메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

The bacterial intimins and invasins: A large and novel family of secreted proteins

Author keywords

[No Author keywords available]

Indexed keywords

INTIMIN; INVASIN; ADHESIN; BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 78650987801     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014403     Document Type: Article
Times cited : (48)

References (61)
  • 1
    • 34447116519 scopus 로고    scopus 로고
    • Protein secretion and membrane insertion systems in gramnegative bacteria
    • Saier MH, Jr. (2006) Protein secretion and membrane insertion systems in gramnegative bacteria. J Membr Biol 214: 75-90.
    • (2006) J Membr Biol , vol.214 , pp. 75-90
    • Saier Jr., M.H.1
  • 2
    • 0035212525 scopus 로고    scopus 로고
    • Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic
    • Wentzel A, Christmann A, Adams T, Kolmar H (2001) Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA. J Bacteriol 183: 7273-7284.
    • (2001) E. Coli Intimin EaeA. J Bacteriol , vol.183 , pp. 7273-7284
    • Wentzel, A.1    Christmann, A.2    Adams, T.3    Kolmar, H.4
  • 3
    • 43049144649 scopus 로고    scopus 로고
    • A novel secretion pathway of Salmonella enterica acts as an antivirulence modulator during salmonellosis
    • Gal-Mor O, Gibson DL, Baluta D, Vallance BA, Finlay BB (2008) A novel secretion pathway of Salmonella enterica acts as an antivirulence modulator during salmonellosis. PLoS Pathog 4: e1000036.
    • (2008) PLoS Pathog , vol.4
    • Gal-Mor, O.1    Gibson, D.L.2    Baluta, D.3    Vallance, B.A.4    Finlay, B.B.5
  • 4
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of nvasin: A bacterial integrin-binding protein
    • Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ (1999) Crystal structure of nvasin: a bacterial integrin-binding protein. Science 286: 291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 5
    • 0034729685 scopus 로고    scopus 로고
    • Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex
    • Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, et al. (2000) Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405: 1073-1077.
    • (2000) Nature , vol.405 , pp. 1073-1077
    • Luo, Y.1    Frey, E.A.2    Pfuetzner, R.A.3    Creagh, A.L.4    Knoechel, D.G.5
  • 6
    • 1642493657 scopus 로고    scopus 로고
    • Adhesins and invasins of pathogenic bacteria: A structural view
    • Niemann HH, Schubert WD, Heinz DW (2004) Adhesins and invasins of pathogenic bacteria: a structural view. Microbes Infect 6: 101-112.
    • (2004) Microbes Infect , vol.6 , pp. 101-112
    • Niemann, H.H.1    Schubert, W.D.2    Heinz, D.W.3
  • 7
    • 1842861589 scopus 로고    scopus 로고
    • Structural biology of bacterial pathogenesis
    • Remaut H, Waksman G (2004) Structural biology of bacterial pathogenesis. Curr Opin Struct Biol 14: 161-170.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 161-170
    • Remaut, H.1    Waksman, G.2
  • 8
    • 0025047435 scopus 로고
    • A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells
    • Jerse AE, Yu J, Tall BD, Kaper JB (1990) A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc Natl Acad Sci U S A 87: 7839-7843.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7839-7843
    • Jerse, A.E.1    Yu, J.2    Tall, B.D.3    Kaper, J.B.4
  • 9
    • 0031768381 scopus 로고    scopus 로고
    • Enteropathogenic and enterohaemorrhagic Escherichia coli: More subversive elements
    • Frankel G, Phillips AD, Rosenshine I, Dougan G, Kaper JB, et al. (1998) Enteropathogenic and enterohaemorrhagic Escherichia coli: more subversive elements. Mol Microbiol 30: 911-921.
    • (1998) Mol Microbiol , vol.30 , pp. 911-921
    • Frankel, G.1    Phillips, A.D.2    Rosenshine, I.3    Dougan, G.4    Kaper, J.B.5
  • 10
    • 0032918787 scopus 로고    scopus 로고
    • Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli
    • Kelly G, Prasannan S, Daniell S, Fleming K, Frankel G, et al. (1999) Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli. Nat Struct Biol 6: 313-318.
    • (1999) Nat Struct Biol , vol.6 , pp. 313-318
    • Kelly, G.1    Prasannan, S.2    Daniell, S.3    Fleming, K.4    Frankel, G.5
  • 11
    • 0032112782 scopus 로고    scopus 로고
    • Sequential assignment of the triple labelled 30.1 kDa cell-adhesion domain of intimin from enteropathogenic
    • Kelly G, Prasannan S, Daniell S, Frankel G, Dougan G, et al. (1998) Sequential assignment of the triple labelled 30.1 kDa cell-adhesion domain of intimin from enteropathogenic E. coli. J Biomol NMR 12: 189-191.
    • (1998) E. Coli. J Biomol NMR , vol.12 , pp. 189-191
    • Kelly, G.1    Prasannan, S.2    Daniell, S.3    Frankel, G.4    Dougan, G.5
  • 12
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny B, DeVinney R, Stein M, Reinscheid DJ, Frey EA, et al. (1997) Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91: 511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    Devinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5
  • 13
    • 1842376874 scopus 로고    scopus 로고
    • Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signaling events, including tyrosine phosphorylation of phospholipase C-gamma1
    • Kenny B, Finlay BB (1997) Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signaling events, including tyrosine phosphorylation of phospholipase C-gamma1. Infect Immun 65: 2528-2536.
    • (1997) Infect Immun , vol.65 , pp. 2528-2536
    • Kenny, B.1    Finlay, B.B.2
  • 14
    • 36448958686 scopus 로고    scopus 로고
    • Characterization of the binding surface of the translocated intimin receptor, an essential protein for EPEC and EHEC cell adhesion
    • Ross NT, Miller BL (2007) Characterization of the binding surface of the translocated intimin receptor, an essential protein for EPEC and EHEC cell adhesion. Protein Sci 16: 2677-2683.
    • (2007) Protein Sci , vol.16 , pp. 2677-2683
    • Ross, N.T.1    Miller, B.L.2
  • 15
    • 63049086403 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli subverts phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon epithelial cell infection
    • Sason H, Milgrom M, Weiss AM, Melamed-Book N, Balla T, et al. (2009) Enteropathogenic Escherichia coli subverts phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon epithelial cell infection. Mol Biol Cell 20: 544-555.
    • (2009) Mol Biol Cell , vol.20 , pp. 544-555
    • Sason, H.1    Milgrom, M.2    Weiss, A.M.3    Melamed-Book, N.4    Balla, T.5
  • 16
    • 31844448929 scopus 로고    scopus 로고
    • The established intimin receptor Tir and the putative eucaryotic intimin receptors nucleolin and beta1 integrin localize at or near the site of enterohemorrhagic Escherichia coli O157:H7 adherence to enterocytes in vivo
    • Sinclair JF, Dean-Nystrom EA, O'Brien AD (2006) The established intimin receptor Tir and the putative eucaryotic intimin receptors nucleolin and beta1 integrin localize at or near the site of enterohemorrhagic Escherichia coli O157:H7 adherence to enterocytes in vivo. Infect Immun 74: 1255-1265.
    • (2006) Infect Immun , vol.74 , pp. 1255-1265
    • Sinclair, J.F.1    Dean-Nystrom, E.A.2    O'Brien, A.D.3
  • 17
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation
    • Jarvis KG, Giron JA, Jerse AE, McDaniel TK, Donnenberg MS, et al. (1995) Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc Natl Acad Sci U S A 92: 7996-8000.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7996-8000
    • Jarvis, K.G.1    Giron, J.A.2    Jerse, A.E.3    McDaniel, T.K.4    Donnenberg, M.S.5
  • 19
    • 11844260767 scopus 로고    scopus 로고
    • Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation
    • Adams TM, Wentzel A, Kolmar H (2005) Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation. J Bacteriol 187: 522-533.
    • (2005) J Bacteriol , vol.187 , pp. 522-533
    • Adams, T.M.1    Wentzel, A.2    Kolmar, H.3
  • 20
    • 9344245722 scopus 로고    scopus 로고
    • Autotransporter and two-partner secretion: Delivery of large-size virulence factors by gram-negative bacterial pathogens
    • Newman CL, Stathopoulos C (2004) Autotransporter and two-partner secretion: delivery of large-size virulence factors by gram-negative bacterial pathogens. Crit Rev Microbiol 30: 275-286.
    • (2004) Crit Rev Microbiol , vol.30 , pp. 275-286
    • Newman, C.L.1    Stathopoulos, C.2
  • 21
    • 0025991209 scopus 로고
    • Mapping and topographic localization of epitopes of the Yersinia pseudotuberculosis invasin protein
    • Leong JM, Fournier RS, Isberg RR (1991) Mapping and topographic localization of epitopes of the Yersinia pseudotuberculosis invasin protein. Infect Immun 59: 3424-3433.
    • (1991) Infect Immun , vol.59 , pp. 3424-3433
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 22
    • 0026500253 scopus 로고
    • Cloning and characterization of the eae gene of enterohaemorrhagic Escherichia coli O157:H7
    • Yu J, Kaper JB (1992) Cloning and characterization of the eae gene of enterohaemorrhagic Escherichia coli O157:H7. Mol Microbiol 6: 411-417.
    • (1992) Mol Microbiol , vol.6 , pp. 411-417
    • Yu, J.1    Kaper, J.B.2
  • 23
    • 0034213976 scopus 로고    scopus 로고
    • Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli
    • Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, et al. (2000) Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli. EMBO J 19: 2452-2464.
    • (2000) EMBO J , vol.19 , pp. 2452-2464
    • Batchelor, M.1    Prasannan, S.2    Daniell, S.3    Reece, S.4    Connerton, I.5
  • 24
    • 0346334430 scopus 로고    scopus 로고
    • Selfassociation of EPEC intimin mediated by the beta-barrel-containing anchor domain: A role in clustering of the Tir receptor
    • Touze T, Hayward RD, Eswaran J, Leong JM, Koronakis V (2004) Selfassociation of EPEC intimin mediated by the beta-barrel-containing anchor domain: a role in clustering of the Tir receptor. Mol Microbiol 51: 73-87.
    • (2004) Mol Microbiol , vol.51 , pp. 73-87
    • Touze, T.1    Hayward, R.D.2    Eswaran, J.3    Leong, J.M.4    Koronakis, V.5
  • 26
    • 33748655033 scopus 로고    scopus 로고
    • Protein-translocating trimeric autotransporters of gram-negative bacteria
    • Kim DS, Chao Y, Saier MH, Jr. (2006) Protein-translocating trimeric autotransporters of gram-negative bacteria. J Bacteriol 188: 5655-5667.
    • (2006) J Bacteriol , vol.188 , pp. 5655-5667
    • Kim, D.S.1    Chao, Y.2    Saier Jr., M.H.3
  • 27
    • 0030688998 scopus 로고    scopus 로고
    • A novel family of channel-forming, autotransporting, bacterial virulence factors
    • Loveless BJ, Saier MH, Jr. (1997) A novel family of channel-forming, autotransporting, bacterial virulence factors. Mol Membr Biol 14: 113-123.
    • (1997) Mol Membr Biol , vol.14 , pp. 113-123
    • Loveless, B.J.1    Saier Jr., M.H.2
  • 29
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases
    • Altschul SF, Koonin EV (1998) Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases. Trends Biochem Sci 23: 444-447.
    • (1998) Trends Biochem Sci , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 31
    • 70349258246 scopus 로고    scopus 로고
    • Bioinformatic analyses of transmembrane transport: Novel software for deducing protein phylogeny, topology, and evolution
    • Yen MR, Choi J, Saier MH, Jr. (2009) Bioinformatic analyses of transmembrane transport: novel software for deducing protein phylogeny, topology, and evolution. J Mol Microbiol Biotechnol 17: 163-176.
    • (2009) J Mol Microbiol Biotechnol , vol.17 , pp. 163-176
    • Yen, M.R.1    Choi, J.2    Saier Jr., M.H.3
  • 32
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: A fast program for clustering and comparing large sets of protein or nucleotide sequences
    • Li W, Godzik A (2006) Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 22: 1658-1659.
    • (2006) Bioinformatics , vol.22 , pp. 1658-1659
    • Li, W.1    Godzik, A.2
  • 33
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 34
    • 0036132240 scopus 로고    scopus 로고
    • A web-based Tree View (TV) program for the visualization of phylogenetic trees
    • Zhai Y, Tchieu J, Saier MH, Jr. (2002) A web-based Tree View (TV) program for the visualization of phylogenetic trees. J Mol Microbiol Biotechnol 4: 69-70.
    • (2002) J Mol Microbiol Biotechnol , vol.4 , pp. 69-70
    • Zhai, Y.1    Tchieu, J.2    Saier Jr., M.H.3
  • 35
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • Saier MH, Jr. (1994) Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiol Rev 58: 71-93.
    • (1994) Microbiol Rev , vol.58 , pp. 71-93
    • Saier Jr., M.H.1
  • 36
    • 0034874253 scopus 로고    scopus 로고
    • A web-based program (WHAT) for the simultaneous prediction of hydropathy, amphipathicity, secondary structure and transmembrane topology for a single protein sequence
    • Zhai Y, Saier MH, Jr. (2001) A web-based program (WHAT) for the simultaneous prediction of hydropathy, amphipathicity, secondary structure and transmembrane topology for a single protein sequence. J Mol Microbiol Biotechnol 3: 501-502.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 501-502
    • Zhai, Y.1    Saier Jr., M.H.2
  • 37
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Moller S, Croning MD, Apweiler R (2001) Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics 17: 646-653.
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.2    Apweiler, R.3
  • 38
    • 0035087954 scopus 로고    scopus 로고
    • A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins
    • Zhai Y, Saier MH, Jr. (2001) A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins. J Mol Microbiol Biotechnol 3: 285-286.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 285-286
    • Zhai, Y.1    Saier Jr., M.H.2
  • 41
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4: 363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 43
    • 39749108675 scopus 로고    scopus 로고
    • The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity
    • Jong WS, Luirink J (2008) The conserved extension of the Hbp autotransporter signal peptide does not determine targeting pathway specificity. Biochem Biophys Res Commun 368: 522-527.
    • (2008) Biochem Biophys Res Commun , vol.368 , pp. 522-527
    • Jong, W.S.1    Luirink, J.2
  • 44
    • 33646918973 scopus 로고    scopus 로고
    • An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex
    • Peterson JH, Szabady RL, Bernstein HD (2006) An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex. J Biol Chem 281: 9038-9048.
    • (2006) J Biol Chem , vol.281 , pp. 9038-9048
    • Peterson, J.H.1    Szabady, R.L.2    Bernstein, H.D.3
  • 47
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman A, Bycroft M (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299: 1113-1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 48
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • Steen A, Buist G, Horsburgh GJ, Venema G, Kuipers OP, et al. (2005) AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning. FEBS J 272: 2854-2868.
    • (2005) FEBS J , vol.272 , pp. 2854-2868
    • Steen, A.1    Buist, G.2    Horsburgh, G.J.3    Venema, G.4    Kuipers, O.P.5
  • 49
    • 0037930133 scopus 로고    scopus 로고
    • Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents
    • Steen A, Buist G, Leenhouts KJ, El Khattabi M, Grijpstra F, et al. (2003) Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. J Biol Chem 278: 23874-23881.
    • (2003) J Biol Chem , vol.278 , pp. 23874-23881
    • Steen, A.1    Buist, G.2    Leenhouts, K.J.3    El Khattabi, M.4    Grijpstra, F.5
  • 50
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 51
    • 0030895157 scopus 로고    scopus 로고
    • Computer simulations of the OmpF porin from the outer membrane of Escherichia coli
    • Watanabe M, Rosenbusch J, Schirmer T, Karplus M (1997) Computer simulations of the OmpF porin from the outer membrane of Escherichia coli. Biophys J 72: 2094-2102.
    • (1997) Biophys J , vol.72 , pp. 2094-2102
    • Watanabe, M.1    Rosenbusch, J.2    Schirmer, T.3    Karplus, M.4
  • 52
    • 67749127364 scopus 로고    scopus 로고
    • Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains
    • Bodelon G, Marin E, Fernandez LA (2009) Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains. J Bacteriol 191: 5169-5179.
    • (2009) J Bacteriol , vol.191 , pp. 5169-5179
    • Bodelon, G.1    Marin, E.2    Fernandez, L.A.3
  • 54
    • 36849016945 scopus 로고    scopus 로고
    • Autotransporter structure reveals intra-barrel cleavage followed by conformational changes
    • Barnard TJ, Dautin N, Lukacik P, Bernstein HD, Buchanan SK (2007) Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nat Struct Mol Biol 14: 1214-1220.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1214-1220
    • Barnard, T.J.1    Dautin, N.2    Lukacik, P.3    Bernstein, H.D.4    Buchanan, S.K.5
  • 55
    • 33748068126 scopus 로고    scopus 로고
    • Role of the alpha-helical linker of the Cterminal translocator in the biogenesis of the serine protease subfamily of autotransporters
    • Kostakioti M, Stathopoulos C (2006) Role of the alpha-helical linker of the Cterminal translocator in the biogenesis of the serine protease subfamily of autotransporters. Infect Immun 74: 4961-4969.
    • (2006) Infect Immun , vol.74 , pp. 4961-4969
    • Kostakioti, M.1    Stathopoulos, C.2
  • 56
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng G, Surana NK, St Geme JW, 3rd, Waksman G (2006) Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J 25: 2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    Geme, S.J.W.3    Waksman, G.4
  • 57
    • 1942471665 scopus 로고    scopus 로고
    • Structure of the translocator domain of a bacterial autotransporter
    • Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, et al. (2004) Structure of the translocator domain of a bacterial autotransporter. EMBO J 23: 1257-1266.
    • (2004) EMBO J , vol.23 , pp. 1257-1266
    • Oomen, C.J.1    van Ulsen, P.2    van Gelder, P.3    Feijen, M.4    Tommassen, J.5
  • 60
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles TJ, Scott-Tucker A, Overduin M, Henderson IR (2009) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 7: 206-214.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 61
    • 0141890189 scopus 로고    scopus 로고
    • Evasion of phagocytosis through cooperation between two ligand-binding regions in Streptococcus pyogenes M protein
    • Carlsson F, Berggard K, Stalhammar-Carlemalm M, Lindahl G (2003) Evasion of phagocytosis through cooperation between two ligand-binding regions in Streptococcus pyogenes M protein. J Exp Med 198: 1057-1068.
    • (2003) J Exp Med , vol.198 , pp. 1057-1068
    • Carlsson, F.1    Berggard, K.2    Stalhammar-Carlemalm, M.3    Lindahl, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.