메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Collagen-like proteins in pathogenic E. coli strains

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COLLAGEN LIKE PROTEIN; FIBRILLAR COLLAGEN; ISOLEUCINE; LEUCINE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VALINE; SHIGA TOXIN;

EID: 84862021997     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037872     Document Type: Article
Times cited : (36)

References (88)
  • 1
    • 78049291873 scopus 로고    scopus 로고
    • Escherichia coli O157
    • Pennington H, (2010) Escherichia coli O157. Lancet 376: 1428-1435.
    • (2010) Lancet , vol.376 , pp. 1428-1435
    • Pennington, H.1
  • 2
    • 73949159257 scopus 로고    scopus 로고
    • Verocytotoxin-producing Escherichia coli (VTEC)
    • Karmali MA, Gannon V, Sargeant JM, (2010) Verocytotoxin-producing Escherichia coli (VTEC). Vet Microbiol 140: 360-370.
    • (2010) Vet Microbiol , vol.140 , pp. 360-370
    • Karmali, M.A.1    Gannon, V.2    Sargeant, J.M.3
  • 3
    • 75849118571 scopus 로고    scopus 로고
    • A brief overview of Escherichia coli O157:H7 and its plasmid O157
    • Lim JY, Yoon J, Hovde CJ, (2010) A brief overview of Escherichia coli O157:H7 and its plasmid O157. J Microbiol Biotechnol 20: 5-14.
    • (2010) J Microbiol Biotechnol , vol.20 , pp. 5-14
    • Lim, J.Y.1    Yoon, J.2    Hovde, C.J.3
  • 4
    • 0035945586 scopus 로고    scopus 로고
    • Genome sequence of enterohaemorrhagic Escherichia coli O157:H7
    • Perna NT, Plunkett G, 3rd, Burland V, Mau B, Glasner JD, et al. (2001) Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature 409: 529-533.
    • (2001) Nature , vol.409 , pp. 529-533
    • Perna, N.T.1    Plunkett 3rd, G.2    Burland, V.3    Mau, B.4    Glasner, J.D.5
  • 5
    • 0035961748 scopus 로고    scopus 로고
    • Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12
    • Hayashi T, Makino K, Ohnishi M, Kurokawa K, Ishii K, et al. (2001) Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12. DNA Res 8: 11-22.
    • (2001) DNA Res , vol.8 , pp. 11-22
    • Hayashi, T.1    Makino, K.2    Ohnishi, M.3    Kurokawa, K.4    Ishii, K.5
  • 6
    • 0035477452 scopus 로고    scopus 로고
    • Diversification of Escherichia coli genomes: are bacteriophages the major contributors?
    • Ohnishi M, Kurokawa K, Hayashi T, (2001) Diversification of Escherichia coli genomes: are bacteriophages the major contributors? Trends Microbiol 9: 481-485.
    • (2001) Trends Microbiol , vol.9 , pp. 481-485
    • Ohnishi, M.1    Kurokawa, K.2    Hayashi, T.3
  • 7
    • 14244251962 scopus 로고    scopus 로고
    • Evolution of genomic content in the stepwise emergence of Escherichia coli O157:H7
    • Wick LM, Qi W, Lacher DW, Whittam TS, (2005) Evolution of genomic content in the stepwise emergence of Escherichia coli O157:H7. J Bacteriol 187: 1783-1791.
    • (2005) J Bacteriol , vol.187 , pp. 1783-1791
    • Wick, L.M.1    Qi, W.2    Lacher, D.W.3    Whittam, T.S.4
  • 8
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins-from cell biology to biomedical applications
    • Johannes L, Romer W, (2010) Shiga toxins-from cell biology to biomedical applications. Nat Rev Microbiol 8: 105-116.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 105-116
    • Johannes, L.1    Romer, W.2
  • 9
    • 33749515943 scopus 로고    scopus 로고
    • An extensive repertoire of type III secretion effectors in Escherichia coli O157 and the role of lambdoid phages in their dissemination
    • Tobe T, Beatson SA, Taniguchi H, Abe H, Bailey CM, et al. (2006) An extensive repertoire of type III secretion effectors in Escherichia coli O157 and the role of lambdoid phages in their dissemination. Proc Natl Acad Sci U S A 103: 14941-14946.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14941-14946
    • Tobe, T.1    Beatson, S.A.2    Taniguchi, H.3    Abe, H.4    Bailey, C.M.5
  • 10
    • 70449568272 scopus 로고    scopus 로고
    • Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli
    • Ogura Y, Ooka T, Iguchi A, Toh H, Asadulghani M, et al. (2009) Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli. Proc Natl Acad Sci U S A 106: 17939-17944.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17939-17944
    • Ogura, Y.1    Ooka, T.2    Iguchi, A.3    Toh, H.4    Asadulghani, M.5
  • 11
    • 0031777043 scopus 로고    scopus 로고
    • Genotypic and phenotypic changes in the emergence of Escherichia coli O157:H7
    • Feng P, Lampel KA, Karch H, Whittam TS, (1998) Genotypic and phenotypic changes in the emergence of Escherichia coli O157:H7. J Infect Dis 177: 1750-1753.
    • (1998) J Infect Dis , vol.177 , pp. 1750-1753
    • Feng, P.1    Lampel, K.A.2    Karch, H.3    Whittam, T.S.4
  • 12
    • 4844229225 scopus 로고    scopus 로고
    • Diversity of stx2 converting bacteriophages induced from Shiga-toxin-producing Escherichia coli strains isolated from cattle
    • Muniesa M, Blanco JE, De Simon M, Serra-Moreno R, Blanch AR, et al. (2004) Diversity of stx2 converting bacteriophages induced from Shiga-toxin-producing Escherichia coli strains isolated from cattle. Microbiology 150: 2959-2971.
    • (2004) Microbiology , vol.150 , pp. 2959-2971
    • Muniesa, M.1    Blanco, J.E.2    de Simon, M.3    Serra-Moreno, R.4    Blanch, A.R.5
  • 13
    • 33744922108 scopus 로고    scopus 로고
    • Complexity of the genomic diversity in enterohemorrhagic Escherichia coli O157 revealed by the combinational use of the O157 Sakai OligoDNA microarray and the Whole Genome PCR scanning
    • Ogura Y, Kurokawa K, Ooka T, Tashiro K, Tobe T, et al. (2006) Complexity of the genomic diversity in enterohemorrhagic Escherichia coli O157 revealed by the combinational use of the O157 Sakai OligoDNA microarray and the Whole Genome PCR scanning. DNA Res 13: 3-14.
    • (2006) DNA Res , vol.13 , pp. 3-14
    • Ogura, Y.1    Kurokawa, K.2    Ooka, T.3    Tashiro, K.4    Tobe, T.5
  • 15
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran GN, Kartha G, (1955) Structure of collagen. Nature 176: 593-595.
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 16
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich A, Crick FH, (1961) The molecular structure of collagen. J Mol Biol 3: 483-506.
    • (1961) J Mol Biol , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.2
  • 17
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella J, Eaton M, Brodsky B, Berman HM, (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science 266: 75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 18
    • 17444415358 scopus 로고    scopus 로고
    • Molecular structure of the collagen triple helix
    • Brodsky B, Persikov AV, (2005) Molecular structure of the collagen triple helix. Adv Protein Chem 70: 301-339.
    • (2005) Adv Protein Chem , vol.70 , pp. 301-339
    • Brodsky, B.1    Persikov, A.V.2
  • 19
    • 0025374159 scopus 로고
    • Capsomer proteins of bacteriophage PRD1, a bacterial virus with a membrane
    • Bamford JK, Bamford DH, (1990) Capsomer proteins of bacteriophage PRD1, a bacterial virus with a membrane. Virology 177: 445-451.
    • (1990) Virology , vol.177 , pp. 445-451
    • Bamford, J.K.1    Bamford, D.H.2
  • 21
    • 0042357053 scopus 로고    scopus 로고
    • Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins
    • Rasmussen M, Jacobsson M, Bjorck L, (2003) Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins. J Biol Chem 278: 32313-32316.
    • (2003) J Biol Chem , vol.278 , pp. 32313-32316
    • Rasmussen, M.1    Jacobsson, M.2    Bjorck, L.3
  • 22
    • 0037178812 scopus 로고    scopus 로고
    • Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices
    • Xu Y, Keene DR, Bujnicki JM, Hook M, Lukomski S, (2002) Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices. J Biol Chem 277: 27312-27318.
    • (2002) J Biol Chem , vol.277 , pp. 27312-27318
    • Xu, Y.1    Keene, D.R.2    Bujnicki, J.M.3    Hook, M.4    Lukomski, S.5
  • 23
    • 22544432231 scopus 로고    scopus 로고
    • Orientation within the exosporium and structural stability of the collagen-like glycoprotein BclA of Bacillus anthracis
    • Boydston JA, Chen P, Steichen CT, Turnbough CL Jr, (2005) Orientation within the exosporium and structural stability of the collagen-like glycoprotein BclA of Bacillus anthracis. J Bacteriol 187: 5310-5317.
    • (2005) J Bacteriol , vol.187 , pp. 5310-5317
    • Boydston, J.A.1    Chen, P.2    Steichen, C.T.3    Turnbough Jr., C.L.4
  • 24
    • 0036042515 scopus 로고    scopus 로고
    • A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium
    • Sylvestre P, Couture-Tosi E, Mock M, (2002) A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol Microbiol 45: 169-178.
    • (2002) Mol Microbiol , vol.45 , pp. 169-178
    • Sylvestre, P.1    Couture-Tosi, E.2    Mock, M.3
  • 25
    • 39449109358 scopus 로고    scopus 로고
    • The integrin Mac-1 (CR3) mediates internalization and directs Bacillus anthracis spores into professional phagocytes
    • Oliva CR, Swiecki MK, Griguer CE, Lisanby MW, Bullard DC, et al. (2008) The integrin Mac-1 (CR3) mediates internalization and directs Bacillus anthracis spores into professional phagocytes. Proc Natl Acad Sci U S A 105: 1261-1266.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 1261-1266
    • Oliva, C.R.1    Swiecki, M.K.2    Griguer, C.E.3    Lisanby, M.W.4    Bullard, D.C.5
  • 26
    • 17144397160 scopus 로고    scopus 로고
    • A streptococcal collagen-like protein interacts with the alpha2beta1 integrin and induces intracellular signaling
    • Humtsoe JO, Kim JK, Xu Y, Keene DR, Hook M, et al. (2005) A streptococcal collagen-like protein interacts with the alpha2beta1 integrin and induces intracellular signaling. J Biol Chem 280: 13848-13857.
    • (2005) J Biol Chem , vol.280 , pp. 13848-13857
    • Humtsoe, J.O.1    Kim, J.K.2    Xu, Y.3    Keene, D.R.4    Hook, M.5
  • 27
    • 74349093820 scopus 로고    scopus 로고
    • Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells
    • Caswell CC, Oliver-Kozup H, Han R, Lukomska E, Lukomski S, (2010) Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells. FEMS Microbiol Lett 303: 61-68.
    • (2010) FEMS Microbiol Lett , vol.303 , pp. 61-68
    • Caswell, C.C.1    Oliver-Kozup, H.2    Han, R.3    Lukomska, E.4    Lukomski, S.5
  • 28
    • 78650072871 scopus 로고    scopus 로고
    • Streptococcal collagen-like surface protein 1 promotes adhesion to the respiratory epithelial cell
    • Chen SM, Tsai YS, Wu CM, Liao SK, Wu LC, et al. (2010) Streptococcal collagen-like surface protein 1 promotes adhesion to the respiratory epithelial cell. BMC Microbiol 10: 320.
    • (2010) BMC Microbiol , vol.10 , pp. 320
    • Chen, S.M.1    Tsai, Y.S.2    Wu, C.M.3    Liao, S.K.4    Wu, L.C.5
  • 29
    • 14744279815 scopus 로고    scopus 로고
    • Global expression of prophage genes in Escherichia coli O157:H7 strain EDL933 in response to norfloxacin
    • Herold S, Siebert J, Huber A, Schmidt H, (2005) Global expression of prophage genes in Escherichia coli O157:H7 strain EDL933 in response to norfloxacin. Antimicrob Agents Chemother 49: 931-944.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 931-944
    • Herold, S.1    Siebert, J.2    Huber, A.3    Schmidt, H.4
  • 30
    • 39049116054 scopus 로고    scopus 로고
    • Global transcriptional response of Escherichia coli O157:H7 to growth transitions in glucose minimal medium
    • Bergholz TM, Wick LM, Qi W, Riordan JT, Ouellette LM, et al. (2007) Global transcriptional response of Escherichia coli O157:H7 to growth transitions in glucose minimal medium. BMC Microbiol 7: 97.
    • (2007) BMC Microbiol , vol.7 , pp. 97
    • Bergholz, T.M.1    Wick, L.M.2    Qi, W.3    Riordan, J.T.4    Ouellette, L.M.5
  • 31
    • 34447519333 scopus 로고    scopus 로고
    • Enterohemorrhagic Escherichia coli biofilms are inhibited by 7-hydroxyindole and stimulated by isatin
    • Lee J, Bansal T, Jayaraman A, Bentley WE, Wood TK, (2007) Enterohemorrhagic Escherichia coli biofilms are inhibited by 7-hydroxyindole and stimulated by isatin. Appl Environ Microbiol 73: 4100-4109.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4100-4109
    • Lee, J.1    Bansal, T.2    Jayaraman, A.3    Bentley, W.E.4    Wood, T.K.5
  • 32
    • 34548500624 scopus 로고    scopus 로고
    • Differential effects of epinephrine, norepinephrine, and indole on Escherichia coli O157:H7 chemotaxis, colonization, and gene expression
    • Bansal T, Englert D, Lee J, Hegde M, Wood TK, et al. (2007) Differential effects of epinephrine, norepinephrine, and indole on Escherichia coli O157:H7 chemotaxis, colonization, and gene expression. Infect Immun 75: 4597-4607.
    • (2007) Infect Immun , vol.75 , pp. 4597-4607
    • Bansal, T.1    Englert, D.2    Lee, J.3    Hegde, M.4    Wood, T.K.5
  • 33
    • 77956593339 scopus 로고    scopus 로고
    • Quantification of Shiga toxin-converting bacteriophages in wastewater and in fecal samples by real-time quantitative PCR
    • Imamovic L, Balleste E, Jofre J, Muniesa M, (2010) Quantification of Shiga toxin-converting bacteriophages in wastewater and in fecal samples by real-time quantitative PCR. Appl Environ Microbiol 76: 5693-5701.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5693-5701
    • Imamovic, L.1    Balleste, E.2    Jofre, J.3    Muniesa, M.4
  • 34
    • 67249140993 scopus 로고    scopus 로고
    • The defective prophage pool of Escherichia coli O157: prophage-prophage interactions potentiate horizontal transfer of virulence determinants
    • Asadulghani M, Ogura Y, Ooka T, Itoh T, Sawaguchi A, et al. (2009) The defective prophage pool of Escherichia coli O157: prophage-prophage interactions potentiate horizontal transfer of virulence determinants. PLoS Pathog 5: e1000408.
    • (2009) PLoS Pathog , vol.5
    • Asadulghani, M.1    Ogura, Y.2    Ooka, T.3    Itoh, T.4    Sawaguchi, A.5
  • 35
    • 0026589426 scopus 로고
    • DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages
    • Haggard-Ljungquist E, Halling C, Calendar R, (1992) DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages. J Bacteriol 174: 1462-1477.
    • (1992) J Bacteriol , vol.174 , pp. 1462-1477
    • Haggard-Ljungquist, E.1    Halling, C.2    Calendar, R.3
  • 36
    • 0026463890 scopus 로고
    • Bacteriophage lambda PaPa: not the mother of all lambda phages
    • Hendrix RW, Duda RL, (1992) Bacteriophage lambda PaPa: not the mother of all lambda phages. Science 258: 1145-1148.
    • (1992) Science , vol.258 , pp. 1145-1148
    • Hendrix, R.W.1    Duda, R.L.2
  • 37
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides
    • Ramshaw JA, Shah NK, Brodsky B, (1998) Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J Struct Biol 122: 86-91.
    • (1998) J Struct Biol , vol.122 , pp. 86-91
    • Ramshaw, J.A.1    Shah, N.K.2    Brodsky, B.3
  • 38
    • 77951975886 scopus 로고    scopus 로고
    • A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence
    • Bella J, (2010) A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence. J Struct Biol 170: 377-391.
    • (2010) J Struct Biol , vol.170 , pp. 377-391
    • Bella, J.1
  • 39
    • 0033793665 scopus 로고    scopus 로고
    • SclA, a novel collagen-like surface protein of Streptococcus pyogenes
    • Rasmussen M, Eden A, Bjorck L, (2000) SclA, a novel collagen-like surface protein of Streptococcus pyogenes. Infect Immun 68: 6370-6377.
    • (2000) Infect Immun , vol.68 , pp. 6370-6377
    • Rasmussen, M.1    Eden, A.2    Bjorck, L.3
  • 40
    • 0034640342 scopus 로고    scopus 로고
    • Sweet is stable: glycosylation stabilizes collagen
    • Bann JG, Peyton DH, Bachinger HP, (2000) Sweet is stable: glycosylation stabilizes collagen. FEBS Lett 473: 237-240.
    • (2000) FEBS Lett , vol.473 , pp. 237-240
    • Bann, J.G.1    Peyton, D.H.2    Bachinger, H.P.3
  • 41
    • 3843062496 scopus 로고    scopus 로고
    • Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium
    • Daubenspeck JM, Zeng H, Chen P, Dong S, Steichen CT, et al. (2004) Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium. J Biol Chem 279: 30945-30953.
    • (2004) J Biol Chem , vol.279 , pp. 30945-30953
    • Daubenspeck, J.M.1    Zeng, H.2    Chen, P.3    Dong, S.4    Steichen, C.T.5
  • 42
    • 35648946905 scopus 로고    scopus 로고
    • Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline
    • Mohs A, Silva T, Yoshida T, Amin R, Lukomski S, et al. (2007) Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline. J Biol Chem 282: 29757-29765.
    • (2007) J Biol Chem , vol.282 , pp. 29757-29765
    • Mohs, A.1    Silva, T.2    Yoshida, T.3    Amin, R.4    Lukomski, S.5
  • 43
    • 34548041437 scopus 로고    scopus 로고
    • Analysis of the kinetics of folding of proteins and peptides using circular dichroism
    • Greenfield NJ, (2006) Analysis of the kinetics of folding of proteins and peptides using circular dichroism. Nat Protoc 1: 2891-2899.
    • (2006) Nat Protoc , vol.1 , pp. 2891-2899
    • Greenfield, N.J.1
  • 44
    • 0027932724 scopus 로고
    • Poly(pro)II helices in globular proteins: identification and circular dichroic analysis
    • Sreerama N, Woody RW, (1994) Poly(pro)II helices in globular proteins: identification and circular dichroic analysis. Biochemistry 33: 10022-10025.
    • (1994) Biochemistry , vol.33 , pp. 10022-10025
    • Sreerama, N.1    Woody, R.W.2
  • 45
    • 0031657823 scopus 로고    scopus 로고
    • Supercoiled protein motifs: the collagen triple-helix and the alpha-helical coiled coil
    • Beck K, Brodsky B, (1998) Supercoiled protein motifs: the collagen triple-helix and the alpha-helical coiled coil. J Struct Biol 122: 17-29.
    • (1998) J Struct Biol , vol.122 , pp. 17-29
    • Beck, K.1    Brodsky, B.2
  • 46
    • 0142211233 scopus 로고    scopus 로고
    • Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily
    • McAlinden A, Smith TA, Sandell LJ, Ficheux D, Parry DA, et al. (2003) Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily. J Biol Chem 278: 42200-42207.
    • (2003) J Biol Chem , vol.278 , pp. 42200-42207
    • McAlinden, A.1    Smith, T.A.2    Sandell, L.J.3    Ficheux, D.4    Parry, D.A.5
  • 47
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg RA, Prockop DJ, (1973) The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem Biophys Res Commun 52: 115-120.
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 48
    • 0015621910 scopus 로고
    • Hydroxyproline stabilizes the triple helix of chick tendon collagen
    • Jimenez S, Harsch M, Rosenbloom J, (1973) Hydroxyproline stabilizes the triple helix of chick tendon collagen. Biochem Biophys Res Commun 52: 106-114.
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 106-114
    • Jimenez, S.1    Harsch, M.2    Rosenbloom, J.3
  • 49
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko KI, (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20: 33-43.
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 51
    • 10344236049 scopus 로고    scopus 로고
    • The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat
    • Kuhnel K, Jarchau T, Wolf E, Schlichting I, Walter U, et al. (2004) The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proc Natl Acad Sci U S A 101: 17027-17032.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17027-17032
    • Kuhnel, K.1    Jarchau, T.2    Wolf, E.3    Schlichting, I.4    Walter, U.5
  • 52
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure
    • Parry DA, Fraser RD, Squire JM, (2008) Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J Struct Biol 163: 258-269.
    • (2008) J Struct Biol , vol.163 , pp. 258-269
    • Parry, D.A.1    Fraser, R.D.2    Squire, J.M.3
  • 53
    • 0023274382 scopus 로고
    • Heterogeneity of Escherichia coli phages encoding Vero cytotoxins: comparison of cloned sequences determining VT1 and VT2 and development of specific gene probes
    • Willshaw GA, Smith HR, Scotland SM, Field AM, Rowe B, (1987) Heterogeneity of Escherichia coli phages encoding Vero cytotoxins: comparison of cloned sequences determining VT1 and VT2 and development of specific gene probes. J Gen Microbiol 133: 1309-1317.
    • (1987) J Gen Microbiol , vol.133 , pp. 1309-1317
    • Willshaw, G.A.1    Smith, H.R.2    Scotland, S.M.3    Field, A.M.4    Rowe, B.5
  • 54
  • 55
    • 0024465413 scopus 로고
    • Comparison of Vero-cytotoxin-encoding phages from Escherichia coli of human and bovine origin
    • Rietra PJ, Willshaw GA, Smith HR, Field AM, Scotland SM, et al. (1989) Comparison of Vero-cytotoxin-encoding phages from Escherichia coli of human and bovine origin. J Gen Microbiol 135: 2307-2318.
    • (1989) J Gen Microbiol , vol.135 , pp. 2307-2318
    • Rietra, P.J.1    Willshaw, G.A.2    Smith, H.R.3    Field, A.M.4    Scotland, S.M.5
  • 56
    • 0033056680 scopus 로고    scopus 로고
    • Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga toxin as a phage late-gene product
    • Plunkett G, 3rd, Rose DJ, Durfee TJ, Blattner FR, (1999) Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga toxin as a phage late-gene product. J Bacteriol 181: 1767-1778.
    • (1999) J Bacteriol , vol.181 , pp. 1767-1778
    • Plunkett 3rd, G.1    Rose, D.J.2    Durfee, T.J.3    Blattner, F.R.4
  • 57
    • 0038443945 scopus 로고    scopus 로고
    • Immunity profiles of wild-type and recombinant shiga-like toxin-encoding bacteriophages and characterization of novel double lysogens
    • Allison HE, Sergeant MJ, James CE, Saunders JR, Smith DL, et al. (2003) Immunity profiles of wild-type and recombinant shiga-like toxin-encoding bacteriophages and characterization of novel double lysogens. Infect Immun 71: 3409-3418.
    • (2003) Infect Immun , vol.71 , pp. 3409-3418
    • Allison, H.E.1    Sergeant, M.J.2    James, C.E.3    Saunders, J.R.4    Smith, D.L.5
  • 58
    • 0043267536 scopus 로고    scopus 로고
    • Shiga toxin 2-converting bacteriophages associated with clonal variability in Escherichia coli O157:H7 strains of human origin isolated from a single outbreak
    • Muniesa M, de Simon M, Prats G, Ferrer D, Panella H, et al. (2003) Shiga toxin 2-converting bacteriophages associated with clonal variability in Escherichia coli O157:H7 strains of human origin isolated from a single outbreak. Infect Immun 71: 4554-4562.
    • (2003) Infect Immun , vol.71 , pp. 4554-4562
    • Muniesa, M.1    de Simon, M.2    Prats, G.3    Ferrer, D.4    Panella, H.5
  • 59
    • 35048894069 scopus 로고    scopus 로고
    • Short-tailed stx phages exploit the conserved YaeT protein to disseminate Shiga toxin genes among enterobacteria
    • Smith DL, James CE, Sergeant MJ, Yaxian Y, Saunders JR, et al. (2007) Short-tailed stx phages exploit the conserved YaeT protein to disseminate Shiga toxin genes among enterobacteria. J Bacteriol 189: 7223-7233.
    • (2007) J Bacteriol , vol.189 , pp. 7223-7233
    • Smith, D.L.1    James, C.E.2    Sergeant, M.J.3    Yaxian, Y.4    Saunders, J.R.5
  • 60
    • 0038154169 scopus 로고    scopus 로고
    • Homotrimeric, beta-stranded viral adhesins and tail proteins
    • Weigele PR, Scanlon E, King J, (2003) Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol 185: 4022-4030.
    • (2003) J Bacteriol , vol.185 , pp. 4022-4030
    • Weigele, P.R.1    Scanlon, E.2    King, J.3
  • 62
    • 0035861998 scopus 로고    scopus 로고
    • Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre
    • van Raaij MJ, Schoehn G, Burda MR, Miller S, (2001) Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. J Mol Biol 314: 1137-1146.
    • (2001) J Mol Biol , vol.314 , pp. 1137-1146
    • van Raaij, M.J.1    Schoehn, G.2    Burda, M.R.3    Miller, S.4
  • 63
    • 0036446878 scopus 로고    scopus 로고
    • Review: conformation and folding of novel beta-structural elements in viral fiber proteins: the triple beta-spiral and triple beta-helix
    • Mitraki A, Miller S, van Raaij MJ, (2002) Review: conformation and folding of novel beta-structural elements in viral fiber proteins: the triple beta-spiral and triple beta-helix. J Struct Biol 137: 236-247.
    • (2002) J Struct Biol , vol.137 , pp. 236-247
    • Mitraki, A.1    Miller, S.2    van Raaij, M.J.3
  • 64
    • 0042463705 scopus 로고    scopus 로고
    • The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold
    • Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, et al. (2003) The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J Mol Biol 331: 361-373.
    • (2003) J Mol Biol , vol.331 , pp. 361-373
    • Thomassen, E.1    Gielen, G.2    Schutz, M.3    Schoehn, G.4    Abrahams, J.P.5
  • 65
    • 79953200183 scopus 로고    scopus 로고
    • Structure of bacteriophage phi29 head fibers has a supercoiled triple repeating helix-turn-helix motif
    • Xiang Y, Rossmann MG, (2011) Structure of bacteriophage phi29 head fibers has a supercoiled triple repeating helix-turn-helix motif. Proc Natl Acad Sci U S A 108: 4806-4810.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4806-4810
    • Xiang, Y.1    Rossmann, M.G.2
  • 66
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain
    • Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG, (1997) Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5: 789-798.
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 67
    • 78651319979 scopus 로고    scopus 로고
    • Ongoing and future developments at the Universal Protein Resource
    • Uniprot, (2011) Ongoing and future developments at the Universal Protein Resource. Nucleic Acids Res 39: D214-219.
    • (2011) Nucleic Acids Res , vol.39
    • Uniprot1
  • 70
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas A, (1996) Prediction and analysis of coiled-coil structures. Methods Enzymol 266: 513-525.
    • (1996) Methods Enzymol , vol.266 , pp. 513-525
    • Lupas, A.1
  • 71
    • 0035999986 scopus 로고    scopus 로고
    • An HMM model for coiled-coil domains and a comparison with PSSM-based predictions
    • Delorenzi M, Speed T, (2002) An HMM model for coiled-coil domains and a comparison with PSSM-based predictions. Bioinformatics 18: 617-625.
    • (2002) Bioinformatics , vol.18 , pp. 617-625
    • Delorenzi, M.1    Speed, T.2
  • 72
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: a program for predicting two- and three-stranded coiled coils
    • Wolf E, Kim PS, Berger B, (1997) MultiCoil: a program for predicting two- and three-stranded coiled coils. Protein Sci 6: 1179-1189.
    • (1997) Protein Sci , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 73
    • 79960117679 scopus 로고    scopus 로고
    • SCORER 2.0: an algorithm for distinguishing parallel dimeric and trimeric coiled-coil sequences
    • Armstrong CT, Vincent TL, Green PJ, Woolfson DN, (2011) SCORER 2.0: an algorithm for distinguishing parallel dimeric and trimeric coiled-coil sequences. Bioinformatics 27: 1908-1914.
    • (2011) Bioinformatics , vol.27 , pp. 1908-1914
    • Armstrong, C.T.1    Vincent, T.L.2    Green, P.J.3    Woolfson, D.N.4
  • 74
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ, (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36: W197-201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 75
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices
    • Kammerer RA, Schulthess T, Landwehr R, Lustig A, Fischer D, et al. (1998) Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices. J Biol Chem 273: 10602-10608.
    • (1998) J Biol Chem , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5
  • 76
    • 34250316620 scopus 로고    scopus 로고
    • Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition
    • Blommel PG, Becker KJ, Duvnjak P, Fox BG, (2007) Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition. Biotechnol Prog 23: 585-598.
    • (2007) Biotechnol Prog , vol.23 , pp. 585-598
    • Blommel, P.G.1    Becker, K.J.2    Duvnjak, P.3    Fox, B.G.4
  • 77
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T, (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 78
    • 0022344789 scopus 로고
    • Mica sandwich technique for preparing macromolecules for rotary shadowing
    • Mould AP, Holmes DF, Kadler KE, Chapman JA, (1985) Mica sandwich technique for preparing macromolecules for rotary shadowing. J Ultrastruct Res 91: 66-76.
    • (1985) J Ultrastruct Res , vol.91 , pp. 66-76
    • Mould, A.P.1    Holmes, D.F.2    Kadler, K.E.3    Chapman, J.A.4
  • 82
    • 0037464552 scopus 로고    scopus 로고
    • Distinctiveness of the genomic sequence of Shiga toxin 2-converting phage isolated from Escherichia coli O157:H7 Okayama strain as compared to other Shiga toxin 2-converting phages
    • Sato T, Shimizu T, Watarai M, Kobayashi M, Kano S, et al. (2003) Distinctiveness of the genomic sequence of Shiga toxin 2-converting phage isolated from Escherichia coli O157:H7 Okayama strain as compared to other Shiga toxin 2-converting phages. Gene 309: 35-48.
    • (2003) Gene , vol.309 , pp. 35-48
    • Sato, T.1    Shimizu, T.2    Watarai, M.3    Kobayashi, M.4    Kano, S.5
  • 83
    • 0034066697 scopus 로고    scopus 로고
    • Four different genes responsible for nonimmune immunoglobulin-binding activities within a single strain of Escherichia coli
    • Sandt CH, Hill CW, (2000) Four different genes responsible for nonimmune immunoglobulin-binding activities within a single strain of Escherichia coli. Infect Immun 68: 2205-2214.
    • (2000) Infect Immun , vol.68 , pp. 2205-2214
    • Sandt, C.H.1    Hill, C.W.2
  • 84
    • 59249089471 scopus 로고    scopus 로고
    • Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths
    • Touchon M, Hoede C, Tenaillon O, Barbe V, Baeriswyl S, et al. (2009) Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths. PLoS Genet 5: e1000344.
    • (2009) PLoS Genet , vol.5
    • Touchon, M.1    Hoede, C.2    Tenaillon, O.3    Barbe, V.4    Baeriswyl, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.