메뉴 건너뛰기




Volumn 9, Issue 1, 2013, Pages

Assembly of the Type II Secretion System such as Found in Vibrio cholerae Depends on the Novel Pilotin AspS

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PILOTIN ALTERNATE SECRETIN PATHWAY SUBUNIT S; SECRETIN; UNCLASSIFIED DRUG;

EID: 84875065984     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003117     Document Type: Article
Times cited : (56)

References (72)
  • 1
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J, (2007) Biogenesis of the gram-negative bacterial outer membrane. Annu Rev Microbiol 61: 191-214.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 2
    • 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
  • 3
    • 79959468179 scopus 로고    scopus 로고
    • beta-Barrel membrane protein assembly by the Bam complex
    • Hagan CL, Silhavy TJ, Kahne D, (2011) beta-Barrel membrane protein assembly by the Bam complex. Annu Rev Biochem 80: 189-210.
    • (2011) Annu Rev Biochem , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 4
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda H, Matsuyama S, (2004) Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 1693: 5-13.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 5
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda S, Tokuda H, (2011) Lipoprotein sorting in bacteria. Annu Rev Microbiol 65: 239-259.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 6
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi DG, Hultgren SJ, (2000) Multiple pathways allow protein secretion across the bacterial outer membrane. Curr Opin Cell Biol 12: 420-430.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 7
    • 0345306190 scopus 로고    scopus 로고
    • Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella
    • Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, et al. (2003) Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149: 3051-3072.
    • (2003) Microbiology , vol.149 , pp. 3051-3072
    • Peabody, C.R.1    Chung, Y.J.2    Yen, M.R.3    Vidal-Ingigliardi, D.4    Pugsley, A.P.5
  • 8
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A, (2004) The underlying mechanisms of type II protein secretion. Biochim Biophys Acta 1694: 163-179.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 9
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: dynamic channels for protein transport across membranes
    • Korotkov KV, Gonen T, Hol WG, (2011) Secretins: dynamic channels for protein transport across membranes. Trends Biochem Sci 36: 433-443.
    • (2011) Trends Biochem Sci , vol.36 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.3
  • 10
    • 80053453930 scopus 로고    scopus 로고
    • Structural and functional studies on the interaction of GspC and GspD in the type II secretion system
    • Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, et al. (2011) Structural and functional studies on the interaction of GspC and GspD in the type II secretion system. PLoS Pathog 7: e1002228.
    • (2011) PLoS Pathog , vol.7
    • Korotkov, K.V.1    Johnson, T.L.2    Jobling, M.G.3    Pruneda, J.4    Pardon, E.5
  • 11
    • 84859885138 scopus 로고    scopus 로고
    • The type II secretion system: biogenesis, molecular architecture and mechanism
    • Korotkov KV, Sandkvist M, Hol WG, (2012) The type II secretion system: biogenesis, molecular architecture and mechanism. Nat Rev Microbiol 10: 336-351.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 336-351
    • Korotkov, K.V.1    Sandkvist, M.2    Hol, W.G.3
  • 14
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie KR, Lory S, Pugsley AP, (1996) Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J 15: 978-988.
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 15
    • 0030965150 scopus 로고    scopus 로고
    • The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function
    • Daefler S, Guilvout I, Hardie KR, Pugsley AP, Russel M, (1997) The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function. Mol Microbiol 24: 465-475.
    • (1997) Mol Microbiol , vol.24 , pp. 465-475
    • Daefler, S.1    Guilvout, I.2    Hardie, K.R.3    Pugsley, A.P.4    Russel, M.5
  • 16
    • 49349091518 scopus 로고    scopus 로고
    • In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD
    • Guilvout I, Chami M, Berrier C, Ghazi A, Engel A, et al. (2008) In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD. J Mol Biol 382: 13-23.
    • (2008) J Mol Biol , vol.382 , pp. 13-23
    • Guilvout, I.1    Chami, M.2    Berrier, C.3    Ghazi, A.4    Engel, A.5
  • 17
    • 80655144742 scopus 로고    scopus 로고
    • Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone
    • Nickerson NN, Tosi T, Dessen A, Baron B, Raynal B, et al. (2011) Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone. J Biol Chem 286: 38833-38843.
    • (2011) J Biol Chem , vol.286 , pp. 38833-38843
    • Nickerson, N.N.1    Tosi, T.2    Dessen, A.3    Baron, B.4    Raynal, B.5
  • 18
    • 83355177984 scopus 로고    scopus 로고
    • Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca
    • Tosi T, Nickerson NN, Mollica L, Jensen MR, Blackledge M, et al. (2011) Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca. Mol Microbiol 82: 1422-1432.
    • (2011) Mol Microbiol , vol.82 , pp. 1422-1432
    • Tosi, T.1    Nickerson, N.N.2    Mollica, L.3    Jensen, M.R.4    Blackledge, M.5
  • 19
    • 79955027962 scopus 로고    scopus 로고
    • Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin
    • Collin S, Guilvout I, Nickerson NN, Pugsley AP, (2011) Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin. Mol Microbiol 80: 655-665.
    • (2011) Mol Microbiol , vol.80 , pp. 655-665
    • Collin, S.1    Guilvout, I.2    Nickerson, N.N.3    Pugsley, A.P.4
  • 20
    • 0031736546 scopus 로고    scopus 로고
    • Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system
    • Shevchik VE, Condemine G, (1998) Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system. Microbiology 144 (Pt 11):: 3219-3228.
    • (1998) Microbiology , vol.144 , Issue.Pt 11 , pp. 3219-3228
    • Shevchik, V.E.1    Condemine, G.2
  • 21
    • 0030993971 scopus 로고    scopus 로고
    • A gene cluster closely related to type II secretion pathway operons of gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strains
    • Schmidt H, Henkel B, Karch H, (1997) A gene cluster closely related to type II secretion pathway operons of gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strains. FEMS Microbiol Lett 148: 265-272.
    • (1997) FEMS Microbiol Lett , vol.148 , pp. 265-272
    • Schmidt, H.1    Henkel, B.2    Karch, H.3
  • 22
    • 84860904270 scopus 로고    scopus 로고
    • Structural and functional insights into the pilotin-secretin complex of the type II secretion system
    • Gu S, Rehman S, Wang X, Shevchik VE, Pickersgill RW, (2012) Structural and functional insights into the pilotin-secretin complex of the type II secretion system. PLoS Pathog 8: e1002531.
    • (2012) PLoS Pathog , vol.8
    • Gu, S.1    Rehman, S.2    Wang, X.3    Shevchik, V.E.4    Pickersgill, R.W.5
  • 23
    • 84863836580 scopus 로고    scopus 로고
    • The Type II Secretion System and Its Ubiquitous Lipoprotein Substrate, SslE, Are Required for Biofilm Formation and Virulence of Enteropathogenic Escherichia coli
    • Baldi DL, Higginson EE, Hocking DM, Praszkier J, Cavaliere R, et al. (2012) The Type II Secretion System and Its Ubiquitous Lipoprotein Substrate, SslE, Are Required for Biofilm Formation and Virulence of Enteropathogenic Escherichia coli. Infect Immun 80: 2042-2052.
    • (2012) Infect Immun , vol.80 , pp. 2042-2052
    • Baldi, D.L.1    Higginson, E.E.2    Hocking, D.M.3    Praszkier, J.4    Cavaliere, R.5
  • 24
    • 84856407458 scopus 로고    scopus 로고
    • A novel extracellular metallopeptidase domain shared by animal host-associated mutualistic and pathogenic microbes
    • Nakjang S, Ndeh DA, Wipat A, Bolam DN, Hirt RP, (2012) A novel extracellular metallopeptidase domain shared by animal host-associated mutualistic and pathogenic microbes. PLoS One 7: e30287.
    • (2012) PLoS One , vol.7
    • Nakjang, S.1    Ndeh, D.A.2    Wipat, A.3    Bolam, D.N.4    Hirt, R.P.5
  • 25
    • 0026082664 scopus 로고
    • ToxR regulates the production of lipoproteins and the expression of serum resistance in Vibrio cholerae
    • Parsot C, Taxman E, Mekalanos JJ, (1991) ToxR regulates the production of lipoproteins and the expression of serum resistance in Vibrio cholerae. Proc Natl Acad Sci U S A 88: 1641-1645.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 1641-1645
    • Parsot, C.1    Taxman, E.2    Mekalanos, J.J.3
  • 27
    • 33845929576 scopus 로고    scopus 로고
    • Transcriptional regulation of the yghJ-pppA-yghG-gspCDEFGHIJKLM cluster, encoding the type II secretion pathway in enterotoxigenic Escherichia coli
    • Yang J, Baldi DL, Tauschek M, Strugnell RA, Robins-Browne RM, (2007) Transcriptional regulation of the yghJ-pppA-yghG-gspCDEFGHIJKLM cluster, encoding the type II secretion pathway in enterotoxigenic Escherichia coli. J Bacteriol 189: 142-150.
    • (2007) J Bacteriol , vol.189 , pp. 142-150
    • Yang, J.1    Baldi, D.L.2    Tauschek, M.3    Strugnell, R.A.4    Robins-Browne, R.M.5
  • 29
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • Frickey T, Lupas A, (2004) CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics 20: 3702-3704.
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 30
    • 84355166675 scopus 로고    scopus 로고
    • Imaging proteins inside cells with fluorescent tags
    • Crivat G, Taraska JW, (2012) Imaging proteins inside cells with fluorescent tags. Trends Biotechnol 30: 8-16.
    • (2012) Trends Biotechnol , vol.30 , pp. 8-16
    • Crivat, G.1    Taraska, J.W.2
  • 31
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout I, Chami M, Engel A, Pugsley AP, Bayan N, (2006) Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J 25: 5241-5249.
    • (2006) EMBO J , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 32
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: a protein secretion system for all seasons
    • Cianciotto NP, (2005) Type II secretion: a protein secretion system for all seasons. Trends Microbiol 13: 581-588.
    • (2005) Trends Microbiol , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 33
    • 50049114967 scopus 로고    scopus 로고
    • A new way out: protein localization on the bacterial cell surface via Tat and a novel Type II secretion system
    • Coulthurst SJ, Palmer T, (2008) A new way out: protein localization on the bacterial cell surface via Tat and a novel Type II secretion system. Mol Microbiol 69: 1331-1335.
    • (2008) Mol Microbiol , vol.69 , pp. 1331-1335
    • Coulthurst, S.J.1    Palmer, T.2
  • 34
    • 71749120639 scopus 로고    scopus 로고
    • HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
    • Viarre V, Cascales E, Ball G, Michel GP, Filloux A, et al. (2009) HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J Biol Chem 284: 33815-33823.
    • (2009) J Biol Chem , vol.284 , pp. 33815-33823
    • Viarre, V.1    Cascales, E.2    Ball, G.3    Michel, G.P.4    Filloux, A.5
  • 35
    • 84864824663 scopus 로고    scopus 로고
    • YghG (GspSbeta) is a novel pilot protein required for localization of the GspDbeta Type II secretion system secretin of enterotoxigenic Escherichia coli
    • Strozen TG, Li G, Howard SP, (2012) YghG (GspSbeta) is a novel pilot protein required for localization of the GspDbeta Type II secretion system secretin of enterotoxigenic Escherichia coli. Infect Immun 80 (8):: 2608-22.
    • (2012) Infect Immun , vol.80 , Issue.8 , pp. 2608-2622
    • Strozen, T.G.1    Li, G.2    Howard, S.P.3
  • 36
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 37
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N, (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-533.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 39
    • 79955540767 scopus 로고    scopus 로고
    • Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species
    • Strozen TG, Stanley H, Gu Y, Boyd J, Bagdasarian M, et al. (2011) Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species. J Bacteriol 193: 2322-2331.
    • (2011) J Bacteriol , vol.193 , pp. 2322-2331
    • Strozen, T.G.1    Stanley, H.2    Gu, Y.3    Boyd, J.4    Bagdasarian, M.5
  • 40
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity
    • Guilvout I, Hardie KR, Sauvonnet N, Pugsley AP, (1999) Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J Bacteriol 181: 7212-7220.
    • (1999) J Bacteriol , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 41
    • 0035957511 scopus 로고    scopus 로고
    • The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi
    • Bouley J, Condemine G, Shevchik VE, (2001) The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi. J Mol Biol 308: 205-219.
    • (2001) J Mol Biol , vol.308 , pp. 205-219
    • Bouley, J.1    Condemine, G.2    Shevchik, V.E.3
  • 42
    • 0028982630 scopus 로고
    • Specificity of the protein secretory apparatus: secretion of the heat-labile enterotoxin B subunit pentamers by different species of gram- bacteria
    • Michel LO, Sandkvist M, Bagdasarian M, (1995) Specificity of the protein secretory apparatus: secretion of the heat-labile enterotoxin B subunit pentamers by different species of gram- bacteria. Gene 152: 41-45.
    • (1995) Gene , vol.152 , pp. 41-45
    • Michel, L.O.1    Sandkvist, M.2    Bagdasarian, M.3
  • 43
    • 77949719676 scopus 로고    scopus 로고
    • Specificity of the type II secretion systems of enterotoxigenic Escherichia coli and Vibrio cholerae for heat-labile enterotoxin and cholera toxin
    • Mudrak B, Kuehn MJ, (2010) Specificity of the type II secretion systems of enterotoxigenic Escherichia coli and Vibrio cholerae for heat-labile enterotoxin and cholera toxin. J Bacteriol 192: 1902-1911.
    • (2010) J Bacteriol , vol.192 , pp. 1902-1911
    • Mudrak, B.1    Kuehn, M.J.2
  • 44
    • 26444506255 scopus 로고    scopus 로고
    • Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca
    • Francetic O, Pugsley AP, (2005) Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca. J Bacteriol 187: 7045-7055.
    • (2005) J Bacteriol , vol.187 , pp. 7045-7055
    • Francetic, O.1    Pugsley, A.P.2
  • 46
    • 0030065420 scopus 로고    scopus 로고
    • A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosa
    • Lu HM, Lory S, (1996) A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosa. EMBO J 15: 429-436.
    • (1996) EMBO J , vol.15 , pp. 429-436
    • Lu, H.M.1    Lory, S.2
  • 47
    • 0031689660 scopus 로고    scopus 로고
    • An ExeAB complex in the type II secretion pathway of Aeromonas hydrophila: effect of ATP-binding cassette mutations on complex formation and function
    • Schoenhofen IC, Stratilo C, Howard SP, (1998) An ExeAB complex in the type II secretion pathway of Aeromonas hydrophila: effect of ATP-binding cassette mutations on complex formation and function. Mol Microbiol 29: 1237-1247.
    • (1998) Mol Microbiol , vol.29 , pp. 1237-1247
    • Schoenhofen, I.C.1    Stratilo, C.2    Howard, S.P.3
  • 48
    • 0033917666 scopus 로고    scopus 로고
    • Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa
    • Voulhoux R, Taupiac MP, Czjzek M, Beaumelle B, Filloux A, (2000) Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa. J Bacteriol 182: 4051-4058.
    • (2000) J Bacteriol , vol.182 , pp. 4051-4058
    • Voulhoux, R.1    Taupiac, M.P.2    Czjzek, M.3    Beaumelle, B.4    Filloux, A.5
  • 49
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 50
    • 0030860064 scopus 로고    scopus 로고
    • Versatile insertion plasmids for targeted genome manipulations in bacteria: isolation, deletion, and rescue of the pathogenicity island LEE of the Escherichia coli O157:H7 genome
    • Posfai G, Koob MD, Kirkpatrick HA, Blattner FR, (1997) Versatile insertion plasmids for targeted genome manipulations in bacteria: isolation, deletion, and rescue of the pathogenicity island LEE of the Escherichia coli O157:H7 genome. J Bacteriol 179: 4426-4428.
    • (1997) J Bacteriol , vol.179 , pp. 4426-4428
    • Posfai, G.1    Koob, M.D.2    Kirkpatrick, H.A.3    Blattner, F.R.4
  • 51
    • 84865523255 scopus 로고    scopus 로고
    • Dynamic Association of BAM Complex Modules Includes Surface Exposure of the Lipoprotein BamC
    • Webb CT, Selkrig J, Perry AJ, Noinaj N, Buchanan SK, et al. (2012) Dynamic Association of BAM Complex Modules Includes Surface Exposure of the Lipoprotein BamC. J Mol Biol 422: 545-555.
    • (2012) J Mol Biol , vol.422 , pp. 545-555
    • Webb, C.T.1    Selkrig, J.2    Perry, A.J.3    Noinaj, N.4    Buchanan, S.K.5
  • 53
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 54
    • 77952988108 scopus 로고    scopus 로고
    • A new generation of homology search tools based on probabilistic inference
    • Eddy SR, (2009) A new generation of homology search tools based on probabilistic inference. Genome Inform 23: 205-211.
    • (2009) Genome Inform , vol.23 , pp. 205-211
    • Eddy, S.R.1
  • 55
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: interactive sequence similarity searching
    • Finn RD, Clements J, Eddy SR, (2011) HMMER web server: interactive sequence similarity searching. Nucleic Acids Res 39: W29-37.
    • (2011) Nucleic Acids Res , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 57
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 58
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J, (2000) Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17: 540-552.
    • (2000) Mol Biol Evol , vol.17 , pp. 540-552
    • Castresana, J.1
  • 59
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • Gouy M, Guindon S, Gascuel O, (2010) SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol Biol Evol 27: 221-224.
    • (2010) Mol Biol Evol , vol.27 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 60
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O, (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52: 696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 63
    • 26444492139 scopus 로고    scopus 로고
    • Protein production and crystallization at the joint center for structural genomics
    • Lesley SA, Wilson IA, (2005) Protein production and crystallization at the joint center for structural genomics. J Struct Funct Genomics 6: 71-79.
    • (2005) J Struct Funct Genomics , vol.6 , pp. 71-79
    • Lesley, S.A.1    Wilson, I.A.2
  • 64
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 66
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams JP, Leslie AG, (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr D Biol Crystallogr 52: 30-42.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 67
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A, (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3: 1171-1179.
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 68
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 70
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J, Merritt EA, (2006) TLSMD web server for the generation of multi-group TLS models. Journal of Applied Crystallography 39: 109-111.
    • (2006) Journal of Applied Crystallography , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 72
    • 61449113235 scopus 로고    scopus 로고
    • Secretion of flagellin by the LEE-encoded type III secretion system of enteropathogenic Escherichia coli
    • Badea L, Beatson SA, Kaparakis M, Ferrero RL, Hartland EL, (2009) Secretion of flagellin by the LEE-encoded type III secretion system of enteropathogenic Escherichia coli. BMC Microbiol 9: 30.
    • (2009) BMC Microbiol , vol.9 , pp. 30
    • Badea, L.1    Beatson, S.A.2    Kaparakis, M.3    Ferrero, R.L.4    Hartland, E.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.