메뉴 건너뛰기




Volumn 91, Issue 1, 2009, Pages 375-387

Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptors

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL PROTEIN CETA; BACTERIAL PROTEIN CETB; BACTERIAL PROTEIN HAMP; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN;

EID: 58149479212     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00578-08     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 33847249975 scopus 로고    scopus 로고
    • Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors
    • Alexander, R. P., and I. B. Zhulin. 2007. Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors. Proc. Natl. Acad. Sci. USA 104:2885-2890.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2885-2890
    • Alexander, R.P.1    Zhulin, I.B.2
  • 3
    • 0030908893 scopus 로고    scopus 로고
    • +-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
    • +-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16:2179-2187.
    • (1997) EMBO J , vol.16 , pp. 2179-2187
    • Ansell, R.1    Granath, K.2    Hohmann, S.3    Thevelein, J.M.4    Adler, L.5
  • 4
    • 0042561788 scopus 로고    scopus 로고
    • Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases
    • Appleman, J. A., L. L. Chen, and V. Stewart. 2003. Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases. J. Bacteriol. 185:4872-4882.
    • (2003) J. Bacteriol , vol.185 , pp. 4872-4882
    • Appleman, J.A.1    Chen, L.L.2    Stewart, V.3
  • 5
    • 0037216619 scopus 로고    scopus 로고
    • Mutational analysis of a conserved signal-transducing element: The HAMP linker of the Escherichia coli nitrate sensor NarX
    • Appleman, J. A., and V. Stewart. 2003. Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX. J. Bacteriol. 185:89-97.
    • (2003) J. Bacteriol , vol.185 , pp. 89-97
    • Appleman, J.A.1    Stewart, V.2
  • 6
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L., and C. P. Ponting. 1999. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176:111-116.
    • (1999) FEMS Microbiol. Lett , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 9
    • 0034705035 scopus 로고    scopus 로고
    • Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli
    • Bibikov, S. I., L. A. Barnes, Y. Gitin, and J. S. Parkinson. 2000. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli. Proc. Natl. Acad. Sci. USA 97:5830-5835.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5830-5835
    • Bibikov, S.I.1    Barnes, L.A.2    Gitin, Y.3    Parkinson, J.S.4
  • 10
    • 0030925238 scopus 로고    scopus 로고
    • A signal transducer for aerotaxis in Escherichia coli
    • Bibikov, S. I., R. Biran, K. E. Rudd, and J. S. Parkinson. 1997. A signal transducer for aerotaxis in Escherichia coli. J. Bacteriol. 179:4075-4079.
    • (1997) J. Bacteriol , vol.179 , pp. 4075-4079
    • Bibikov, S.I.1    Biran, R.2    Rudd, K.E.3    Parkinson, J.S.4
  • 11
    • 1942453423 scopus 로고    scopus 로고
    • Infection with Campylobacter jejuni induces tyrosine-phosphorylated proteins into INT-407 cells
    • Biswas, D., H. Niwa, and K. Itoh. 2004. Infection with Campylobacter jejuni induces tyrosine-phosphorylated proteins into INT-407 cells. Microbiol. Immunol. 48:221-228.
    • (2004) Microbiol. Immunol , vol.48 , pp. 221-228
    • Biswas, D.1    Niwa, H.2    Itoh, K.3
  • 13
    • 33646597727 scopus 로고    scopus 로고
    • Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Buron-Barral, M. C., K. K. Gosink, and J. S. Parkinson. 2006. Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer. J. Bacteriol. 188:3477-3486.
    • (2006) J. Bacteriol , vol.188 , pp. 3477-3486
    • Buron-Barral, M.C.1    Gosink, K.K.2    Parkinson, J.S.3
  • 14
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler, S. L., and J. J. Falke. 1998. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor. Biochemistry 37:10746-10756.
    • (1998) Biochemistry , vol.37 , pp. 10746-10756
    • Butler, S.L.1    Falke, J.J.2
  • 16
    • 0037340113 scopus 로고    scopus 로고
    • Membrane localization of the ToxR winged-helix domain is required for TcpP-mediated virulence gene activation in Vibrio cholerae
    • Crawford, J. A., E. S. Krukonis, and V. J. DiRita. 2003. Membrane localization of the ToxR winged-helix domain is required for TcpP-mediated virulence gene activation in Vibrio cholerae. Mol. Microbiol. 47:1459-1473.
    • (2003) Mol. Microbiol , vol.47 , pp. 1459-1473
    • Crawford, J.A.1    Krukonis, E.S.2    DiRita, V.J.3
  • 17
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., E. Wallin, I. Simon, G. von Heijne, and A. Elofsson. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10:673-676.
    • (1997) Protein Eng , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    von Heijne, G.4    Elofsson, A.5
  • 18
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff, J. A., and G. J. Barton. 2000. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40:502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 19
    • 49249120898 scopus 로고    scopus 로고
    • Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni
    • Elliott, K. T., and V. J. DiRita. 2008. Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni. Mol. Microbiol. 69: 1091-1103.
    • (2008) Mol. Microbiol , vol.69 , pp. 1091-1103
    • Elliott, K.T.1    DiRita, V.J.2
  • 20
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 21
    • 34247103273 scopus 로고    scopus 로고
    • Preliminary FoodNet data on the incidence of infection with pathogens transmitted commonly through food - 10 states, 2006
    • Foodnet. 2007. Preliminary FoodNet data on the incidence of infection with pathogens transmitted commonly through food - 10 states, 2006. MMWR Morb. Mortal. Wkly. Rep. 56:336-339.
    • (2007) MMWR Morb. Mortal. Wkly. Rep , vol.56 , pp. 336-339
    • Foodnet1
  • 22
    • 31444443960 scopus 로고    scopus 로고
    • Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed
    • Fukuda, Y., Y. Okamura, H. Takeyama, and T. Matsunaga. 2006. Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed. FEBS Lett. 580:801-812.
    • (2006) FEBS Lett , vol.580 , pp. 801-812
    • Fukuda, Y.1    Okamura, Y.2    Takeyama, H.3    Matsunaga, T.4
  • 23
    • 0036128480 scopus 로고    scopus 로고
    • Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis
    • Golden, N. J., and D. W. Acheson. 2002. Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis. Infect. Immun. 70:1761-1771.
    • (2002) Infect. Immun , vol.70 , pp. 1761-1771
    • Golden, N.J.1    Acheson, D.W.2
  • 25
    • 35648945254 scopus 로고    scopus 로고
    • Campylobacter flagella: Not just for motility
    • Guerry, P. 2007. Campylobacter flagella: not just for motility. Trends Microbiol. 15:456-461.
    • (2007) Trends Microbiol , vol.15 , pp. 456-461
    • Guerry, P.1
  • 26
    • 0028198979 scopus 로고
    • Systems of experimental genetics for Campylobacter species
    • Guerry, P., R. Yao, R. A. Alm, D. H. Burr, and T. J. Trust. 1994. Systems of experimental genetics for Campylobacter species. Methods Enzymol. 235:474-481.
    • (1994) Methods Enzymol , vol.235 , pp. 474-481
    • Guerry, P.1    Yao, R.2    Alm, R.A.3    Burr, D.H.4    Trust, T.J.5
  • 27
    • 0035050923 scopus 로고    scopus 로고
    • Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility
    • Hendrixson, D. R., B. J. Akerley, and V. J. DiRita. 2001. Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility. Mol. Microbiol. 40:214-224.
    • (2001) Mol. Microbiol , vol.40 , pp. 214-224
    • Hendrixson, D.R.1    Akerley, B.J.2    DiRita, V.J.3
  • 28
    • 1942532926 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract
    • Hendrixson, D. R., and V. J. DiRita. 2004. Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract. Mol. Microbiol. 52:471-484.
    • (2004) Mol. Microbiol , vol.52 , pp. 471-484
    • Hendrixson, D.R.1    DiRita, V.J.2
  • 29
    • 0032765704 scopus 로고    scopus 로고
    • Campylobacter jejuni 81-176 associates with microtubules and dynein during invasion of human intestinal cells
    • Hu, L., and D. J. Kopecko. 1999. Campylobacter jejuni 81-176 associates with microtubules and dynein during invasion of human intestinal cells. Infect. Immun. 67:4171-4182.
    • (1999) Infect. Immun , vol.67 , pp. 4171-4182
    • Hu, L.1    Kopecko, D.J.2
  • 30
    • 32344447753 scopus 로고    scopus 로고
    • Signal transduction events involved in human epithelial cell invasion by Campylobacter jejuni 81-176
    • Hu, L., J. P. McDaniel, and D. J. Kopecko. 2006. Signal transduction events involved in human epithelial cell invasion by Campylobacter jejuni 81-176. Microb. Pathog. 40:91-100.
    • (2006) Microb. Pathog , vol.40 , pp. 91-100
    • Hu, L.1    McDaniel, J.P.2    Kopecko, D.J.3
  • 32
    • 0347359161 scopus 로고    scopus 로고
    • Modification of glycolysis affects cell sensitivity to apoptosis induced by oxidative stress and mediated by mitochondria
    • Jeong, D. W., T. S. Kim, I. T. Cho, and I. Y. Kim. 2004. Modification of glycolysis affects cell sensitivity to apoptosis induced by oxidative stress and mediated by mitochondria. Biochem. Biophys. Res. Commun. 313:984-991.
    • (2004) Biochem. Biophys. Res. Commun , vol.313 , pp. 984-991
    • Jeong, D.W.1    Kim, T.S.2    Cho, I.T.3    Kim, I.Y.4
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0024459765 scopus 로고
    • Adhesion to and invasion of HEp-2 cells by Campylobacter spp
    • Konkel, M. E., and L. A. Joens. 1989. Adhesion to and invasion of HEp-2 cells by Campylobacter spp. Infect. Immun. 57:2984-2990.
    • (1989) Infect. Immun , vol.57 , pp. 2984-2990
    • Konkel, M.E.1    Joens, L.A.2
  • 35
    • 0033016809 scopus 로고    scopus 로고
    • Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells
    • Konkel, M. E., B. J. Kim, V. Rivera-Amill, and S. G. Garvis. 1999. Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells. Mol. Microbiol. 32:691-701.
    • (1999) Mol. Microbiol , vol.32 , pp. 691-701
    • Konkel, M.E.1    Kim, B.J.2    Rivera-Amill, V.3    Garvis, S.G.4
  • 36
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel, M. E., J. D. Klena, V. Rivera-Amill, M. R. Monteville, D. Biswas, B. Raphael, and J. Mickelson. 2004. Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J. Bacteriol. 186:3296-3303.
    • (2004) J. Bacteriol , vol.186 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4    Biswas, D.5    Raphael, B.6    Mickelson, J.7
  • 37
    • 0035423127 scopus 로고    scopus 로고
    • Campylobacter jejuni - microtubule-dependent invasion
    • Kopecko, D. J., L. Hu, and K. J. Zaal. 2001. Campylobacter jejuni - microtubule-dependent invasion. Trends Microbiol. 9:389-396.
    • (2001) Trends Microbiol , vol.9 , pp. 389-396
    • Kopecko, D.J.1    Hu, L.2    Zaal, K.J.3
  • 40
    • 11144338821 scopus 로고    scopus 로고
    • Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix
    • Ma, Q., M. S. Johnson, and B. L. Taylor. 2005. Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix. J. Bacteriol. 187:193-201.
    • (2005) J. Bacteriol , vol.187 , pp. 193-201
    • Ma, Q.1    Johnson, M.S.2    Taylor, B.L.3
  • 42
    • 0033597281 scopus 로고    scopus 로고
    • A turn propensity scale for transmembrane helices
    • Monne, M., M. Hermansson, and G. von Heijne. 1999. A turn propensity scale for transmembrane helices. J. Mol. Biol. 288:141-145.
    • (1999) J. Mol. Biol , vol.288 , pp. 141-145
    • Monne, M.1    Hermansson, M.2    von Heijne, G.3
  • 43
    • 0033527670 scopus 로고    scopus 로고
    • Turns in transmembrane helices: Determination of the minimal length of a "helical hairpin" and derivation of a fine-grained turn propensity scale
    • Monne, M., I. Nilsson, A. Elofsson, and G. von Heijne. 1999. Turns in transmembrane helices: determination of the minimal length of a "helical hairpin" and derivation of a fine-grained turn propensity scale. J. Mol. Biol. 293:807-814.
    • (1999) J. Mol. Biol , vol.293 , pp. 807-814
    • Monne, M.1    Nilsson, I.2    Elofsson, A.3    von Heijne, G.4
  • 44
    • 0027255262 scopus 로고
    • Unusual microtubule-dependent endocytosis mechanisms triggered by Campylobacter jejuni and Citrobacter freundii
    • Oelschlaeger, T. A., P. Guerry, and D. J. Kopecko. 1993. Unusual microtubule-dependent endocytosis mechanisms triggered by Campylobacter jejuni and Citrobacter freundii. Proc. Natl. Acad. Sci. USA 90:6884-6888.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6884-6888
    • Oelschlaeger, T.A.1    Guerry, P.2    Kopecko, D.J.3
  • 45
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
    • Rebbapragada, A., M. S. Johnson, G. P. Harding, A. J. Zuccarelli, H. M. Fletcher, I. B. Zhulin, and B. L. Taylor. 1997. The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Proc. Natl. Acad. Sci. USA 94:10541-10546.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5    Zhulin, I.B.6    Taylor, B.L.7
  • 47
    • 0032539854 scopus 로고    scopus 로고
    • Computational learning reveals coiled coil-like motifs in histidine kinase linker domains
    • Singh, M., B. Berger, P. S. Kim, J. M. Berger, and A. G. Cochran. 1998. Computational learning reveals coiled coil-like motifs in histidine kinase linker domains. Proc. Natl. Acad. Sci. USA 95:2738-2743.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2738-2743
    • Singh, M.1    Berger, B.2    Kim, P.S.3    Berger, J.M.4    Cochran, A.G.5
  • 48
    • 3242885338 scopus 로고    scopus 로고
    • Song, Y. C., S. Jin, H. Louie, D. Ng, R. Lau, Y. Zhang, R. Weerasekera, S. Al Rashid, 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.
    • Song, Y. C., S. Jin, H. Louie, D. Ng, R. Lau, Y. Zhang, R. Weerasekera, S. Al Rashid, 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.
  • 49
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • Szymanski, C. M., D. H. Burr, and P. Guerry. 2002. Campylobacter protein glycosylation affects host cell interactions. Infect. Immun. 70:2242-2244.
    • (2002) Infect. Immun , vol.70 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 50
    • 34548356914 scopus 로고    scopus 로고
    • Aer on the inside looking out: Paradigm for a PAS-HAMP role in sensing oxygen, redox and energy
    • Taylor, B. L. 2007. Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy. Mol. Microbiol. 65:1415-1424.
    • (2007) Mol. Microbiol , vol.65 , pp. 1415-1424
    • Taylor, B.L.1
  • 51
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 52
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 54
    • 40449120005 scopus 로고    scopus 로고
    • Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer
    • Watts, K. J., M. S. Johnson, and B. L. Taylor. 2008. Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer. J. Bacteriol. 190:2118-2127.
    • (2008) J. Bacteriol , vol.190 , pp. 2118-2127
    • Watts, K.J.1    Johnson, M.S.2    Taylor, B.L.3
  • 55
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner, M. P., G. L. Costa, W. Schoettlin, J. Cline, E. Mathur, and J. C. Bauer. 1994. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151:119-123.
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 56
    • 0027327182 scopus 로고
    • Construction of new Campylobacter cloning vectors and a new mutational cat cassette
    • Yao, R., R. A. Alm, T. J. Trust, and P. Guerry. 1993. Construction of new Campylobacter cloning vectors and a new mutational cat cassette. Gene 130:127-130.
    • (1993) Gene , vol.130 , pp. 127-130
    • Yao, R.1    Alm, R.A.2    Trust, T.J.3    Guerry, P.4
  • 57
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: Molecular biology and pathogenesis
    • Young, K. T., L. M. Davis, and V. J. DiRita. 2007. Campylobacter jejuni: molecular biology and pathogenesis. Nat. Rev. Microbiol. 5:665-679.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    DiRita, V.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.