli due to structural differences in fimH genes, J Bacteriol. 177:3680-3686.
    • (1995) J Bacteriol , vol.177 , pp. 3680-3686
    • Sokurenko, E.V.1    Courtney, H.S.2    Maslow, J.3    Siitonen, A.4    Hasty, D.L.5
  • 101
    • 0028153922 scopus 로고
    • FimH family of type 1 fimbrial adhesins: Functional heterogeneity due to minor sequence variations among fimH genes
    • Sokurenko, E.V., Courtney, H.S., Ohman, D.E., Klemm, P., and Hasty, D.L., 1994, FimH family of type 1 fimbrial adhesins: functional heterogeneity due to minor sequence variations among fimH genes, J Bacteriol. 176:748-755.
    • (1994) J Bacteriol , vol.176 , pp. 748-755
    • Sokurenko, E.V.1    Courtney, H.S.2    Ohman, D.E.3    Klemm, P.4    Hasty, D.L.5
  • 102
  • 103
    • 0031824082 scopus 로고    scopus 로고
    • The globoseries glycosphingolipid sialosyl galactosyl globoside is found in urinary tract tissues and is a preferred binding receptor in vitro for uropathogenic Escherichia coli expressing pap-encoded adhesins
    • Stapleton, A.E., Stroud, M.R., Hakomori, S.I., and Stamm, W.E., 1998, The globoseries glycosphingolipid sialosyl galactosyl globoside is found in urinary tract tissues and is a preferred binding receptor in vitro for uropathogenic Escherichia coli expressing pap-encoded adhesins, Infect Immun. 66:3856-3861.
    • (1998) Infect Immun , vol.66 , pp. 3856-3861
    • Stapleton, A.E.1    Stroud, M.R.2    Hakomori, S.I.3    Stamm, W.E.4
  • 104
    • 0029147944 scopus 로고
    • Structural requirements for the glycolipid receptor of human uropathogenic Escherichia coli
    • Striker, R., Nilsson, U., Stonecipher, A., Magnusson, G., and Hultgren, S.J., 1995, Structural requirements for the glycolipid receptor of human uropathogenic Escherichia coli, Mol Microbiol. 16:1021-1029.
    • (1995) Mol Microbiol , vol.16 , pp. 1021-1029
    • Striker, R.1    Nilsson, U.2    Stonecipher, A.3    Magnusson, G.4    Hultgren, S.J.5
  • 105
    • 0025335568 scopus 로고
    • Host-specificity of uropathogenic Escherichia coli depends on differences in binding specificity to Gal alpha 1-4Gal-containing isoreceptors
    • Stromberg, N., Marklund, B.I., Lund, B., Ilver, D., Hamers, A., Gaastra, W., Karlsson, K.A., and Normark, S., 1990, Host-specificity of uropathogenic Escherichia coli depends on differences in binding specificity to Gal alpha 1-4Gal-containing isoreceptors, EMBO J. 9:2001-2010.
    • (1990) EMBO J , vol.9 , pp. 2001-2010
    • Stromberg, N.1    Marklund, B.I.2    Lund, B.3    Ilver, D.4    Hamers, A.5    Gaastra, W.6    Karlsson, K.A.7    Normark, S.8
  • 106
    • 0025990949 scopus 로고
    • Saccharide orientation at the cell surface affects glycolipid receptor function
    • Stromberg, N., Nyholm, P.G., Pascher, I., and Normark, S., 1991, Saccharide orientation at the cell surface affects glycolipid receptor function, Proc Natl Acad Sci USA. 88:9340-9344.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9340-9344
    • Stromberg, N.1    Nyholm, P.G.2    Pascher, I.3    Normark, S.4
  • 107
    • 0034900034 scopus 로고    scopus 로고
    • The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors
    • Sung, M.A., Fleming, K., Chen, H.A., and Matthews, S., 2001, The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors, EMBO Rep. 2:621-627.
    • (2001) EMBO Rep , vol.2 , pp. 621-627
    • Sung, M.A.1    Fleming, K.2    Chen, H.A.3    Matthews, S.4
  • 110
    • 0035282690 scopus 로고    scopus 로고
    • Carbohydrate receptor depletion as an antimicrobial strategy for prevention of urinary tract infection
    • Svensson, M., Platt, F., Frendeus, B., Butters, T., Dwek, R., and Svanborg, C., 2001b, Carbohydrate receptor depletion as an antimicrobial strategy for prevention of urinary tract infection, J Infect Dis. 183 Suppl 1:S70-73.
    • (2001) J Infect Dis , vol.183 , Issue.1 SUPPL.
    • Svensson, M.1    Platt, F.2    Frendeus, B.3    Butters, T.4    Dwek, R.5    Svanborg, C.6
  • 111
    • 0026027036 scopus 로고
    • Molecular structure of the Dr adhesin: Nucleotide sequence and mapping of receptor-binding domain by use of fusion constructs
    • Swanson, T.N., Bilge, S.S., Nowicki, B., and Moseley, S.L., 1991, Molecular structure of the Dr adhesin: nucleotide sequence and mapping of receptor-binding domain by use of fusion constructs, Infect Immun. 59:261-268.
    • (1991) Infect Immun , vol.59 , pp. 261-268
    • Swanson, T.N.1    Bilge, S.S.2    Nowicki, B.3    Moseley, S.L.4
  • 112
    • 0034051753 scopus 로고    scopus 로고
    • Assembly of complex organelles: Pilus biogenesis in gram-negative bacteria as a model system
    • Thanassi, D.G. and Hultgren, S.J., 2000, Assembly of complex organelles: pilus biogenesis in gram-negative bacteria as a model system, Methods. 20:111-126.
    • (2000) Methods , vol.20 , pp. 111-126
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 113
    • 0032035356 scopus 로고    scopus 로고
    • The chaperone/usher pathway: A major terminal branch of the general secretory pathway
    • Thanassi, D.G., Saulino, E.T., and Hultgren, S.J., 1998a, The chaperone/usher pathway: a major terminal branch of the general secretory pathway, Curr Opin Microbiol. 1:223-231.
    • (1998) Curr Opin Microbiol , vol.1 , pp. 223-231
    • Thanassi, D.G.1    Saulino, E.T.2    Hultgren, S.J.3
  • 114
    • 0032539855 scopus 로고    scopus 로고
    • The PapC usher forms an oligomeric channel: Implications for pilus biogenesis across the outer membrane
    • Thanassi, D.G., Saulino, E.T., Lombardo, M.J., Roth, R., Heuser, J., and Hultgren, S.J., 1998b, The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane, Proc Natl Acad Sci USA. 95:3146-3151.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3146-3151
    • Thanassi, D.G.1    Saulino, E.T.2    Lombardo, M.J.3    Roth, R.4    Heuser, J.5    Hultgren, S.J.6
  • 115
    • 0036842083 scopus 로고    scopus 로고
    • Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis
    • Thanassi, D.G., Stathopoulos, C., Dodson, K., Geiger, D., and Hultgren, S.J., 2002, Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis, J Bacteriol. 184:6260-6269.
    • (2002) J Bacteriol , vol.184 , pp. 6260-6269
    • Thanassi, D.G.1    Stathopoulos, C.2    Dodson, K.3    Geiger, D.4    Hultgren, S.J.5
  • 116
    • 0030924003 scopus 로고    scopus 로고
    • Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection
    • Thankavel, K., Madison, B., Ikeda, T., Malaviya, R., Shah, A.H., Arumugam, P.M., and Abraham, S.N., 1997, Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection, J Clin Invest. 100:1123-1136.
    • (1997) J Clin Invest , vol.100 , pp. 1123-1136
    • Thankavel, K.1    Madison, B.2    Ikeda, T.3    Malaviya, R.4    Shah, A.H.5    Arumugam, P.M.6    Abraham, S.N.7
  • 117
    • 0037188917 scopus 로고    scopus 로고
    • Bacterial adhesion to target cells enhanced by shear force
    • Thomas, W.E., Trintchina, E., Forero, M., Vogel, V., and Sokurenko, E.V., 2002, Bacterial adhesion to target cells enhanced by shear force, Cell. 109:913-923.
    • (2002) Cell , vol.109 , pp. 913-923
    • Thomas, W.E.1    Trintchina, E.2    Forero, M.3    Vogel, V.4    Sokurenko, E.V.5
  • 118
    • 0036068831 scopus 로고    scopus 로고
    • Identification of amino acids in the Dr adhesin required for binding to decay-accelerating factor
    • Van Loy, C.P., Sokurenko, E.V., Samudrala, R., and Moseley, S.L., 2002, Identification of amino acids in the Dr adhesin required for binding to decay-accelerating factor, Mol Microbiol. 45:439-452.
    • (2002) Mol Microbiol , vol.45 , pp. 439-452
    • Van Loy, C.P.1    Sokurenko, E.V.2    Samudrala, R.3    Moseley, S.L.4
  • 119
    • 0037111626 scopus 로고    scopus 로고
    • The role of bacterial virulence and host factors in patients with Escherichia coli bacteremia who have acute cholangitis or upper urinary tract infection
    • Wang, M.C., Tseng, C.C., Chen, C.Y., Wu, J.J., and Huang, J.J., 2002, The role of bacterial virulence and host factors in patients with Escherichia coli bacteremia who have acute cholangitis or upper urinary tract infection, Clin Infect Dis. 35:1161-1166.
    • (2002) Clin Infect Dis , vol.35 , pp. 1161-1166
    • Wang, M.C.1    Tseng, C.C.2    Chen, C.Y.3    Wu, J.J.4    Huang, J.J.5
  • 122
    • 0027424720 scopus 로고
    • Molecular cloning of a 47 kDa tissue-specific and differentiation- dependent urothelial cell surface glycoprotein
    • Wu, X.-R. and Sun, T.-T., 1993, Molecular cloning of a 47 kDa tissue-specific and differentiation-dependent urothelial cell surface glycoprotein, J Cell Sci. 106:31-43.
    • (1993) J Cell Sci , vol.106 , pp. 31-43
    • Wu, X.-R.1    Sun, T.-T.2
  • 124
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: Preserved folding energy drives fiber formation
    • Zavialov, A.V., Berglund, J., Pudney, A.F., Fooks, L.J., Ibrahim, T.M., MacIntyre, S., and Knight, S.D., 2003, Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation, Cell 113:587-596.
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5    MacIntyre, S.6    Knight, S.D.7
  • 125
    • 0034747254 scopus 로고    scopus 로고
    • Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: Evidence from in vitro FimH binding
    • Zhou, G., Mo, W.J., Sebbel, P., Min, G., Neubert, T.A., Glockshuber, R., Wu, X.R., Sun, T.T., and Kong, X.P., 2001, Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro FimH binding, J Cell Sci. 114:4095-4103.
    • (2001) J Cell Sci , vol.114 , pp. 4095-4103
    • Zhou, G.1    Mo, W.J.2    Sebbel, P.3    Min, G.4    Neubert, T.A.5    Glockshuber, R.6    Wu, X.R.7    Sun, T.T.8    Kong, X.P.9


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