메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

In-Silico Structural and Functional Characterization of a V. cholerae O395 Hypothetical Protein Containing a PDZ1 and an Uncommon Protease Domain

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PEPTIDE HYDROLASE;

EID: 84874160175     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056725     Document Type: Article
Times cited : (8)

References (78)
  • 2
    • 17144462135 scopus 로고    scopus 로고
    • DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae
    • Heidelberg JF, Eisen JA, Nelson WC, Clayton RA, Gwinn ML, et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406: 477-483.
    • (2000) Nature , vol.406 , pp. 477-483
    • Heidelberg, J.F.1    Eisen, J.A.2    Nelson, W.C.3    Clayton, R.A.4    Gwinn, M.L.5
  • 3
    • 0030901705 scopus 로고    scopus 로고
    • Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution
    • Hacker J, Blum-Oehler G, Muhldorfer I, Tschape H, (1997) Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution. Mol Microbiol 23: 1089-1097.
    • (1997) Mol Microbiol , vol.23 , pp. 1089-1097
    • Hacker, J.1    Blum-Oehler, G.2    Muhldorfer, I.3    Tschape, H.4
  • 5
    • 0033758756 scopus 로고    scopus 로고
    • Pathogenicity islands and the evolution of microbes
    • Hacker J, Kaper JB, (2000) Pathogenicity islands and the evolution of microbes. Annu Rev Microbiol 54: 641-679.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 641-679
    • Hacker, J.1    Kaper, J.B.2
  • 6
    • 0030057090 scopus 로고    scopus 로고
    • Lysogenic conversion by a filamentous phage encoding cholera toxin
    • Waldor MK, Mekalanos JJ, (1996) Lysogenic conversion by a filamentous phage encoding cholera toxin. Science 272: 1910-1914.
    • (1996) Science , vol.272 , pp. 1910-1914
    • Waldor, M.K.1    Mekalanos, J.J.2
  • 7
    • 0033609358 scopus 로고    scopus 로고
    • A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria
    • Karaolis DK, Somara S, Maneval DR Jr, Johnson JA, Kaper JB, (1999) A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria. Nature 399: 375-379.
    • (1999) Nature , vol.399 , pp. 375-379
    • Karaolis, D.K.1    Somara, S.2    Maneval Jr., D.R.3    Johnson, J.A.4    Kaper, J.B.5
  • 8
    • 0021139224 scopus 로고
    • Recombinant nontoxinogenic Vibrio cholerae strains as attenuated cholera vaccine candidates
    • Kaper JB, Lockman H, Baldini MM, Levine MM, (1984) Recombinant nontoxinogenic Vibrio cholerae strains as attenuated cholera vaccine candidates. Nature 308: 655-658.
    • (1984) Nature , vol.308 , pp. 655-658
    • Kaper, J.B.1    Lockman, H.2    Baldini, M.M.3    Levine, M.M.4
  • 9
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: triage by chaperones and proteases
    • Gottesman S, Wickner S, Maurizi MR, (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 10
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S, (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 11
    • 25844494542 scopus 로고    scopus 로고
    • Sick chaperones, cellular stress, and disease
    • Macario AJ, Conway de Macario E, (2005) Sick chaperones, cellular stress, and disease. N Engl J Med 353: 1489-1501.
    • (2005) N Engl J Med , vol.353 , pp. 1489-1501
    • Macario, A.J.1    Conway de Macario, E.2
  • 12
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ, (2003) Folding proteins in fatal ways. Nature 426: 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 13
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: implications for protein composition and cell fate
    • Clausen T, Southan C, Ehrmann M, (2002) The HtrA family of proteases: implications for protein composition and cell fate. Mol Cell 10: 443-455.
    • (2002) Mol Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 14
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen MJ, Wren BW, (1997) The HtrA family of serine proteases. Mol Microbiol 26: 209-221.
    • (1997) Mol Microbiol , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 16
    • 84874147843 scopus 로고    scopus 로고
    • Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response
    • Hansen G, Hilgenfeld R, (2012) Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response. Cell Mol Life Sci.
    • (2012) Cell Mol Life Sci
    • Hansen, G.1    Hilgenfeld, R.2
  • 17
    • 80052235693 scopus 로고    scopus 로고
    • Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope
    • Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, et al. (2011) Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope. J Biol Chem 286: 30680-30690.
    • (2011) J Biol Chem , vol.286 , pp. 30680-30690
    • Sawa, J.1    Malet, H.2    Krojer, T.3    Canellas, F.4    Ehrmann, M.5
  • 18
    • 10744222163 scopus 로고    scopus 로고
    • The extracellular proteome of Bacillus subtilis under secretion stress conditions
    • Antelmann H, Darmon E, Noone D, Veening JW, Westers H, et al. (2003) The extracellular proteome of Bacillus subtilis under secretion stress conditions. Mol Microbiol 49: 143-156.
    • (2003) Mol Microbiol , vol.49 , pp. 143-156
    • Antelmann, H.1    Darmon, E.2    Noone, D.3    Veening, J.W.4    Westers, H.5
  • 19
    • 0036716436 scopus 로고    scopus 로고
    • Role of the htrA gene in Klebsiella pneumoniae virulence
    • Cortes G, de Astorza B, Benedi VJ, Alberti S, (2002) Role of the htrA gene in Klebsiella pneumoniae virulence. Infect Immun 70: 4772-4776.
    • (2002) Infect Immun , vol.70 , pp. 4772-4776
    • Cortes, G.1    de Astorza, B.2    Benedi, V.J.3    Alberti, S.4
  • 20
    • 2542617706 scopus 로고    scopus 로고
    • Role of HtrA in the virulence and competence of Streptococcus pneumoniae
    • Ibrahim YM, Kerr AR, McCluskey J, Mitchell TJ, (2004) Role of HtrA in the virulence and competence of Streptococcus pneumoniae. Infect Immun 72: 3584-3591.
    • (2004) Infect Immun , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1    Kerr, A.R.2    McCluskey, J.3    Mitchell, T.J.4
  • 21
    • 0034868619 scopus 로고    scopus 로고
    • Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
    • Jones CH, Bolken TC, Jones KF, Zeller GO, Hruby DE, (2001) Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes. Infect Immun 69: 5538-5545.
    • (2001) Infect Immun , vol.69 , pp. 5538-5545
    • Jones, C.H.1    Bolken, T.C.2    Jones, K.F.3    Zeller, G.O.4    Hruby, D.E.5
  • 22
    • 64049118038 scopus 로고    scopus 로고
    • Salmonella enterica Serovar Typhimurium HtrA: regulation of expression and role of the chaperone and protease activities during infection
    • Lewis C, Skovierova H, Rowley G, Rezuchova B, Homerova D, et al. (2009) Salmonella enterica Serovar Typhimurium HtrA: regulation of expression and role of the chaperone and protease activities during infection. Microbiology 155: 873-881.
    • (2009) Microbiology , vol.155 , pp. 873-881
    • Lewis, C.1    Skovierova, H.2    Rowley, G.3    Rezuchova, B.4    Homerova, D.5
  • 23
    • 33748561788 scopus 로고    scopus 로고
    • Single, double and triple mutants of Salmonella enterica serovar Typhimurium degP (htrA), degQ (hhoA) and degS (hhoB) have diverse phenotypes on exposure to elevated temperature and their growth in vivo is attenuated to different extents
    • Mo E, Peters SE, Willers C, Maskell DJ, Charles IG, (2006) Single, double and triple mutants of Salmonella enterica serovar Typhimurium degP (htrA), degQ (hhoA) and degS (hhoB) have diverse phenotypes on exposure to elevated temperature and their growth in vivo is attenuated to different extents. Microb Pathog 41: 174-182.
    • (2006) Microb Pathog , vol.41 , pp. 174-182
    • Mo, E.1    Peters, S.E.2    Willers, C.3    Maskell, D.J.4    Charles, I.G.5
  • 24
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio TL, (2005) Envelope stress responses and Gram-negative bacterial pathogenesis. Mol Microbiol 56: 1119-1128.
    • (2005) Mol Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 25
    • 29644445406 scopus 로고    scopus 로고
    • Listeria monocytogenes 10403S HtrA is necessary for resistance to cellular stress and virulence
    • Wilson RL, Brown LL, Kirkwood-Watts D, Warren TK, Lund SA, et al. (2006) Listeria monocytogenes 10403S HtrA is necessary for resistance to cellular stress and virulence. Infect Immun 74: 765-768.
    • (2006) Infect Immun , vol.74 , pp. 765-768
    • Wilson, R.L.1    Brown, L.L.2    Kirkwood-Watts, D.3    Warren, T.K.4    Lund, S.A.5
  • 26
    • 54949145378 scopus 로고    scopus 로고
    • Characterization of DegQVh, a serine protease and a protective immunogen from a pathogenic Vibrio harveyi strain
    • Zhang WW, Sun K, Cheng S, Sun L, (2008) Characterization of DegQVh, a serine protease and a protective immunogen from a pathogenic Vibrio harveyi strain. Appl Environ Microbiol 74: 6254-6262.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6254-6262
    • Zhang, W.W.1    Sun, K.2    Cheng, S.3    Sun, L.4
  • 27
    • 42949103095 scopus 로고    scopus 로고
    • On detection and assessment of statistical significance of Genomic Islands
    • Chatterjee R, Chaudhuri K, Chaudhuri P, (2008) On detection and assessment of statistical significance of Genomic Islands. BMC Genomics 9: 150.
    • (2008) BMC Genomics , vol.9 , pp. 150
    • Chatterjee, R.1    Chaudhuri, K.2    Chaudhuri, P.3
  • 28
    • 0242321088 scopus 로고    scopus 로고
    • Pathogenicity islands and phages in Vibrio cholerae evolution
    • Faruque SM, Mekalanos JJ, (2003) Pathogenicity islands and phages in Vibrio cholerae evolution. Trends Microbiol 11: 505-510.
    • (2003) Trends Microbiol , vol.11 , pp. 505-510
    • Faruque, S.M.1    Mekalanos, J.J.2
  • 29
    • 38749125193 scopus 로고    scopus 로고
    • Three pathogenicity islands of Vibrio cholerae can excise from the chromosome and form circular intermediates
    • Murphy RA, Boyd EF, (2008) Three pathogenicity islands of Vibrio cholerae can excise from the chromosome and form circular intermediates. J Bacteriol 190: 636-647.
    • (2008) J Bacteriol , vol.190 , pp. 636-647
    • Murphy, R.A.1    Boyd, E.F.2
  • 30
    • 11044226569 scopus 로고    scopus 로고
    • The Vibrio seventh pandemic island-II is a 26.9 kb genomic island present in Vibrio cholerae El Tor and O139 serogroup isolates that shows homology to a 43.4 kb genomic island in V. vulnificus
    • O'Shea YA, Finnan S, Reen FJ, Morrissey JP, O'Gara F, et al. (2004) The Vibrio seventh pandemic island-II is a 26.9 kb genomic island present in Vibrio cholerae El Tor and O139 serogroup isolates that shows homology to a 43.4 kb genomic island in V. vulnificus. Microbiology 150: 4053-4063.
    • (2004) Microbiology , vol.150 , pp. 4053-4063
    • O'Shea, Y.A.1    Finnan, S.2    Reen, F.J.3    Morrissey, J.P.4    O'Gara, F.5
  • 31
    • 17644389617 scopus 로고    scopus 로고
    • Support vector machine-based method for subcellular localization of human proteins using amino acid compositions, their order, and similarity search
    • Garg A, Bhasin M, Raghava GP, (2005) Support vector machine-based method for subcellular localization of human proteins using amino acid compositions, their order, and similarity search. J Biol Chem 280: 14427-14432.
    • (2005) J Biol Chem , vol.280 , pp. 14427-14432
    • Garg, A.1    Bhasin, M.2    Raghava, G.P.3
  • 32
    • 33746218840 scopus 로고    scopus 로고
    • Prediction of protein subcellular localization
    • Yu CS, Chen YC, Lu CH, Hwang JK, (2006) Prediction of protein subcellular localization. Proteins 64: 643-651.
    • (2006) Proteins , vol.64 , pp. 643-651
    • Yu, C.S.1    Chen, Y.C.2    Lu, C.H.3    Hwang, J.K.4
  • 33
    • 1942505330 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions
    • Yu CS, Lin CJ, Hwang JK, (2004) Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions. Protein Sci 13: 1402-1406.
    • (2004) Protein Sci , vol.13 , pp. 1402-1406
    • Yu, C.S.1    Lin, C.J.2    Hwang, J.K.3
  • 34
    • 0034843744 scopus 로고    scopus 로고
    • Support vector machine approach for protein subcellular localization prediction
    • Hua S, Sun Z, (2001) Support vector machine approach for protein subcellular localization prediction. Bioinformatics 17: 721-728.
    • (2001) Bioinformatics , vol.17 , pp. 721-728
    • Hua, S.1    Sun, Z.2
  • 35
    • 0043123167 scopus 로고    scopus 로고
    • Tools for comparative protein structure modeling and analysis
    • Eswar N, John B, Mirkovic N, Fiser A, Ilyin VA, et al. (2003) Tools for comparative protein structure modeling and analysis. Nucleic Acids Res 31: 3375-3380.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3375-3380
    • Eswar, N.1    John, B.2    Mirkovic, N.3    Fiser, A.4    Ilyin, V.A.5
  • 36
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 37
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen MY, Sali A, (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15: 2507-2524.
    • (2006) Protein Sci , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 39
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N, Peitsch MC, (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 41
    • 78349284741 scopus 로고    scopus 로고
    • Protein loop modeling by using fragment assembly and analytical loop closure
    • Lee J, Lee D, Park H, Coutsias EA, Seok C, (2010) Protein loop modeling by using fragment assembly and analytical loop closure. Proteins 78: 3428-3436.
    • (2010) Proteins , vol.78 , pp. 3428-3436
    • Lee, J.1    Lee, D.2    Park, H.3    Coutsias, E.A.4    Seok, C.5
  • 42
    • 0000243829 scopus 로고
    • PROCHECK - a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK- a program to check the stereochemical quality of protein structures. J App Cryst 26: 283-291.
    • (1993) J App Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: a protein structure alignment algorithm based on the TM-score
    • Zhang Y, Skolnick J, (2005) TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res 33: 2302-2309.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 44
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar Fourier correlations
    • Ritchie DW, Kemp GJ, (2000) Protein docking using spherical polar Fourier correlations. Proteins 39: 178-194.
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.2
  • 45
    • 50149107174 scopus 로고    scopus 로고
    • Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
    • Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, et al. (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc Natl Acad Sci U S A 105: 11939-11944.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11939-11944
    • Jiang, J.1    Zhang, X.2    Chen, Y.3    Wu, Y.4    Zhou, Z.H.5
  • 46
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T, (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416: 455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 47
    • 77954384306 scopus 로고    scopus 로고
    • HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
    • Krojer T, Sawa J, Huber R, Clausen T, (2010) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat Struct Mol Biol 17: 844-852.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 844-852
    • Krojer, T.1    Sawa, J.2    Huber, R.3    Clausen, T.4
  • 48
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer T, Sawa J, Schafer E, Saibil HR, Ehrmann M, et al. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453: 885-890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5
  • 49
    • 35348985928 scopus 로고    scopus 로고
    • Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress
    • Hasselblatt H, Kurzbauer R, Wilken C, Krojer T, Sawa J, et al. (2007) Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress. Genes Dev 21: 2659-2670.
    • (2007) Genes Dev , vol.21 , pp. 2659-2670
    • Hasselblatt, H.1    Kurzbauer, R.2    Wilken, C.3    Krojer, T.4    Sawa, J.5
  • 50
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT, (2003) OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113: 61-71.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 51
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T, (2004) Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease. Cell 117: 483-494.
    • (2004) Cell , vol.117 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 52
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H, (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 53
    • 23044468282 scopus 로고    scopus 로고
    • Nuclear speckles and nucleoli targeting by PIP2-PDZ domain interactions
    • Mortier E, Wuytens G, Leenaerts I, Hannes F, Heung MY, et al. (2005) Nuclear speckles and nucleoli targeting by PIP2-PDZ domain interactions. Embo J 24: 2556-2565.
    • (2005) Embo J , vol.24 , pp. 2556-2565
    • Mortier, E.1    Wuytens, G.2    Leenaerts, I.3    Hannes, F.4    Heung, M.Y.5
  • 54
    • 35648957794 scopus 로고    scopus 로고
    • Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes
    • Pan L, Wu H, Shen C, Shi Y, Jin W, et al. (2007) Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes. Embo J 26: 4576-4587.
    • (2007) Embo J , vol.26 , pp. 4576-4587
    • Pan, L.1    Wu, H.2    Shen, C.3    Shi, Y.4    Jin, W.5
  • 55
    • 28644434920 scopus 로고    scopus 로고
    • Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin
    • Yan J, Wen W, Xu W, Long JF, Adams ME, et al. (2005) Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin. Embo J 24: 3985-3995.
    • (2005) Embo J , vol.24 , pp. 3985-3995
    • Yan, J.1    Wen, W.2    Xu, W.3    Long, J.F.4    Adams, M.E.5
  • 56
    • 0036289460 scopus 로고    scopus 로고
    • PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane
    • Zimmermann P, Meerschaert K, Reekmans G, Leenaerts I, Small JV, et al. (2002) PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane. Mol Cell 9: 1215-1225.
    • (2002) Mol Cell , vol.9 , pp. 1215-1225
    • Zimmermann, P.1    Meerschaert, K.2    Reekmans, G.3    Leenaerts, I.4    Small, J.V.5
  • 58
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • Pils B, Schultz J, (2004) Inactive enzyme-homologues find new function in regulatory processes. J Mol Biol 340: 399-404.
    • (2004) J Mol Biol , vol.340 , pp. 399-404
    • Pils, B.1    Schultz, J.2
  • 59
    • 79960601819 scopus 로고    scopus 로고
    • The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies
    • Wrase R, Scott H, Hilgenfeld R, Hansen G, (2011) The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies. Proc Natl Acad Sci U S A 108: 10490-10495.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 10490-10495
    • Wrase, R.1    Scott, H.2    Hilgenfeld, R.3    Hansen, G.4
  • 60
    • 56749154097 scopus 로고    scopus 로고
    • Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration
    • Ekici OD, Paetzel M, Dalbey RE, (2008) Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci 17: 2023-2037.
    • (2008) Protein Sci , vol.17 , pp. 2023-2037
    • Ekici, O.D.1    Paetzel, M.2    Dalbey, R.E.3
  • 61
    • 0026697771 scopus 로고
    • Effects of site-directed mutations on processing and activities of penicillin G acylase from Escherichia coli ATCC 11105
    • Choi KS, Kim JA, Kang HS, (1992) Effects of site-directed mutations on processing and activities of penicillin G acylase from Escherichia coli ATCC 11105. J Bacteriol 174: 6270-6276.
    • (1992) J Bacteriol , vol.174 , pp. 6270-6276
    • Choi, K.S.1    Kim, J.A.2    Kang, H.S.3
  • 62
    • 0034730417 scopus 로고    scopus 로고
    • Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft
    • Hewitt L, Kasche V, Lummer K, Lewis RJ, Murshudov GN, et al. (2000) Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft. J Mol Biol 302: 887-898.
    • (2000) J Mol Biol , vol.302 , pp. 887-898
    • Hewitt, L.1    Kasche, V.2    Lummer, K.3    Lewis, R.J.4    Murshudov, G.N.5
  • 63
    • 0037169550 scopus 로고    scopus 로고
    • Precursor structure of cephalosporin acylase. Insights into autoproteolytic activation in a new N-terminal hydrolase family
    • Kim Y, Kim S, Earnest TN, Hol WG, (2002) Precursor structure of cephalosporin acylase. Insights into autoproteolytic activation in a new N-terminal hydrolase family. J Biol Chem 277: 2823-2829.
    • (2002) J Biol Chem , vol.277 , pp. 2823-2829
    • Kim, Y.1    Kim, S.2    Earnest, T.N.3    Hol, W.G.4
  • 65
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 66
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, et al. (2005) Protein database searches using compositionally adjusted substitution matrices. Febs J 272: 5101-5109.
    • (2005) Febs J , vol.272 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3    Agarwala, R.4    Morgulis, A.5
  • 67
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC, (2003) SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 68
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0-remote homology modeling using structure-guided sequence profiles
    • Nielsen M, Lundegaard C, Lund O, Petersen TN, (2010) CPHmodels-3.0-remote homology modeling using structure-guided sequence profiles. Nucleic Acids Res 38: W576-581.
    • (2010) Nucleic Acids Res , vol.38
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 69
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ, (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Suppl 5: 39-46.
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 71
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: automatic comparative molecular modelling of protein
    • Combet C, Jambon M, Deleage G, Geourjon C, (2002) Geno3D: automatic comparative molecular modelling of protein. Bioinformatics 18: 213-214.
    • (2002) Bioinformatics , vol.18 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deleage, G.3    Geourjon, C.4
  • 72
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J, (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21: 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 73
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 74
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K, (2001) FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310: 243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 75
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J, (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 76
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar RC, (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 77
    • 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
  • 78
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RK, Sali A, (2000) Modeling of loops in protein structures. Protein Sci 9: 1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.