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Volumn 1843, Issue 8, 2014, Pages 1629-1641

The Type 1 secretion pathway - The hemolysin system and beyond

Author keywords

ABC transporter; Host pathogen interaction; Membrane fusion proteins; Protein interaction; Type I secretion systems

Indexed keywords

ABC TRANSPORTER; ADHESIN; ALPHA HEMOLYSIN; CALCIUM ION; HEMOLYSIN; MEMBRANE FUSION PROTEIN; MUTANT PROTEIN; PROTEINASE; TOLC PROTEIN; TRIACYLGLYCEROL LIPASE;

EID: 84902329691     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.09.017     Document Type: Review
Times cited : (155)

References (182)
  • 3
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review)
    • Holland I.B., Schmitt L., Young J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review). Mol. Membr. Biol. 2005, 22:29-39.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 4
    • 0021125517 scopus 로고
    • Functional characterization of a cloned haemolysin determinant from E. coli of human origin, encoding information for the secretion of a 107K polypeptide
    • Mackman N., Holland I.B. Functional characterization of a cloned haemolysin determinant from E. coli of human origin, encoding information for the secretion of a 107K polypeptide. Mol. Gen. Genet. 1984, 196:129-134.
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 129-134
    • Mackman, N.1    Holland, I.B.2
  • 5
    • 0019792611 scopus 로고
    • Haemolysin contributes to virulence of extra-intestinal E. coli infections
    • Welch R.A., Dellinger E.P., Minshew B., Falkow S. Haemolysin contributes to virulence of extra-intestinal E. coli infections. Nature 1981, 294:665-667.
    • (1981) Nature , vol.294 , pp. 665-667
    • Welch, R.A.1    Dellinger, E.P.2    Minshew, B.3    Falkow, S.4
  • 6
    • 0020415823 scopus 로고
    • Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli
    • Goebel W., Hedgpeth J. Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli. J. Bacteriol. 1982, 151:1290-1298.
    • (1982) J. Bacteriol. , vol.151 , pp. 1290-1298
    • Goebel, W.1    Hedgpeth, J.2
  • 7
    • 0028023120 scopus 로고
    • Secretion of the Serratia marcescens HasA protein by an ABC transporter
    • Letoffe S., Ghigo J.M., Wandersman C. Secretion of the Serratia marcescens HasA protein by an ABC transporter. J. Bacteriol. 1994, 176:5372-5377.
    • (1994) J. Bacteriol. , vol.176 , pp. 5372-5377
    • Letoffe, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 8
    • 0042065283 scopus 로고    scopus 로고
    • Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein
    • Hinsa S.M., Espinosa-Urgel M., Ramos J.L., O'Toole G.A. Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol. Microbiol. 2003, 49:905-918.
    • (2003) Mol. Microbiol. , vol.49 , pp. 905-918
    • Hinsa, S.M.1    Espinosa-Urgel, M.2    Ramos, J.L.3    O'Toole, G.A.4
  • 9
    • 0028567924 scopus 로고
    • Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
    • Stanley P., Packman L.C., Koronakis V., Hughes C. Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. Science 1994, 266:1992-1996.
    • (1994) Science , vol.266 , pp. 1992-1996
    • Stanley, P.1    Packman, L.C.2    Koronakis, V.3    Hughes, C.4
  • 10
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function
    • Stanley P., Koronakis V., Hughes C. Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function. Microbiol. Mol. Biol. Rev. 1998, 62:309-333.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 11
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 2000, 405:914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 12
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: the bacterial exit duct for proteins and drugs
    • Koronakis V., Eswaran J., Hughes C. Structure and function of TolC: the bacterial exit duct for proteins and drugs. Annu. Rev. Biochem. 2004, 73:467-489.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 16
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., Pos K.M. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 2006, 313:1295-1298.
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 17
    • 0031780199 scopus 로고    scopus 로고
    • Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system
    • Kawai E., Akatsuka H., Idei A., Shibatani T., Omori K. Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system. Mol. Microbiol. 1998, 27:941-952.
    • (1998) Mol. Microbiol. , vol.27 , pp. 941-952
    • Kawai, E.1    Akatsuka, H.2    Idei, A.3    Shibatani, T.4    Omori, K.5
  • 18
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores
    • Wandersman C., Stojiljkovic I. Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr. Opin. Microbiol. 2000, 3:215-220.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2
  • 19
    • 0026445951 scopus 로고
    • Hemin uptake system of Yersinia enterocolitica: similarities with other TonB-dependent systems in gram-negative bacteria
    • Stojiljkovic I., Hantke K. Hemin uptake system of Yersinia enterocolitica: similarities with other TonB-dependent systems in gram-negative bacteria. EMBO J. 1992, 11:4359-4367.
    • (1992) EMBO J. , vol.11 , pp. 4359-4367
    • Stojiljkovic, I.1    Hantke, K.2
  • 20
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman C., Delepelaire P. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 2004, 58:611-647.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 21
    • 0029806326 scopus 로고    scopus 로고
    • Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: a TolC analogue
    • Binet R., Wandersman C. Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: a TolC analogue. Mol. Microbiol. 1996, 22:265-273.
    • (1996) Mol. Microbiol. , vol.22 , pp. 265-273
    • Binet, R.1    Wandersman, C.2
  • 22
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein
    • Binet R., Wandersman C. Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein. EMBO J. 1995, 14:2298-2306.
    • (1995) EMBO J. , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 23
    • 0033955445 scopus 로고    scopus 로고
    • Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa
    • Ochsner U.A., Johnson Z., Vasil M.L. Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa. Microbiology 2000, 146(Pt 1):185-198.
    • (2000) Microbiology , vol.146 , Issue.1 PART , pp. 185-198
    • Ochsner, U.A.1    Johnson, Z.2    Vasil, M.L.3
  • 24
    • 0029023052 scopus 로고
    • Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa
    • Ochsner U.A., Reiser J. Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:6424-6428.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6424-6428
    • Ochsner, U.A.1    Reiser, J.2
  • 26
    • 33646236127 scopus 로고    scopus 로고
    • Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade
    • Cwerman H., Wandersman C., Biville F. Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade. J. Bacteriol. 2006, 188:3357-3364.
    • (2006) J. Bacteriol. , vol.188 , pp. 3357-3364
    • Cwerman, H.1    Wandersman, C.2    Biville, F.3
  • 27
    • 0038236453 scopus 로고    scopus 로고
    • Haemophore-mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules
    • Rossi M.S., Paquelin A., Ghigo J.M., Wandersman C. Haemophore-mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules. Mol. Microbiol. 2003, 48:1467-1480.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1467-1480
    • Rossi, M.S.1    Paquelin, A.2    Ghigo, J.M.3    Wandersman, C.4
  • 28
    • 0022260426 scopus 로고
    • Nucleotide sequence of an Escherichia coli chromosomal hemolysin
    • Felmlee T., Pellett S., Welch R.A. Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J. Bacteriol. 1985, 163:94-105.
    • (1985) J. Bacteriol. , vol.163 , pp. 94-105
    • Felmlee, T.1    Pellett, S.2    Welch, R.A.3
  • 29
    • 0021732545 scopus 로고
    • Expression and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli
    • Juarez A., Hughes C., Vogel M., Goebel W. Expression and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli. Mol. Gen. Genet. 1984, 197:196-203.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 196-203
    • Juarez, A.1    Hughes, C.2    Vogel, M.3    Goebel, W.4
  • 30
    • 0024049169 scopus 로고
    • Identification of the promoters directing in vivo expression of hemolysin genes in Proteus vulgaris and Escherichia coli
    • Koronakis V., Hughes C. Identification of the promoters directing in vivo expression of hemolysin genes in Proteus vulgaris and Escherichia coli. Mol. Gen. Genet. 1988, 213:99-104.
    • (1988) Mol. Gen. Genet. , vol.213 , pp. 99-104
    • Koronakis, V.1    Hughes, C.2
  • 31
    • 0023924635 scopus 로고
    • Transcriptional organization of the Escherichia coli hemolysin genes
    • Welch R.A., Pellett S. Transcriptional organization of the Escherichia coli hemolysin genes. J. Bacteriol. 1988, 170:1622-1630.
    • (1988) J. Bacteriol. , vol.170 , pp. 1622-1630
    • Welch, R.A.1    Pellett, S.2
  • 32
    • 0025249908 scopus 로고
    • HlyB-dependent secretion of hemolysin by uropathogenic Escherichia coli requires conserved sequences flanking the chromosomal hly determinant
    • Cross M.A., Koronakis V., Stanley P.L., Hughes C. HlyB-dependent secretion of hemolysin by uropathogenic Escherichia coli requires conserved sequences flanking the chromosomal hly determinant. J. Bacteriol. 1990, 172:1217-1224.
    • (1990) J. Bacteriol. , vol.172 , pp. 1217-1224
    • Cross, M.A.1    Koronakis, V.2    Stanley, P.L.3    Hughes, C.4
  • 33
    • 0018865447 scopus 로고
    • Rough mutants of Salmonella typhimurium: immunochemical and structural analysis of lipopolysaccharides from rfaH mutants
    • Lindberg A.A., Hellerqvist C.G. Rough mutants of Salmonella typhimurium: immunochemical and structural analysis of lipopolysaccharides from rfaH mutants. J. Gen. Microbiol. 1980, 116:25-32.
    • (1980) J. Gen. Microbiol. , vol.116 , pp. 25-32
    • Lindberg, A.A.1    Hellerqvist, C.G.2
  • 34
    • 0026609257 scopus 로고
    • Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes
    • Bailey M.J., Koronakis V., Schmoll T., Hughes C. Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes. Mol. Microbiol. 1992, 6:1003-1012.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1003-1012
    • Bailey, M.J.1    Koronakis, V.2    Schmoll, T.3    Hughes, C.4
  • 35
    • 0030996159 scopus 로고    scopus 로고
    • Enhancing transcription through the Escherichia coli hemolysin operon, hlyCABD: RfaH and upstream JUMPStart DNA sequences function together via a postinitiation mechanism
    • Leeds J.A., Welch R.A. Enhancing transcription through the Escherichia coli hemolysin operon, hlyCABD: RfaH and upstream JUMPStart DNA sequences function together via a postinitiation mechanism. J. Bacteriol. 1997, 179:3519-3527.
    • (1997) J. Bacteriol. , vol.179 , pp. 3519-3527
    • Leeds, J.A.1    Welch, R.A.2
  • 36
    • 0030063067 scopus 로고    scopus 로고
    • Suppression of transcription polarity in the Escherichia coli haemolysin operon by a short upstream element shared by polysaccharide and DNA transfer determinants
    • Nieto J.M., Bailey M.J., Hughes C., Koronakis V. Suppression of transcription polarity in the Escherichia coli haemolysin operon by a short upstream element shared by polysaccharide and DNA transfer determinants. Mol. Microbiol. 1996, 19:705-713.
    • (1996) Mol. Microbiol. , vol.19 , pp. 705-713
    • Nieto, J.M.1    Bailey, M.J.2    Hughes, C.3    Koronakis, V.4
  • 37
    • 0028318945 scopus 로고
    • The JUMPstart sequence: a 39bp element common to several polysaccharide gene clusters
    • Hobbs M., Reeves P.R. The JUMPstart sequence: a 39bp element common to several polysaccharide gene clusters. Mol. Microbiol. 1994, 12:855-856.
    • (1994) Mol. Microbiol. , vol.12 , pp. 855-856
    • Hobbs, M.1    Reeves, P.R.2
  • 38
    • 0030718529 scopus 로고    scopus 로고
    • RfaH and the ops element, components of a novel system controlling bacterial transcription elongation
    • Bailey M.J., Hughes C., Koronakis V. RfaH and the ops element, components of a novel system controlling bacterial transcription elongation. Mol. Microbiol. 1997, 26:845-851.
    • (1997) Mol. Microbiol. , vol.26 , pp. 845-851
    • Bailey, M.J.1    Hughes, C.2    Koronakis, V.3
  • 39
    • 0037133970 scopus 로고    scopus 로고
    • The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand
    • Artsimovitch I., Landick R. The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell 2002, 109:193-203.
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 41
    • 0021943351 scopus 로고
    • Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin
    • Nicaud J.M., Mackman N., Gray L., Holland I.B. Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin. Mol. Gen. Genet. 1985, 199:111-116.
    • (1985) Mol. Gen. Genet. , vol.199 , pp. 111-116
    • Nicaud, J.M.1    Mackman, N.2    Gray, L.3    Holland, I.B.4
  • 42
    • 0025292413 scopus 로고
    • The mechanism of secretion of hemolysin and other polypeptides from gram-negative bacteria
    • Holland I.B., Blight M.A., Kenny B. The mechanism of secretion of hemolysin and other polypeptides from gram-negative bacteria. J. Bioenerg. Biomembr. 1990, 22:473-491.
    • (1990) J. Bioenerg. Biomembr. , vol.22 , pp. 473-491
    • Holland, I.B.1    Blight, M.A.2    Kenny, B.3
  • 43
    • 0028967167 scopus 로고
    • Evidence for post-transcriptional regulation of the synthesis of the Escherichia coli HlyB haemolysin translocator and production of polyclonal anti-HlyB antibody
    • Blight M.A., Menichi B., Holland I.B. Evidence for post-transcriptional regulation of the synthesis of the Escherichia coli HlyB haemolysin translocator and production of polyclonal anti-HlyB antibody. Mol. Gen. Genet. 1995, 247:73-85.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 73-85
    • Blight, M.A.1    Menichi, B.2    Holland, I.B.3
  • 44
    • 0033020320 scopus 로고    scopus 로고
    • Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator
    • Pimenta A.L., Young J., Holland I.B., Blight M.A. Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator. Mol. Gen. Genet. 1999, 261:122-132.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 122-132
    • Pimenta, A.L.1    Young, J.2    Holland, I.B.3    Blight, M.A.4
  • 45
    • 0345268708 scopus 로고    scopus 로고
    • Expression of cnf1 by Escherichia coli J96 involves a large upstream DNA region including the hlyCABD operon, and is regulated by the RfaH protein
    • Landraud L., Gibert M., Popoff M.R., Boquet P., Gauthier M. Expression of cnf1 by Escherichia coli J96 involves a large upstream DNA region including the hlyCABD operon, and is regulated by the RfaH protein. Mol. Microbiol. 2003, 47:1653-1667.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1653-1667
    • Landraud, L.1    Gibert, M.2    Popoff, M.R.3    Boquet, P.4    Gauthier, M.5
  • 46
    • 33746629034 scopus 로고    scopus 로고
    • Role of histone-like proteins H-NS and StpA in expression of virulence determinants of uropathogenic Escherichia coli
    • Muller C.M., Dobrindt U., Nagy G., Emody L., Uhlin B.E., Hacker J. Role of histone-like proteins H-NS and StpA in expression of virulence determinants of uropathogenic Escherichia coli. J. Bacteriol. 2006, 188:5428-5438.
    • (2006) J. Bacteriol. , vol.188 , pp. 5428-5438
    • Muller, C.M.1    Dobrindt, U.2    Nagy, G.3    Emody, L.4    Uhlin, B.E.5    Hacker, J.6
  • 47
    • 0036276019 scopus 로고    scopus 로고
    • Efficient expression of the alpha-haemolysin determinant in the uropathogenic Escherichia coli strain 536 requires the leuX-encoded tRNA(5)(Leu)
    • Dobrindt U., Emody L., Gentschev I., Goebel W., Hacker J. Efficient expression of the alpha-haemolysin determinant in the uropathogenic Escherichia coli strain 536 requires the leuX-encoded tRNA(5)(Leu). Mol. Genet. Genomics 2002, 267:370-379.
    • (2002) Mol. Genet. Genomics , vol.267 , pp. 370-379
    • Dobrindt, U.1    Emody, L.2    Gentschev, I.3    Goebel, W.4    Hacker, J.5
  • 48
    • 66849115110 scopus 로고    scopus 로고
    • Regulation of the type I protein secretion system by the MisR/MisS two-component system in Neisseria meningitidis
    • Sannigrahi S., Zhang X., Tzeng Y.L. Regulation of the type I protein secretion system by the MisR/MisS two-component system in Neisseria meningitidis. Microbiology 2009, 155:1588-1601.
    • (2009) Microbiology , vol.155 , pp. 1588-1601
    • Sannigrahi, S.1    Zhang, X.2    Tzeng, Y.L.3
  • 49
    • 80052527806 scopus 로고    scopus 로고
    • HlyU is a positive regulator of hemolysin expression in Vibrio anguillarum
    • Li L., Mou X., Nelson D.R. HlyU is a positive regulator of hemolysin expression in Vibrio anguillarum. J. Bacteriol. 2011, 193:4779-4789.
    • (2011) J. Bacteriol. , vol.193 , pp. 4779-4789
    • Li, L.1    Mou, X.2    Nelson, D.R.3
  • 50
    • 47349116549 scopus 로고    scopus 로고
    • RpoS, H-NS, and DsrA influence EHEC hemolysin operon (ehxCABD) transcription in Escherichia coli O157:H7 strain EDL933
    • Li H., Granat A., Stewart V., Gillespie J.R. RpoS, H-NS, and DsrA influence EHEC hemolysin operon (ehxCABD) transcription in Escherichia coli O157:H7 strain EDL933. FEMS Microbiol. Lett. 2008, 285:257-262.
    • (2008) FEMS Microbiol. Lett. , vol.285 , pp. 257-262
    • Li, H.1    Granat, A.2    Stewart, V.3    Gillespie, J.R.4
  • 52
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman C., Delepelaire P. TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:4776-4780.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 53
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals
    • Koronakis V., Li J., Koronakis E., Stauffer K. Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals. Mol. Microbiol. 1997, 23:617-626.
    • (1997) Mol. Microbiol. , vol.23 , pp. 617-626
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 54
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu T., Koronakis E., Hughes C., Koronakis V. Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore. EMBO J. 1998, 17:6487-6496.
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 55
    • 8844241421 scopus 로고    scopus 로고
    • Type I secretion in gram-negative bacteria
    • Delepelaire P. Type I secretion in gram-negative bacteria. Biochim. Biophys. Acta 2004, 1694:149-161.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 149-161
    • Delepelaire, P.1
  • 57
    • 0037459244 scopus 로고    scopus 로고
    • Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus
    • Eswaran J., Hughes C., Koronakis V. Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus. J. Mol. Biol. 2003, 327:309-315.
    • (2003) J. Mol. Biol. , vol.327 , pp. 309-315
    • Eswaran, J.1    Hughes, C.2    Koronakis, V.3
  • 58
    • 0034792632 scopus 로고    scopus 로고
    • The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis
    • Sharff A., Fanutti C., Shi J., Calladine C., Luisi B. The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis. Eur. J. Biochem. 2001, 268:5011-5026.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5011-5026
    • Sharff, A.1    Fanutti, C.2    Shi, J.3    Calladine, C.4    Luisi, B.5
  • 59
    • 0023432172 scopus 로고
    • Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12
    • Misra R., Reeves P.R. Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12. J. Bacteriol. 1987, 169:4722-4730.
    • (1987) J. Bacteriol. , vol.169 , pp. 4722-4730
    • Misra, R.1    Reeves, P.R.2
  • 60
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh T., Paulsen I.T., Saier M.H. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J. Bacteriol. 1994, 176:3825-3831.
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier, M.H.3
  • 61
    • 0020629077 scopus 로고
    • Transport of hemolysin across the outer membrane of Escherichia coli requires two functions
    • Wagner W., Vogel M., Goebel W. Transport of hemolysin across the outer membrane of Escherichia coli requires two functions. J. Bacteriol. 1983, 154:200-210.
    • (1983) J. Bacteriol. , vol.154 , pp. 200-210
    • Wagner, W.1    Vogel, M.2    Goebel, W.3
  • 64
    • 0026012975 scopus 로고
    • Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of a large family of prokaryote and eukaryote surface transport proteins
    • Wang R.C., Seror S.J., Blight M., Pratt J.M., Broome-Smith J.K., Holland I.B. Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of a large family of prokaryote and eukaryote surface transport proteins. J. Mol. Biol. 1991, 217:441-454.
    • (1991) J. Mol. Biol. , vol.217 , pp. 441-454
    • Wang, R.C.1    Seror, S.J.2    Blight, M.3    Pratt, J.M.4    Broome-Smith, J.K.5    Holland, I.B.6
  • 65
    • 84863712924 scopus 로고    scopus 로고
    • Membrane fusion proteins of type I secretion system and tripartite efflux pumps share a binding motif for TolC in gram-negative bacteria
    • Lee M., Jun S.Y., Yoon B.Y., Song S., Lee K., Ha N.C. Membrane fusion proteins of type I secretion system and tripartite efflux pumps share a binding motif for TolC in gram-negative bacteria. PLoS One 2012, 7:e40460.
    • (2012) PLoS One , vol.7
    • Lee, M.1    Jun, S.Y.2    Yoon, B.Y.3    Song, S.4    Lee, K.5    Ha, N.C.6
  • 67
    • 79955946992 scopus 로고    scopus 로고
    • Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria
    • Xu Y., Lee M., Moeller A., Song S., Yoon B.Y., Kim H.M., Jun S.Y., Lee K., Ha N.C. Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria. J. Biol. Chem. 2011, 286:17910-17920.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17910-17920
    • Xu, Y.1    Lee, M.2    Moeller, A.3    Song, S.4    Yoon, B.Y.5    Kim, H.M.6    Jun, S.Y.7    Lee, K.8    Ha, N.C.9
  • 69
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 1992, 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 70
    • 0037133735 scopus 로고    scopus 로고
    • Structure and association of ATP-binding cassette transporter nucleotide-binding domains
    • Kerr I.D. Structure and association of ATP-binding cassette transporter nucleotide-binding domains. Biochim. Biophys. Acta 2002, 1561:47-64.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 47-64
    • Kerr, I.D.1
  • 71
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • (table of contents)
    • Davidson A.L., Dassa E., Orelle C., Chen J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 2008, 72:317-364. (table of contents).
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 73
    • 0038799733 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains
    • Schmitt L., Benabdelhak H., Blight M.A., Holland I.B., Stubbs M.T. Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains. J. Mol. Biol. 2003, 330:333-342.
    • (2003) J. Mol. Biol. , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, I.B.4    Stubbs, M.T.5
  • 74
    • 22244452024 scopus 로고    scopus 로고
    • Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter
    • Zaitseva J., Jenewein S., Wiedenmann A., Benabdelhak H., Holland I.B., Schmitt L. Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter. Biochemistry 2005, 44:9680-9690.
    • (2005) Biochemistry , vol.44 , pp. 9680-9690
    • Zaitseva, J.1    Jenewein, S.2    Wiedenmann, A.3    Benabdelhak, H.4    Holland, I.B.5    Schmitt, L.6
  • 75
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva J., Oswald C., Jumpertz T., Jenewein S., Wiedenmann A., Holland I.B., Schmitt L. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 2006, 25:3432-3443.
    • (2006) EMBO J. , vol.25 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5    Holland, I.B.6    Schmitt, L.7
  • 76
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 2006, 443:180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 77
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel E., Doeven M.K., Poolman B. ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett. 2006, 580:1023-1035.
    • (2006) FEBS Lett. , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 78
    • 31844434196 scopus 로고    scopus 로고
    • Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB
    • Hanekop N., Zaitseva J., Jenewein S., Holland I.B., Schmitt L. Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB. FEBS Lett. 2006, 580:1036-1041.
    • (2006) FEBS Lett. , vol.580 , pp. 1036-1041
    • Hanekop, N.1    Zaitseva, J.2    Jenewein, S.3    Holland, I.B.4    Schmitt, L.5
  • 79
  • 80
    • 8344241152 scopus 로고    scopus 로고
    • How do ABC transporters drive transport?
    • van der Does C., Tampe R. How do ABC transporters drive transport?. Biol. Chem. 2004, 385:927-933.
    • (2004) Biol. Chem. , vol.385 , pp. 927-933
    • van der Does, C.1    Tampe, R.2
  • 81
    • 84864564117 scopus 로고    scopus 로고
    • Perspectives on the structure-function of ABC transporters: the Switch and Constant Contact models
    • George A.M., Jones P.M. Perspectives on the structure-function of ABC transporters: the Switch and Constant Contact models. Prog. Biophys. Mol. Biol. 2012, 109:95-107.
    • (2012) Prog. Biophys. Mol. Biol. , vol.109 , pp. 95-107
    • George, A.M.1    Jones, P.M.2
  • 82
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D., Oldham M.L., Orelle C., Davidson A.L., Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 2009, 33:528-536.
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 83
    • 80053091327 scopus 로고    scopus 로고
    • Snapshots of the maltose transporter during ATP hydrolysis
    • Oldham M.L., Chen J. Snapshots of the maltose transporter during ATP hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:15152-15156.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 15152-15156
    • Oldham, M.L.1    Chen, J.2
  • 84
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham M.L., Khare D., Quiocho F.A., Davidson A.L., Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 2007, 450:515-521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 85
    • 0029908021 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding
    • Letoffe S., Delepelaire P., Wandersman C. Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J. 1996, 15:5804-5811.
    • (1996) EMBO J. , vol.15 , pp. 5804-5811
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 86
    • 0035955547 scopus 로고    scopus 로고
    • Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli
    • Balakrishnan L., Hughes C., Koronakis V. Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli. J. Mol. Biol. 2001, 313:501-510.
    • (2001) J. Mol. Biol. , vol.313 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3
  • 87
    • 0344405700 scopus 로고    scopus 로고
    • A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A
    • Benabdelhak H., Kiontke S., Horn C., Ernst R., Blight M.A., Holland I.B., Schmitt L. A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A. J. Mol. Biol. 2003, 327:1169-1179.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1169-1179
    • Benabdelhak, H.1    Kiontke, S.2    Horn, C.3    Ernst, R.4    Blight, M.A.5    Holland, I.B.6    Schmitt, L.7
  • 88
    • 0027171205 scopus 로고
    • Complementation of transport-deficient mutants of Escherichia coli alpha-hemolysin by second-site mutations in the transporter hemolysin B
    • Zhang F., Sheps J.A., Ling V. Complementation of transport-deficient mutants of Escherichia coli alpha-hemolysin by second-site mutations in the transporter hemolysin B. J. Biol. Chem. 1993, 268:19889-19895.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19889-19895
    • Zhang, F.1    Sheps, J.A.2    Ling, V.3
  • 89
    • 77955355049 scopus 로고    scopus 로고
    • Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin
    • Jumpertz T., Chervaux C., Racher K., Zouhair M., Blight M.A., Holland I.B., Schmitt L. Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin. Microbiology 2010, 156:2495-2505.
    • (2010) Microbiology , vol.156 , pp. 2495-2505
    • Jumpertz, T.1    Chervaux, C.2    Racher, K.3    Zouhair, M.4    Blight, M.A.5    Holland, I.B.6    Schmitt, L.7
  • 90
    • 0027945133 scopus 로고
    • Identification and preliminary characterization of temperature-sensitive mutations affecting HlyB, the translocator required for the secretion of haemolysin (HlyA) from Escherichia coli
    • Blight M.A., Pimenta A.L., Lazzaroni J.C., Dando C., Kotelevets L., Seror S.J., Holland I.B. Identification and preliminary characterization of temperature-sensitive mutations affecting HlyB, the translocator required for the secretion of haemolysin (HlyA) from Escherichia coli. Mol. Gen. Genet. 1994, 245:431-440.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 431-440
    • Blight, M.A.1    Pimenta, A.L.2    Lazzaroni, J.C.3    Dando, C.4    Kotelevets, L.5    Seror, S.J.6    Holland, I.B.7
  • 91
    • 13544264496 scopus 로고    scopus 로고
    • Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli
    • Sugamata Y., Shiba T. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli. Appl. Environ. Microbiol. 2005, 71:656-662.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 656-662
    • Sugamata, Y.1    Shiba, T.2
  • 92
    • 0030696854 scopus 로고    scopus 로고
    • In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli
    • Schlor S., Schmidt A., Maier E., Benz R., Goebel W., Gentschev I. In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli. Mol. Gen. Genet. 1997, 256:306-319.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 306-319
    • Schlor, S.1    Schmidt, A.2    Maier, E.3    Benz, R.4    Goebel, W.5    Gentschev, I.6
  • 93
    • 0028151060 scopus 로고
    • Identification and characterization of two functional domains of the hemolysin translocator protein HlyD
    • Schulein R., Gentschev I., Schlor S., Gross R., Goebel W. Identification and characterization of two functional domains of the hemolysin translocator protein HlyD. Mol. Gen. Genet. 1994, 245:203-211.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 203-211
    • Schulein, R.1    Gentschev, I.2    Schlor, S.3    Gross, R.4    Goebel, W.5
  • 94
    • 27144531235 scopus 로고    scopus 로고
    • Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin
    • Pimenta A.L., Racher K., Jamieson L., Blight M.A., Holland I.B. Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin. J. Bacteriol. 2005, 187:7471-7480.
    • (2005) J. Bacteriol. , vol.187 , pp. 7471-7480
    • Pimenta, A.L.1    Racher, K.2    Jamieson, L.3    Blight, M.A.4    Holland, I.B.5
  • 96
    • 0024795976 scopus 로고
    • A novel C-terminal signal sequence targets Escherichia coli haemolysin directly to the medium
    • Gray L., Baker K., Kenny B., Mackman N., Haigh R., Holland I.B. A novel C-terminal signal sequence targets Escherichia coli haemolysin directly to the medium. J. Cell Sci. Suppl. 1989, 11:45-57.
    • (1989) J. Cell Sci. Suppl. , vol.11 , pp. 45-57
    • Gray, L.1    Baker, K.2    Kenny, B.3    Mackman, N.4    Haigh, R.5    Holland, I.B.6
  • 97
    • 0022800438 scopus 로고
    • The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli
    • Gray L., Mackman N., Nicaud J.M., Holland I.B. The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli. Mol. Gen. Genet. 1986, 205:127-133.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 127-133
    • Gray, L.1    Mackman, N.2    Nicaud, J.M.3    Holland, I.B.4
  • 98
    • 0026095620 scopus 로고
    • Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or beta-galactosidase fused to the Hly C-terminal signal domain
    • Kenny B., Haigh R., Holland I.B. Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or beta-galactosidase fused to the Hly C-terminal signal domain. Mol. Microbiol. 1991, 5:2557-2568.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2557-2568
    • Kenny, B.1    Haigh, R.2    Holland, I.B.3
  • 99
    • 0026683501 scopus 로고
    • Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region
    • Kenny B., Taylor S., Holland I.B. Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region. Mol. Microbiol. 1992, 6:1477-1489.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1477-1489
    • Kenny, B.1    Taylor, S.2    Holland, I.B.3
  • 100
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin
    • Chervaux C., Holland I.B. Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin. J. Bacteriol. 1996, 178:1232-1236.
    • (1996) J. Bacteriol. , vol.178 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 101
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley P., Koronakis V., Hughes C. Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 1991, 5:2391-2403.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 102
    • 0029023510 scopus 로고
    • Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A
    • Yin Y., Zhang F., Ling V., Arrowsmith C.H. Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A. FEBS Lett. 1995, 366:1-5.
    • (1995) FEBS Lett. , vol.366 , pp. 1-5
    • Yin, Y.1    Zhang, F.2    Ling, V.3    Arrowsmith, C.H.4
  • 103
    • 0028936779 scopus 로고
    • Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA
    • Zhang F., Yin Y., Arrowsmith C.H., Ling V. Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. Biochemistry 1995, 34:4193-4201.
    • (1995) Biochemistry , vol.34 , pp. 4193-4201
    • Zhang, F.1    Yin, Y.2    Arrowsmith, C.H.3    Ling, V.4
  • 106
    • 0033105139 scopus 로고    scopus 로고
    • Slow changes in cytosolic free Ca2+ in Escherichia coli highlight two putative influx mechanisms in response to changes in extracellular calcium
    • Jones H.E., Holland I.B., Baker H.L., Campbell A.K. Slow changes in cytosolic free Ca2+ in Escherichia coli highlight two putative influx mechanisms in response to changes in extracellular calcium. Cell Calcium 1999, 25:265-274.
    • (1999) Cell Calcium , vol.25 , pp. 265-274
    • Jones, H.E.1    Holland, I.B.2    Baker, H.L.3    Campbell, A.K.4
  • 108
    • 0029042476 scopus 로고
    • Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi
    • Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. J. Mol. Biol. 1995, 248:653-661.
    • (1995) J. Mol. Biol. , vol.248 , pp. 653-661
    • Baumann, U.1    Bauer, M.2    Letoffe, S.3    Delepelaire, P.4    Wandersman, C.5
  • 109
    • 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. 1993, 12:3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 110
    • 33845892486 scopus 로고    scopus 로고
    • The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand
    • Czjzek M., Letoffe S., Wandersman C., Delepierre M., Lecroisey A., Izadi-Pruneyre N. The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand. J. Mol. Biol. 2007, 365:1176-1186.
    • (2007) J. Mol. Biol. , vol.365 , pp. 1176-1186
    • Czjzek, M.1    Letoffe, S.2    Wandersman, C.3    Delepierre, M.4    Lecroisey, A.5    Izadi-Pruneyre, N.6
  • 111
    • 35748968219 scopus 로고    scopus 로고
    • A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens
    • Meier R., Drepper T., Svensson V., Jaeger K.E., Baumann U. A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens. J. Biol. Chem. 2007, 282:31477-31483.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31477-31483
    • Meier, R.1    Drepper, T.2    Svensson, V.3    Jaeger, K.E.4    Baumann, U.5
  • 112
    • 84867404639 scopus 로고    scopus 로고
    • An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain
    • Lecher J., Schwarz C.K., Stoldt M., Smits S.H., Willbold D., Schmitt L. An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain. Structure 2012, 20:1778-1787.
    • (2012) Structure , vol.20 , pp. 1778-1787
    • Lecher, J.1    Schwarz, C.K.2    Stoldt, M.3    Smits, S.H.4    Willbold, D.5    Schmitt, L.6
  • 113
    • 0032481311 scopus 로고    scopus 로고
    • The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter
    • Delepelaire P., Wandersman C. The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. EMBO J. 1998, 17:936-944.
    • (1998) EMBO J. , vol.17 , pp. 936-944
    • Delepelaire, P.1    Wandersman, C.2
  • 114
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC-transporters
    • Schmitt L., Tampé R. Structure and mechanism of ABC-transporters. Curr. Opin. Struct. Biol. 2002, 12:754-760.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampé, R.2
  • 115
    • 2942578482 scopus 로고    scopus 로고
    • Peptide signal molecules and bacteriocins in Gram-negative bacteria: a genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters
    • Dirix G., Monsieurs P., Dombrecht B., Daniels R., Marchal K., Vanderleyden J., Michiels J. Peptide signal molecules and bacteriocins in Gram-negative bacteria: a genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters. Peptides 2004, 25:1425-1440.
    • (2004) Peptides , vol.25 , pp. 1425-1440
    • Dirix, G.1    Monsieurs, P.2    Dombrecht, B.3    Daniels, R.4    Marchal, K.5    Vanderleyden, J.6    Michiels, J.7
  • 116
    • 77951235672 scopus 로고    scopus 로고
    • Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway
    • Ishii S., Yano T., Ebihara A., Okamoto A., Manzoku M., Hayashi H. Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway. J. Biol. Chem. 2010, 285:10777-10785.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10777-10785
    • Ishii, S.1    Yano, T.2    Ebihara, A.3    Okamoto, A.4    Manzoku, M.5    Hayashi, H.6
  • 117
    • 77955296461 scopus 로고    scopus 로고
    • Multiple signals direct the assembly and function of a type 1 secretion system
    • Masi M., Wandersman C. Multiple signals direct the assembly and function of a type 1 secretion system. J. Bacteriol. 2010, 192:3861-3869.
    • (2010) J. Bacteriol. , vol.192 , pp. 3861-3869
    • Masi, M.1    Wandersman, C.2
  • 118
    • 0025363228 scopus 로고
    • Effects of Escherichia coli hemolysin on human monocytes. Cytocidal action and stimulation of interleukin 1 release
    • Bhakdi S., Muhly M., Korom S., Schmidt G. Effects of Escherichia coli hemolysin on human monocytes. Cytocidal action and stimulation of interleukin 1 release. J. Clin. Invest. 1990, 85:1746-1753.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1746-1753
    • Bhakdi, S.1    Muhly, M.2    Korom, S.3    Schmidt, G.4
  • 119
    • 0020532037 scopus 로고
    • Cytotoxic effect of an alpha-hemolytic Escherichia coli strain on human blood monocytes and granulocytes in vitro
    • Gadeberg O.V., Orskov I., Rhodes J.M. Cytotoxic effect of an alpha-hemolytic Escherichia coli strain on human blood monocytes and granulocytes in vitro. Infect. Immun. 1983, 41:358-364.
    • (1983) Infect. Immun. , vol.41 , pp. 358-364
    • Gadeberg, O.V.1    Orskov, I.2    Rhodes, J.M.3
  • 120
    • 0019989629 scopus 로고
    • Effect of Escherichia coli alpha-hemolysin on human peripheral leukocyte function in vitro
    • Cavalieri S.J., Snyder I.S. Effect of Escherichia coli alpha-hemolysin on human peripheral leukocyte function in vitro. Infect. Immun. 1982, 37:966-974.
    • (1982) Infect. Immun. , vol.37 , pp. 966-974
    • Cavalieri, S.J.1    Snyder, I.S.2
  • 121
    • 0026331369 scopus 로고
    • Subhemolytic doses of Escherichia coli hemolysin evoke large quantities of lipoxygenase products in human neutrophils
    • Grimminger F., Scholz C., Bhakdi S., Seeger W. Subhemolytic doses of Escherichia coli hemolysin evoke large quantities of lipoxygenase products in human neutrophils. J. Biol. Chem. 1991, 266:14262-14269.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14262-14269
    • Grimminger, F.1    Scholz, C.2    Bhakdi, S.3    Seeger, W.4
  • 122
    • 0025000851 scopus 로고
    • Effects of Escherichia coli hemolysin on endothelial cell function
    • Suttorp N., Floer B., Schnittler H., Seeger W., Bhakdi S. Effects of Escherichia coli hemolysin on endothelial cell function. Infect. Immun. 1990, 58:3796-3801.
    • (1990) Infect. Immun. , vol.58 , pp. 3796-3801
    • Suttorp, N.1    Floer, B.2    Schnittler, H.3    Seeger, W.4    Bhakdi, S.5
  • 123
    • 0023158052 scopus 로고
    • Mechanism of Escherichia coli alpha-hemolysin-induced injury to isolated renal tubular cells
    • Keane W.F., Welch R., Gekker G., Peterson P.K. Mechanism of Escherichia coli alpha-hemolysin-induced injury to isolated renal tubular cells. Am. J. Pathol. 1987, 126:350-357.
    • (1987) Am. J. Pathol. , vol.126 , pp. 350-357
    • Keane, W.F.1    Welch, R.2    Gekker, G.3    Peterson, P.K.4
  • 125
    • 0016665575 scopus 로고
    • Properties of strains of Escherichia coli isolated from a variety of sources
    • Cooke E.M., Ewins S.P. Properties of strains of Escherichia coli isolated from a variety of sources. J. Med. Microbiol. 1975, 8:107-111.
    • (1975) J. Med. Microbiol. , vol.8 , pp. 107-111
    • Cooke, E.M.1    Ewins, S.P.2
  • 126
    • 0018870162 scopus 로고
    • Uropathogenic properties of Escherichia coli in recurrent urinary-tract infection
    • Brooks H.J., O'Grady F., McSherry M.A., Cattell W.R. Uropathogenic properties of Escherichia coli in recurrent urinary-tract infection. J. Med. Microbiol. 1980, 13:57-68.
    • (1980) J. Med. Microbiol. , vol.13 , pp. 57-68
    • Brooks, H.J.1    O'Grady, F.2    McSherry, M.A.3    Cattell, W.R.4
  • 127
    • 0018887185 scopus 로고
    • Hemolytic activity in enterotoxigenic and non-enterotoxigenic strains of Escherichia coli
    • DeBoy J.M., Wachsmuth I.K., Davis B.R. Hemolytic activity in enterotoxigenic and non-enterotoxigenic strains of Escherichia coli. J. Clin. Microbiol. 1980, 12:193-198.
    • (1980) J. Clin. Microbiol. , vol.12 , pp. 193-198
    • DeBoy, J.M.1    Wachsmuth, I.K.2    Davis, B.R.3
  • 128
    • 0017885062 scopus 로고
    • Association of hemolysin production, hemagglutination of human erythrocytes, and virulence for chicken embryos of extraintestinal Escherichia coli isolates
    • Minshew B.H., Jorgensen J., Counts G.W., Falkow S. Association of hemolysin production, hemagglutination of human erythrocytes, and virulence for chicken embryos of extraintestinal Escherichia coli isolates. Infect. Immun. 1978, 20:50-54.
    • (1978) Infect. Immun. , vol.20 , pp. 50-54
    • Minshew, B.H.1    Jorgensen, J.2    Counts, G.W.3    Falkow, S.4
  • 129
    • 0016165402 scopus 로고
    • The kinetics of erythrocyte lysis by Escherichia coli haemolysin
    • Rennie R.P., Freer J.H., Arbuthnott J.P. The kinetics of erythrocyte lysis by Escherichia coli haemolysin. J. Med. Microbiol. 1974, 7:189-195.
    • (1974) J. Med. Microbiol. , vol.7 , pp. 189-195
    • Rennie, R.P.1    Freer, J.H.2    Arbuthnott, J.P.3
  • 130
    • 0022654450 scopus 로고
    • Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores
    • Bhakdi S., Mackman N., Nicaud J.M., Holland I.B. Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores. Infect. Immun. 1986, 52:63-69.
    • (1986) Infect. Immun. , vol.52 , pp. 63-69
    • Bhakdi, S.1    Mackman, N.2    Nicaud, J.M.3    Holland, I.B.4
  • 131
    • 0015529164 scopus 로고
    • Molecular sieving of red cell membranes during gradual osmotic hemolysis
    • MacGregor R.D., Tobias C.A. Molecular sieving of red cell membranes during gradual osmotic hemolysis. J. Membr. Biol. 1972, 10:345-356.
    • (1972) J. Membr. Biol. , vol.10 , pp. 345-356
    • MacGregor, R.D.1    Tobias, C.A.2
  • 132
    • 0028281989 scopus 로고
    • Pore-formation by Escherichia coli hemolysin (HlyA) and other members of the RTX toxins family
    • Menestrina G., Moser C., Pellet S., Welch R. Pore-formation by Escherichia coli hemolysin (HlyA) and other members of the RTX toxins family. Toxicology 1994, 87:249-267.
    • (1994) Toxicology , vol.87 , pp. 249-267
    • Menestrina, G.1    Moser, C.2    Pellet, S.3    Welch, R.4
  • 135
    • 0029793144 scopus 로고    scopus 로고
    • Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayers
    • Bakas L., Ostolaza H., Vaz W.L., Goni F.M. Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayers. Biophys. J. 1996, 71:1869-1876.
    • (1996) Biophys. J. , vol.71 , pp. 1869-1876
    • Bakas, L.1    Ostolaza, H.2    Vaz, W.L.3    Goni, F.M.4
  • 136
    • 0030976393 scopus 로고    scopus 로고
    • Prelytic and lytic conformations of erythrocyte-associated Escherichia coli hemolysin
    • Moayeri M., Welch R.A. Prelytic and lytic conformations of erythrocyte-associated Escherichia coli hemolysin. Infect. Immun. 1997, 65:2233-2239.
    • (1997) Infect. Immun. , vol.65 , pp. 2233-2239
    • Moayeri, M.1    Welch, R.A.2
  • 137
    • 0029084310 scopus 로고
    • Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: protein binding does not always lead to lytic activity
    • Ostolaza H., Goni F.M. Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: protein binding does not always lead to lytic activity. FEBS Lett. 1995, 371:303-306.
    • (1995) FEBS Lett. , vol.371 , pp. 303-306
    • Ostolaza, H.1    Goni, F.M.2
  • 139
    • 0029809008 scopus 로고    scopus 로고
    • The effects of calcium and other polyvalent cations on channel formation by Escherichia coli alpha-hemolysin in red blood cells and lipid bilayer membranes
    • Dobereiner A., Schmid A., Ludwig A., Goebel W., Benz R. The effects of calcium and other polyvalent cations on channel formation by Escherichia coli alpha-hemolysin in red blood cells and lipid bilayer membranes. Eur. J. Biochem. 1996, 240:454-460.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 454-460
    • Dobereiner, A.1    Schmid, A.2    Ludwig, A.3    Goebel, W.4    Benz, R.5
  • 140
    • 0025288364 scopus 로고
    • Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes
    • Boehm D.F., Welch R.A., Snyder I.S. Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes. Infect. Immun. 1990, 58:1959-1964.
    • (1990) Infect. Immun. , vol.58 , pp. 1959-1964
    • Boehm, D.F.1    Welch, R.A.2    Snyder, I.S.3
  • 141
    • 0024504752 scopus 로고
    • Synthesis, inactivation, and localization of extracellular and intracellular Escherichia coli hemolysins
    • Oropeza-Wekerle R.L., Muller E., Kern P., Meyermann R., Goebel W. Synthesis, inactivation, and localization of extracellular and intracellular Escherichia coli hemolysins. J. Bacteriol. 1989, 171:2783-2788.
    • (1989) J. Bacteriol. , vol.171 , pp. 2783-2788
    • Oropeza-Wekerle, R.L.1    Muller, E.2    Kern, P.3    Meyermann, R.4    Goebel, W.5
  • 142
    • 0029979169 scopus 로고    scopus 로고
    • Purification of Escherichia coli pro-haemolysin, and a comparison with the properties of mature alpha-haemolysin
    • Soloaga A., Ostolaza H., Goni F.M., de la Cruz F. Purification of Escherichia coli pro-haemolysin, and a comparison with the properties of mature alpha-haemolysin. Eur. J. Biochem. 1996, 238:418-422.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 418-422
    • Soloaga, A.1    Ostolaza, H.2    Goni, F.M.3    de la Cruz, F.4
  • 143
    • 0024455884 scopus 로고
    • Electrical properties and molecular architecture of the channel formed by Escherichia coli hemolysin in planar lipid membranes
    • Ropele M., Menestrina G. Electrical properties and molecular architecture of the channel formed by Escherichia coli hemolysin in planar lipid membranes. Biochim. Biophys. Acta 1989, 985:9-18.
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 9-18
    • Ropele, M.1    Menestrina, G.2
  • 144
    • 0024548586 scopus 로고
    • Quantitative study of the binding and hemolytic efficiency of Escherichia coli hemolysin
    • Eberspacher B., Hugo F., Bhakdi S. Quantitative study of the binding and hemolytic efficiency of Escherichia coli hemolysin. Infect. Immun. 1989, 57:983-988.
    • (1989) Infect. Immun. , vol.57 , pp. 983-988
    • Eberspacher, B.1    Hugo, F.2    Bhakdi, S.3
  • 145
    • 69949119994 scopus 로고    scopus 로고
    • Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process
    • Herlax V., Mate S., Rimoldi O., Bakas L. Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process. J. Biol. Chem. 2009, 284:25199-25210.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25199-25210
    • Herlax, V.1    Mate, S.2    Rimoldi, O.3    Bakas, L.4
  • 147
    • 0023933497 scopus 로고
    • Killing of human myelomonocytic leukemia and lymphocytic cell lines by Actinobacillus actinomycetemcomitans leukotoxin
    • Simpson D.L., Berthold P., Taichman N.S. Killing of human myelomonocytic leukemia and lymphocytic cell lines by Actinobacillus actinomycetemcomitans leukotoxin. Infect. Immun. 1988, 56:1162-1166.
    • (1988) Infect. Immun. , vol.56 , pp. 1162-1166
    • Simpson, D.L.1    Berthold, P.2    Taichman, N.S.3
  • 148
    • 44449178675 scopus 로고    scopus 로고
    • RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
    • Morova J., Osicka R., Masin J., Sebo P. RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:5355-5360.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5355-5360
    • Morova, J.1    Osicka, R.2    Masin, J.3    Sebo, P.4
  • 149
    • 0026541137 scopus 로고
    • Circulating integrins: alpha 5 beta 1, alpha 6 beta 4 and Mac-1, but not alpha 3 beta 1, alpha 4 beta 1 or LFA-1
    • Bretscher M.S. Circulating integrins: alpha 5 beta 1, alpha 6 beta 4 and Mac-1, but not alpha 3 beta 1, alpha 4 beta 1 or LFA-1. EMBO J. 1992, 11:405-410.
    • (1992) EMBO J. , vol.11 , pp. 405-410
    • Bretscher, M.S.1
  • 150
    • 0035918310 scopus 로고    scopus 로고
    • Glycophorin as a receptor for Escherichia coli alpha-hemolysin in erythrocytes
    • Cortajarena A.L., Goni F.M., Ostolaza H. Glycophorin as a receptor for Escherichia coli alpha-hemolysin in erythrocytes. J. Biol. Chem. 2001, 276:12513-12519.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12513-12519
    • Cortajarena, A.L.1    Goni, F.M.2    Ostolaza, H.3
  • 152
    • 0031647028 scopus 로고    scopus 로고
    • Comparative study of the cytoplasmic domain of band 3 from human and rabbit erythrocyte membranes
    • Ligi F., Ciacci C., Palma F. Comparative study of the cytoplasmic domain of band 3 from human and rabbit erythrocyte membranes. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1998, 121:265-271.
    • (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.121 , pp. 265-271
    • Ligi, F.1    Ciacci, C.2    Palma, F.3
  • 154
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge T.J. Structures of gram-negative cell walls and their derived membrane vesicles. J. Bacteriol. 1999, 181:4725-4733.
    • (1999) J. Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 156
    • 33645070224 scopus 로고    scopus 로고
    • Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli
    • Balsalobre C., Silvan J.M., Berglund S., Mizunoe Y., Uhlin B.E., Wai S.N. Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli. Mol. Microbiol. 2006, 59:99-112.
    • (2006) Mol. Microbiol. , vol.59 , pp. 99-112
    • Balsalobre, C.1    Silvan, J.M.2    Berglund, S.3    Mizunoe, Y.4    Uhlin, B.E.5    Wai, S.N.6
  • 157
    • 10644226878 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty N.C., Mason K.M., Reedy M., Miller S.E., Kuehn M.J. Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells. EMBO J. 2004, 23:4538-4549.
    • (2004) EMBO J. , vol.23 , pp. 4538-4549
    • Kesty, N.C.1    Mason, K.M.2    Reedy, M.3    Miller, S.E.4    Kuehn, M.J.5
  • 159
    • 0023086182 scopus 로고
    • Damage to mammalian cells by proteins that form transmembrane pores
    • Bhakdi S., Tranum-Jensen J. Damage to mammalian cells by proteins that form transmembrane pores. Rev. Physiol. Biochem. Pharmacol. 1987, 107:147-223.
    • (1987) Rev. Physiol. Biochem. Pharmacol. , vol.107 , pp. 147-223
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 160
    • 0024282476 scopus 로고
    • Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism
    • Menestrina G. Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism. FEBS Lett. 1988, 232:217-220.
    • (1988) FEBS Lett. , vol.232 , pp. 217-220
    • Menestrina, G.1
  • 161
    • 0023666566 scopus 로고
    • Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranes
    • Menestrina G., Mackman N., Holland I.B., Bhakdi S. Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranes. Biochim. Biophys. Acta 1987, 905:109-117.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 109-117
    • Menestrina, G.1    Mackman, N.2    Holland, I.B.3    Bhakdi, S.4
  • 162
    • 77952029786 scopus 로고    scopus 로고
    • Escherichia coli alpha-hemolysin triggers shrinkage of erythrocytes via K(Ca)3.1 and TMEM16A channels with subsequent phosphatidylserine exposure
    • Skals M., Jensen U.B., Ousingsawat J., Kunzelmann K., Leipziger J., Praetorius H.A. Escherichia coli alpha-hemolysin triggers shrinkage of erythrocytes via K(Ca)3.1 and TMEM16A channels with subsequent phosphatidylserine exposure. J. Biol. Chem. 2010, 285:15557-15565.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15557-15565
    • Skals, M.1    Jensen, U.B.2    Ousingsawat, J.3    Kunzelmann, K.4    Leipziger, J.5    Praetorius, H.A.6
  • 163
    • 0028100376 scopus 로고
    • Effects of temperature, time, and toxin concentration on lesion formation by the Escherichia coli hemolysin
    • Moayeri M., Welch R.A. Effects of temperature, time, and toxin concentration on lesion formation by the Escherichia coli hemolysin. Infect. Immun. 1994, 62:4124-4134.
    • (1994) Infect. Immun. , vol.62 , pp. 4124-4134
    • Moayeri, M.1    Welch, R.A.2
  • 164
    • 0018860239 scopus 로고
    • Effects of a single hit from the alpha hemolysin produced by Escherichia coli on the morphology of sheep erythrocytes
    • Jorgensen S.E., Hammer R.F., Wu G.K. Effects of a single hit from the alpha hemolysin produced by Escherichia coli on the morphology of sheep erythrocytes. Infect. Immun. 1980, 27:988-994.
    • (1980) Infect. Immun. , vol.27 , pp. 988-994
    • Jorgensen, S.E.1    Hammer, R.F.2    Wu, G.K.3
  • 165
    • 0005777513 scopus 로고
    • Properties of the hemolytic activities of Escherichia coli
    • Short E.C., Kurtz H.J. Properties of the hemolytic activities of Escherichia coli. Infect. Immun. 1971, 3:678-687.
    • (1971) Infect. Immun. , vol.3 , pp. 678-687
    • Short, E.C.1    Kurtz, H.J.2
  • 166
    • 0026671837 scopus 로고
    • Haemolysin of Escherichia coli: comparison of pore-forming properties between chromosome and plasmid-encoded haemolysins
    • Benz R., Dobereiner A., Ludwig A., Goebel W. Haemolysin of Escherichia coli: comparison of pore-forming properties between chromosome and plasmid-encoded haemolysins. FEMS Microbiol. Immunol. 1992, 5:55-62.
    • (1992) FEMS Microbiol. Immunol. , vol.5 , pp. 55-62
    • Benz, R.1    Dobereiner, A.2    Ludwig, A.3    Goebel, W.4
  • 167
    • 0027485301 scopus 로고
    • Oligomerization of Escherichia coli haemolysin (HlyA) is involved in pore formation
    • Ludwig A., Benz R., Goebel W. Oligomerization of Escherichia coli haemolysin (HlyA) is involved in pore formation. Mol. Gen. Genet. 1993, 241:89-96.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 89-96
    • Ludwig, A.1    Benz, R.2    Goebel, W.3
  • 168
    • 0037713171 scopus 로고    scopus 로고
    • A receptor-binding region in Escherichia coli alpha-haemolysin
    • Cortajarena A.L., Goni F.M., Ostolaza H. A receptor-binding region in Escherichia coli alpha-haemolysin. J. Biol. Chem. 2003, 278:19159-19163.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19159-19163
    • Cortajarena, A.L.1    Goni, F.M.2    Ostolaza, H.3
  • 169
    • 0024041944 scopus 로고
    • Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion
    • Felmlee T., Welch R.A. Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion. Proc. Natl. Acad. Sci. U. S. A. 1988, 85:5269-5273.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5269-5273
    • Felmlee, T.1    Welch, R.A.2
  • 170
    • 0025805768 scopus 로고
    • Mutations affecting pore formation by haemolysin from Escherichia coli
    • Ludwig A., Schmid A., Benz R., Goebel W. Mutations affecting pore formation by haemolysin from Escherichia coli. Mol. Gen. Genet. 1991, 226:198-208.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 198-208
    • Ludwig, A.1    Schmid, A.2    Benz, R.3    Goebel, W.4
  • 171
    • 0034864185 scopus 로고    scopus 로고
    • Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles
    • Hyland C., Vuillard L., Hughes C., Koronakis V. Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles. J. Bacteriol. 2001, 183:5364-5370.
    • (2001) J. Bacteriol. , vol.183 , pp. 5364-5370
    • Hyland, C.1    Vuillard, L.2    Hughes, C.3    Koronakis, V.4
  • 173
    • 0032531818 scopus 로고    scopus 로고
    • Calcium-a life and death signal
    • Berridge M.J., Bootman M.D., Lipp P. Calcium-a life and death signal. Nature 1998, 395:645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 175
    • 1242343771 scopus 로고    scopus 로고
    • Calcium signalling during cell interactions with bacterial pathogens
    • TranVan Nhieu G., Clair C., Grompone G., Sansonetti P. Calcium signalling during cell interactions with bacterial pathogens. Biol. Cell. 2004, 96:93-101.
    • (2004) Biol. Cell. , vol.96 , pp. 93-101
    • TranVan Nhieu, G.1    Clair, C.2    Grompone, G.3    Sansonetti, P.4
  • 177
    • 0025980794 scopus 로고
    • Alpha-haemolysin from E. coli. Purification and self-aggregation properties
    • Ostolaza H., Bartolome B., Serra J.L., de la Cruz F., Goni F.M. Alpha-haemolysin from E. coli. Purification and self-aggregation properties. FEBS Lett. 1991, 280:195-198.
    • (1991) FEBS Lett. , vol.280 , pp. 195-198
    • Ostolaza, H.1    Bartolome, B.2    Serra, J.L.3    de la Cruz, F.4    Goni, F.M.5
  • 178
    • 0025642947 scopus 로고
    • Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium
    • Schnittler H.J., Wilke A., Gress T., Suttorp N., Drenckhahn D. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J. Physiol. 1990, 431:379-401.
    • (1990) J. Physiol. , vol.431 , pp. 379-401
    • Schnittler, H.J.1    Wilke, A.2    Gress, T.3    Suttorp, N.4    Drenckhahn, D.5
  • 179
    • 84855998874 scopus 로고    scopus 로고
    • The UPEC pore-forming toxin alpha-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways
    • Dhakal B.K., Mulvey M.A. The UPEC pore-forming toxin alpha-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways. Cell Host Microbe 2012, 11:58-69.
    • (2012) Cell Host Microbe , vol.11 , pp. 58-69
    • Dhakal, B.K.1    Mulvey, M.A.2
  • 180
    • 62649090086 scopus 로고    scopus 로고
    • Alpha-hemolysin from Escherichia coli uses endogenous amplification through P2X receptor activation to induce hemolysis
    • Skals M., Jorgensen N.R., Leipziger J., Praetorius H.A. Alpha-hemolysin from Escherichia coli uses endogenous amplification through P2X receptor activation to induce hemolysis. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:4030-4035.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 4030-4035
    • Skals, M.1    Jorgensen, N.R.2    Leipziger, J.3    Praetorius, H.A.4
  • 182
    • 2342423633 scopus 로고    scopus 로고
    • The Pro-451 to Leu polymorphism within the C-terminal tail of P2X7 receptor impairs cell death but not phospholipase D activation in murine thymocytes
    • Le Stunff H., Auger R., Kanellopoulos J., Raymond M.N. The Pro-451 to Leu polymorphism within the C-terminal tail of P2X7 receptor impairs cell death but not phospholipase D activation in murine thymocytes. J. Biol. Chem. 2004, 279:16918-16926.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16918-16926
    • Le Stunff, H.1    Auger, R.2    Kanellopoulos, J.3    Raymond, M.N.4


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