메뉴 건너뛰기




Volumn 188, Issue 12, 2006, Pages 4312-4320

Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; CHAPERONIN; CHEA KINASE; CHEMOTACTIC PEPTIDE; FLAGELLIN; PROTEIN AHP; PROTEIN FLAA; PROTEIN FLAB; PROTEIN FLAC; PROTEIN FLGG; PROTEIN FLGG2; PROTEIN FLID; PROTEIN PEB1; PROTEIN TPX; PROTEOME; UNCLASSIFIED DRUG;

EID: 33744967758     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01975-05     Document Type: Article
Times cited : (224)

References (65)
  • 1
    • 0035870985 scopus 로고    scopus 로고
    • Campylobacter jejuni infections: Update on emerging issues and trends
    • Allos, B. M. 2001. Campylobacter jejuni infections: update on emerging issues and trends. Clin. Infect. Dis. 32:1201-1206.
    • (2001) Clin. Infect. Dis. , vol.32 , pp. 1201-1206
    • Allos, B.M.1
  • 2
    • 0032525168 scopus 로고    scopus 로고
    • Thin aggregative fimbriae enhance Salmonella enteridis biofilm formation
    • Austin, J. W., G. Sanders, W. W. Kay, and S. K. Collinson. 1998. Thin aggregative fimbriae enhance Salmonella enteridis biofilm formation. FEMS Microhiol. Lett. 162:295-301.
    • (1998) FEMS Microhiol. Lett. , vol.162 , pp. 295-301
    • Austin, J.W.1    Sanders, G.2    Kay, W.W.3    Collinson, S.K.4
  • 3
    • 0029347038 scopus 로고
    • Development of bacterial biofilms in dairy processing lines
    • Austin, J. W., and G. Bergeron. 1995. Development of bacterial biofilms in dairy processing lines. J. Dairy Res. 62:509-519.
    • (1995) J. Dairy Res. , vol.62 , pp. 509-519
    • Austin, J.W.1    Bergeron, G.2
  • 4
    • 0032837846 scopus 로고    scopus 로고
    • An iron-regulated alkyl hydroperoxide reductasc (AhpC) confers acrotolerance and oxidative stress resistance to the microacrophilic pathogen Campylobacter jejuni
    • Baillon, M. A., A. H. M. van Vliet, J. M. Ketley, C. Constantinidou, and C. W. Penn. 1999. An iron-regulated alkyl hydroperoxide reductasc (AhpC) confers acrotolerance and oxidative stress resistance to the microacrophilic pathogen Campylobacter jejuni. J. Bacteriol. 181:4798-4804.
    • (1999) J. Bacteriol. , vol.181 , pp. 4798-4804
    • Baillon, M.A.1    Van Vliet, A.H.M.2    Ketley, J.M.3    Constantinidou, C.4    Penn, C.W.5
  • 6
    • 0033969301 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-G and initiation factor 1F2
    • Caldas, T., S. Laalami, and G. Richarme. 2000. Chaperone properties of bacterial elongation factor EF-G and initiation factor 1F2. J. Biol. Chem. 275:855-860.
    • (2000) J. Biol. Chem. , vol.275 , pp. 855-860
    • Caldas, T.1    Laalami, S.2    Richarme, G.3
  • 7
    • 9144271205 scopus 로고    scopus 로고
    • Analysis of Pseudomonas fluorescent F113 genes implicated in flagellar filament synthesis and their role in competitive root colonization
    • Capdevila, S., F. M. Martinez-Granero, M. Sanchez-Contreras, R. Rivilla, and M. Martin. 2004. Analysis of Pseudomonas fluorescent F113 genes implicated in flagellar filament synthesis and their role in competitive root colonization. Microbiology 150:3889-3897.
    • (2004) Microbiology , vol.150 , pp. 3889-3897
    • Capdevila, S.1    Martinez-Granero, F.M.2    Sanchez-Contreras, M.3    Rivilla, R.4    Martin, M.5
  • 9
    • 2342662203 scopus 로고    scopus 로고
    • Characterization of monospecies biofilm formation by Helicobacler pylori
    • Cole, S. P., J. Harwood, R. Lee, R. She, and D. G. Guiney. 2004. Characterization of monospecies biofilm formation by Helicobacler pylori. S. Bacteriol. 186:3124-3132.
    • (2004) S. Bacteriol. , vol.186 , pp. 3124-3132
    • Cole, S.P.1    Harwood, J.2    Lee, R.3    She, R.4    Guiney, D.G.5
  • 11
    • 0034443286 scopus 로고    scopus 로고
    • Microbial biofilms: From ecology to molecular genetics
    • Davey, M. E., and G. A. O'Toole. 2000. Microbial biofilms: from ecology to molecular genetics. Microbiol. Mol. Biol. Rev. 64:847-867.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 847-867
    • Davey, M.E.1    O'Toole, G.A.2
  • 12
    • 0037313237 scopus 로고    scopus 로고
    • Understanding biolilm resistance to antibacterial agents
    • Davies, D. 2003. Understanding biolilm resistance to antibacterial agents. Nat. Rev. 2:114-122.
    • (2003) Nat. Rev. , vol.2 , pp. 114-122
    • Davies, D.1
  • 13
    • 0026041701 scopus 로고
    • Scanning electron microscopy of piliated Neisseria gonorrhoeae processed with hexamethyl-disilazane
    • Dekker, N. P., C. J. Lammel, and G. F. Brooks. 1991. Scanning electron microscopy of piliated Neisseria gonorrhoeae processed with hexamethyl- disilazane. J. Electron Microsc. Technol. 19:461-467.
    • (1991) J. Electron Microsc. Technol. , vol.19 , pp. 461-467
    • Dekker, N.P.1    Lammel, C.J.2    Brooks, G.F.3
  • 14
    • 0036228505 scopus 로고    scopus 로고
    • Biofilms: Survival mechanisms of clinically relevant microorganisms
    • Donlan, R. M., and J. W. Costerton. 2002. Biofilms: survival mechanisms of clinically relevant microorganisms. Clin. Microbiol. Rev. 15:167-193.
    • (2002) Clin. Microbiol. Rev. , vol.15 , pp. 167-193
    • Donlan, R.M.1    Costerton, J.W.2
  • 15
    • 14544306021 scopus 로고    scopus 로고
    • Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolticus
    • Enos-Berlage, J. L., Z. T. Guvener, C. E. Keenan, and L. L. McCarter. 2005. Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolticus. Mol. Microbiol. 55:1160-1182.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1160-1182
    • Enos-Berlage, J.L.1    Guvener, Z.T.2    Keenan, C.E.3    McCarter, L.L.4
  • 16
    • 0036670725 scopus 로고    scopus 로고
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
    • Frazzon, J., J. R. Fick, and D. R. Dean. 2001. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem. Soc. Trans. 30:680-685.
    • (2001) Biochem. Soc. Trans. , vol.30 , pp. 680-685
    • Frazzon, J.1    Fick, J.R.2    Dean, D.R.3
  • 17
    • 9644274213 scopus 로고    scopus 로고
    • Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus
    • Frees, D., A. Chastanet, S. Qazi, K. Sørensen, P. Hill, T. Msadek, and H. Ingmer. 2004. Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus. Mol. Microbiol. 54:1445-1462.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1445-1462
    • Frees, D.1    Chastanet, A.2    Qazi, S.3    Sørensen, K.4    Hill, P.5    Msadek, T.6    Ingmer, H.7
  • 18
    • 1242297814 scopus 로고    scopus 로고
    • Genes involved in matrix formation in Pseudomonas aeruginosa PA14
    • Friedman, L., and R. Kolter. 2004. Genes involved in matrix formation in Pseudomonas aeruginosa PA14. Mol. Microbiol. 51:675-690.
    • (2004) Mol. Microbiol. , vol.51 , pp. 675-690
    • Friedman, L.1    Kolter, R.2
  • 20
    • 0031831529 scopus 로고    scopus 로고
    • Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance
    • Gerth, U., E. Kruger, I. Derre, T. Msadek, and M. Hecker. 1998. Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance. Mol. Microbiol. 28:787-802.
    • (1998) Mol. Microbiol. , vol.28 , pp. 787-802
    • Gerth, U.1    Kruger, E.2    Derre, I.3    Msadek, T.4    Hecker, M.5
  • 21
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker, M., W. Schumann, and U. Volker. 1996. Heat-shock and general stress response in Bacillus subtilis. Mol. Microbiol. 417-428.
    • (1996) Mol. Microbiol. , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Volker, U.3
  • 23
    • 0142182383 scopus 로고    scopus 로고
    • Carbon starvation survival of Listeria monocytogenes in planktonic state and in biofilm: A proteomic study
    • Helloin, E., L. Jänsch, and L. Phan-Thanh. 2003. Carbon starvation survival of Listeria monocytogenes in planktonic state and in biofilm: a proteomic study. Proteomics 3:2052-2064.
    • (2003) Proteomics , vol.3 , pp. 2052-2064
    • Helloin, E.1    Jänsch, L.2    Phan-Thanh, L.3
  • 24
    • 23644456851 scopus 로고    scopus 로고
    • The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits
    • Hirokawa, G., R. M. Nijman, V. S. Raj, H. Kaji, K. Igarashi, and A. Kaji. 2005. The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits. RNA 11:1317-1328.
    • (2005) RNA , vol.11 , pp. 1317-1328
    • Hirokawa, G.1    Nijman, R.M.2    Raj, V.S.3    Kaji, H.4    Igarashi, K.5    Kaji, A.6
  • 25
    • 20444483297 scopus 로고    scopus 로고
    • ClpXP protease controls expression of the type III protein secretion system through regulation of RpoS and Gr1R levels in enterohemorrhagic Escherichia coli
    • Iyoda, S., and H. Watanabe. 2005. ClpXP protease controls expression of the type III protein secretion system through regulation of RpoS and Gr1R levels in enterohemorrhagic Escherichia coli. J. Bacteriol. 187:4086-4094.
    • (2005) J. Bacteriol. , vol.187 , pp. 4086-4094
    • Iyoda, S.1    Watanabe, H.2
  • 26
    • 9644301279 scopus 로고    scopus 로고
    • The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein
    • Jackson, M. W., E. Silva-Herzog, and G. V. Plano. 2004. The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein. Mol. Microbiol. 54:1364-1378.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1364-1378
    • Jackson, M.W.1    Silva-Herzog, E.2    Plano, G.V.3
  • 28
    • 1842588824 scopus 로고    scopus 로고
    • Aeromonas flagella (polar and lateral) are enterocyte adhesins that contribute to biofilm formation on surfaces
    • Kirov, S. M., M. Castrisios, and J. G. Shaw. 2004. Aeromonas flagella (polar and lateral) are enterocyte adhesins that contribute to biofilm formation on surfaces. Infect. Immun. 72:1939-1945.
    • (2004) Infect. Immun. , vol.72 , pp. 1939-1945
    • Kirov, S.M.1    Castrisios, M.2    Shaw, J.G.3
  • 29
    • 0028290369 scopus 로고
    • Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance
    • Krüger, E., U. Völker, and M. Hecker. 1994. Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance. J. Bacteriol. 176:3360-3367.
    • (1994) J. Bacteriol. , vol.176 , pp. 3360-3367
    • Krüger, E.1    Völker, U.2    Hecker, M.3
  • 30
    • 28244447376 scopus 로고    scopus 로고
    • BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis
    • Latasa, C., A. Roux, A. Toledo-Arana, J.-M. Ghigo, C. Gamazo, J. R. Penades, and I. Lasa. 2005. BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis. Mol. Microbiol. 58:1322-1339.
    • (2005) Mol. Microbiol. , vol.58 , pp. 1322-1339
    • Latasa, C.1    Roux, A.2    Toledo-Arana, A.3    Ghigo, J.-M.4    Gamazo, C.5    Penades, J.R.6    Lasa, I.7
  • 31
    • 15744396567 scopus 로고    scopus 로고
    • Lessons from DNA microarray analysis: The gene expression profile of biofilms
    • Lazazzera, B. A. 2005. Lessons from DNA microarray analysis: the gene expression profile of biofilms. Curr. Opin. Microbiol. 8:222-227.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 222-227
    • Lazazzera, B.A.1
  • 32
    • 24044525647 scopus 로고    scopus 로고
    • Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction
    • Lee, Y., H. Lee Do, C. W. Kho, A. Y. Lee, M. Jang, S. Cho, C. H. Lee, J. S. Lee, P. K. Myung, B. C. Park, and S. G. Park. 2005. Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett. 579:4769-4774.
    • (2005) FEBS Lett. , vol.579 , pp. 4769-4774
    • Lee, Y.1    Lee Do, H.2    Kho, C.W.3    Lee, A.Y.4    Jang, M.5    Cho, S.6    Lee, C.H.7    Lee, J.S.8    Myung, P.K.9    Park, B.C.10    Park, S.G.11
  • 33
    • 0036843009 scopus 로고    scopus 로고
    • Regulation and physiological significance of ClpC and ClpP in Streptococcus mutans
    • Lenios, J. A. C., and R. A. Burne. 2002. Regulation and physiological significance of ClpC and ClpP in Streptococcus mutans. J. Bacteriol. 184:6357-6366.
    • (2002) J. Bacteriol. , vol.184 , pp. 6357-6366
    • Lenios, J.A.C.1    Burne, R.A.2
  • 34
    • 0242553802 scopus 로고    scopus 로고
    • The role of transport vehicles, modules and transport crates as potential sources of Campylobacter infections for broilers
    • McKenna, J. P., A. N. Oza, and S. W. J. McDowell. 2001. The role of transport vehicles, modules and transport crates as potential sources of Campylobacter infections for broilers. Int. J. Med. Microbiol. 291:38.
    • (2001) Int. J. Med. Microbiol. , vol.291 , pp. 38
    • McKenna, J.P.1    Oza, A.N.2    McDowell, S.W.J.3
  • 36
    • 0033784513 scopus 로고    scopus 로고
    • Detection and characterization of autoagglutination activity by Campylobacter jejuni
    • Misawa, N., and M. J. Blaser. 2000. Detection and characterization of autoagglutination activity by Campylobacter jejuni. Infect. Immun. 68:6168-6175.
    • (2000) Infect. Immun. , vol.68 , pp. 6168-6175
    • Misawa, N.1    Blaser, M.J.2
  • 37
    • 0037315734 scopus 로고    scopus 로고
    • Specific detection of Areobacter and Campylobacter strains in water and sewage by PCR and fluorescent in situ hybridization
    • Moreno, Y., S. Botella, J. L. Alonso, M. A. Ferrus, M. Hernandez, and J. Hernandez. 2003. Specific detection of Areobacter and Campylobacter strains in water and sewage by PCR and fluorescent in situ hybridization. Appl. Environ. Microhiol. 69:1181-1186.
    • (2003) Appl. Environ. Microhiol. , vol.69 , pp. 1181-1186
    • Moreno, Y.1    Botella, S.2    Alonso, J.L.3    Ferrus, M.A.4    Hernandez, M.5    Hernandez, J.6
  • 38
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: A genetic analysis
    • O'Toole, G. A., and R. Kolter. 1998. Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis. Mol. Microbiol. 28:449-461.
    • (1998) Mol. Microbiol. , vol.28 , pp. 449-461
    • O'Toole, G.A.1    Kolter, R.2
  • 40
    • 0031885909 scopus 로고    scopus 로고
    • Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice
    • Pei, Z., C. Burucoa, B. Grignon, S. Baqar, X. Z. Huang, D. J. Kopecko, A. L. Bourgeois, J. L. Fauchere, and M. J. Blaser. 1998. Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice. Infect. Immun. 66:938-943.
    • (1998) Infect. Immun. , vol.66 , pp. 938-943
    • Pei, Z.1    Burucoa, C.2    Grignon, B.3    Baqar, S.4    Huang, X.Z.5    Kopecko, D.J.6    Bourgeois, A.L.7    Fauchere, J.L.8    Blaser, M.J.9
  • 41
    • 0025994829 scopus 로고
    • Identification, purification, and characterization of major antigenic proteins of Campylobacler jejuni
    • Pei, Z. H., R. T. Ellison III, and M. J. Blaser. 1991. Identification, purification, and characterization of major antigenic proteins of Campylobacler jejuni. J. Biol. Chem. 266:16363-16369.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16363-16369
    • Pei, Z.H.1    Ellison III, R.T.2    Blaser, M.J.3
  • 42
    • 0032902058 scopus 로고    scopus 로고
    • New insights into the ATP-dependent C1p protease: Escherichia coli and beyond
    • Porankiewicz, J., J. Wang, and A. K. Clarke. 1999. New insights into the ATP-dependent C1p protease: Escherichia coli and beyond. Mol. Microbiol. 32:449-458.
    • (1999) Mol. Microbiol. , vol.32 , pp. 449-458
    • Porankiewicz, J.1    Wang, J.2    Clarke, A.K.3
  • 43
    • 37249046796 scopus 로고    scopus 로고
    • 1 January last date modified. [Online.]
    • Public Health Agency of Canada. 1 January 2006, last date modified. Canada communicable disease report. [Online.] http://dsol-smed.phac-aspc.gc.ca /dsol-smed/indis/index_e.html.
    • (2006) Canada Communicable Disease Report
  • 44
    • 0032603137 scopus 로고    scopus 로고
    • Quantifying protein in 2-D PAGE solubilization buffers
    • Ramagli, L. S. 1999. Quantifying protein in 2-D PAGE solubilization buffers. Methods Mol. Biol. 112:99-103.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 99-103
    • Ramagli, L.S.1
  • 45
    • 0035458302 scopus 로고    scopus 로고
    • Prevalence, antigenic specificity, and bactericidal activity of poultry anti-Campylobacter maternal antibodies
    • Sahin, O., Q. Zhang, J. C. Meitzler, B. S. Harr, T. Y. Morishita, and R. Mohan. 2001. Prevalence, antigenic specificity, and bactericidal activity of poultry anti-Campylobacter maternal antibodies. Appl. Environ. Microbiol. 67:3951-3957.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3951-3957
    • Sahin, O.1    Zhang, Q.2    Meitzler, J.C.3    Harr, B.S.4    Morishita, T.Y.5    Mohan, R.6
  • 47
    • 15444369720 scopus 로고    scopus 로고
    • Effect of heat, acidification, and chlorination on Salmonella enterica serovar Typhimurium cells in a biofilm formed at the air-liquid interface
    • Scher, K., U. Romling, and S. Yaron. 2005. Effect of heat, acidification, and chlorination on Salmonella enterica serovar Typhimurium cells in a biofilm formed at the air-liquid interface. Appl. Environ. Microbiol. 71:1163-1168.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1163-1168
    • Scher, K.1    Romling, U.2    Yaron, S.3
  • 48
    • 0035992111 scopus 로고    scopus 로고
    • The carry-over of Campylobacter isolates between sequential poultry flocks
    • Shreeve, J. E., M. Toszeghy, A. Ridley, and D. G. Newell. 2002. The carry-over of Campylobacter isolates between sequential poultry flocks. Avian Dis. 46:378-385.
    • (2002) Avian Dis. , vol.46 , pp. 378-385
    • Shreeve, J.E.1    Toszeghy, M.2    Ridley, A.3    Newell, D.G.4
  • 49
    • 4344700535 scopus 로고    scopus 로고
    • The physiological role of ferritin-like compounds in bacteria
    • Smith, J. L. 2004. The physiological role of ferritin-like compounds in bacteria. Crit. Rev. Microbiol. 30:173-185.
    • (2004) Crit. Rev. Microbiol. , vol.30 , pp. 173-185
    • Smith, J.L.1
  • 50
    • 0036270804 scopus 로고    scopus 로고
    • Genetic analysis of Salmonella enteritidis biofilm formation: Critical role of cellulose
    • Solano, C., B. Garcia, J. Valle, C. Berasain, J.-M. Ghigo, C. Gamazo, and I. Lasa. 2002. Genetic analysis of Salmonella enteritidis biofilm formation: critical role of cellulose. Mol. Microbiol. 43:793-808.
    • (2002) Mol. Microbiol. , vol.43 , pp. 793-808
    • Solano, C.1    Garcia, B.2    Valle, J.3    Berasain, C.4    Ghigo, J.-M.5    Gamazo, C.6    Lasa, I.7
  • 51
    • 3242885338 scopus 로고    scopus 로고
    • FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC 43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion
    • Song, Y. C., S. Jin, H. Louie, D. Ng, R. Lau, Y. Zhang, R. Weerasekera, S. Al Tashid, L. A. Ward, S. D. Der, and V. L. Chan. 2004. FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC 43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion. Mol. Microbiol. 53:541-553.
    • (2004) Mol. Microbiol. , vol.53 , pp. 541-553
    • Song, Y.C.1    Jin, S.2    Louie, H.3    Ng, D.4    Lau, R.5    Zhang, Y.6    Weerasekera, R.7    Al Tashid, S.8    Ward, L.A.9    Der, S.D.10    Chan, V.L.11
  • 52
    • 0037732623 scopus 로고    scopus 로고
    • Cattle and sheep farms as reservoirs of Campylobacter
    • Stanley, K., and K. Jones. 2003. Cattle and sheep farms as reservoirs of Campylobacter. J. Appl. Microbiol. 94(Suppl. 1):104-113.
    • (2003) J. Appl. Microbiol. , vol.94 , Issue.SUPPL. 1 , pp. 104-113
    • Stanley, K.1    Jones, K.2
  • 54
    • 0026444522 scopus 로고
    • The occurrence of Campylobacter in a mountain brook
    • In German
    • Stelzer, W., and J. Jacob. 1992. The occurrence of Campylobacter in a mountain brook. Zentralbl. Mikrobiol. 147:45-50. (In German.)
    • (1992) Zentralbl. Mikrobiol. , vol.147 , pp. 45-50
    • Stelzer, W.1    Jacob, J.2
  • 56
    • 0031252126 scopus 로고    scopus 로고
    • Flagellin a gene restriction fragment length polymorphism patterns of Campylobacter spp. isolates from broiler production sources
    • Stern, N. J., M. A. Myszewski, H. M. Barnhart, and D. W. Dreesen. 1997. Flagellin A gene restriction fragment length polymorphism patterns of Campylobacter spp. isolates from broiler production sources. Avian Dis. 41:899-905.
    • (1997) Avian Dis. , vol.41 , pp. 899-905
    • Stern, N.J.1    Myszewski, M.A.2    Barnhart, H.M.3    Dreesen, D.W.4
  • 58
    • 0035984079 scopus 로고    scopus 로고
    • Effectivness of chemical sanitizers againsi Campylobacter jejuni-containing biofilms
    • Trachoo, N., and J. F. Frank. 2002. Effectivness of chemical sanitizers againsi Campylobacter jejuni-containing biofilms. J. Food Prot. 65:1117-1121.
    • (2002) J. Food Prot. , vol.65 , pp. 1117-1121
    • Trachoo, N.1    Frank, J.F.2
  • 59
    • 0035984086 scopus 로고    scopus 로고
    • Survival of Campylobacter jejuni in biofilms isolated from chicken houses
    • Trachoo, N., J. F. Frank, and N. J. Stern. 2002. Survival of Campylobacter jejuni in biofilms isolated from chicken houses. J. Food Prot. 65:1110-1116.
    • (2002) J. Food Prot. , vol.65 , pp. 1110-1116
    • Trachoo, N.1    Frank, J.F.2    Stern, N.J.3
  • 60
    • 0036285109 scopus 로고    scopus 로고
    • The role of iron in Campylobacter gene regulation, metabolism, and oxidative stress defence
    • van Vliet, A. H. M., J. M. Ketley, S. F. Park, and C. W. Penn. 2002. The role of iron in Campylobacter gene regulation, metabolism, and oxidative stress defence. FEMS Microbiol. Rev. 26:173-186.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 173-186
    • Van Vliet, A.H.M.1    Ketley, J.M.2    Park, S.F.3    Penn, C.W.4
  • 61
    • 15844362276 scopus 로고    scopus 로고
    • The pel genes of the Pseudomonas aeroginosa PAK strain are involved at early and late stages of biofilm formation
    • Vasseur, P., I. Vallet-Gely, C. Soscia, S. Genin, and A. Filloux. 2005. The pel genes of the Pseudomonas aeroginosa PAK strain are involved at early and late stages of biofilm formation. Microbiology 151:985-997.
    • (2005) Microbiology , vol.151 , pp. 985-997
    • Vasseur, P.1    Vallet-Gely, I.2    Soscia, C.3    Genin, S.4    Filloux, A.5
  • 63
    • 0242417584 scopus 로고    scopus 로고
    • Prevalence of Campylobactcr jejuni, Campylobacter lari, and Campylobacter coli in different ecological guilds and taxa of migrating birds
    • Waldenstrom, J., T. Broman, I. Carlsson, D. Hasselquist, R. P. Achterberg, J. A. Wagenaar, and B. Olsen. 2002. Prevalence of Campylobactcr jejuni, Campylobacter lari, and Campylobacter coli in different ecological guilds and taxa of migrating birds. Appl. Environ. Microbiol. 68:5911-5917.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5911-5917
    • Waldenstrom, J.1    Broman, T.2    Carlsson, I.3    Hasselquist, D.4    Achterberg, R.P.5    Wagenaar, J.A.6    Olsen, B.7
  • 65
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., M. R. Maurizi, and S. Gottesman. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.