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Volumn 93, Issue 6, 2014, Pages 1224-1245

Utilization of host-derived cysteine-containing peptides overcomes the restricted sulphur metabolism of Campylobacter jejuni

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CAMPYLOBACTER PEPTIDE TRANSPORTER A PROTEIN; CYSTEINE; GLUTATHIONE; METHIONINE; SULFIDE; SULFUR; THIOSULFATE; UNCLASSIFIED DRUG; CARRIER PROTEIN; CPTA PROTEIN, BACTERIA; PEPTIDE PERMEASE; PROTEINASE;

EID: 84908407307     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12732     Document Type: Article
Times cited : (32)

References (99)
  • 1
    • 84877829941 scopus 로고    scopus 로고
    • Microbial quest for food in vivo: 'nutritional virulence' as an emerging paradigm
    • Abu Kwaik, Y., and Bumann, D. (2013) Microbial quest for food in vivo: 'nutritional virulence' as an emerging paradigm. Cell Microbiol 15: 882-890.
    • (2013) Cell Microbiol , vol.15 , pp. 882-890
    • Abu Kwaik, Y.1    Bumann, D.2
  • 2
    • 0016921170 scopus 로고
    • Intestinal phase of protein assimilation in man
    • Adibi, S.A. (1976) Intestinal phase of protein assimilation in man. Am J Clin Nutr 29: 205-215.
    • (1976) Am J Clin Nutr , vol.29 , pp. 205-215
    • Adibi, S.A.1
  • 3
    • 79952101897 scopus 로고    scopus 로고
    • MCLMAN, a new minimal medium for Campylobacter jejuni NCTC 11168
    • Alazzam, B., Bonnassie-Rouxin, S., Dufour, V., and Ermel, G. (2011) MCLMAN, a new minimal medium for Campylobacter jejuni NCTC 11168. Res Microbiol 162: 173-179.
    • (2011) Res Microbiol , vol.162 , pp. 173-179
    • Alazzam, B.1    Bonnassie-Rouxin, S.2    Dufour, V.3    Ermel, G.4
  • 4
    • 59249084463 scopus 로고    scopus 로고
    • Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis
    • Alkhuder, K., Meibom, K.L., Dubail, I., Dupuis, M., and Charbit, A. (2009) Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis. PLoS Pathog 5: e1000284.
    • (2009) PLoS Pathog , vol.5 , pp. e1000284
    • Alkhuder, K.1    Meibom, K.L.2    Dubail, I.3    Dupuis, M.4    Charbit, A.5
  • 6
    • 84884169299 scopus 로고    scopus 로고
    • Molecular methods to investigate adhesion, transmigration, invasion and intracellular survival of the foodborne pathogen Campylobacter jejuni
    • Backert, S., and Hofreuter, D. (2013) Molecular methods to investigate adhesion, transmigration, invasion and intracellular survival of the foodborne pathogen Campylobacter jejuni. J Microbiol Methods 95: 8-23.
    • (2013) J Microbiol Methods , vol.95 , pp. 8-23
    • Backert, S.1    Hofreuter, D.2
  • 7
    • 34548658907 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase has a role in the persistent colonization of the avian gut by Campylobacter jejuni
    • Barnes, I.H., Bagnall, M.C., Browning, D.D., Thompson, S.A., Manning, G., and Newell, D.G. (2007) Gamma-glutamyl transpeptidase has a role in the persistent colonization of the avian gut by Campylobacter jejuni. Microb Pathog 43: 198-207.
    • (2007) Microb Pathog , vol.43 , pp. 198-207
    • Barnes, I.H.1    Bagnall, M.C.2    Browning, D.D.3    Thompson, S.A.4    Manning, G.5    Newell, D.G.6
  • 8
    • 84655167617 scopus 로고    scopus 로고
    • Chemotactic behavior of Campylobacter spp. in function of different temperatures (37°C and 42°C)
    • Baserisalehi, M., and Bahador, N. (2011) Chemotactic behavior of Campylobacter spp. in function of different temperatures (37°C and 42°C). Anaerobe 17: 459-462.
    • (2011) Anaerobe , vol.17 , pp. 459-462
    • Baserisalehi, M.1    Bahador, N.2
  • 10
    • 0022642470 scopus 로고
    • Extraintestinal Campylobacter jejuni and Campylobacter coli infections: host factors and strain characteristics
    • Blaser, M.J., Perez, G.P., Smith, P.F., Patton, C., Tenover, F.C., Lastovica, A.J., and Wang, W.I. (1986) Extraintestinal Campylobacter jejuni and Campylobacter coli infections: host factors and strain characteristics. J Infect Dis 153: 552-559.
    • (1986) J Infect Dis , vol.153 , pp. 552-559
    • Blaser, M.J.1    Perez, G.P.2    Smith, P.F.3    Patton, C.4    Tenover, F.C.5    Lastovica, A.J.6    Wang, W.I.7
  • 11
    • 57649123534 scopus 로고    scopus 로고
    • Global phenotypic characterization of bacteria
    • Bochner, B.R. (2009) Global phenotypic characterization of bacteria. FEMS Microbiol Rev 33: 191-205.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 191-205
    • Bochner, B.R.1
  • 12
    • 84864681437 scopus 로고    scopus 로고
    • Rapid paracellular transmigration of Campylobacter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin
    • Boehm, M., Hoy, B., Rohde, M., Tegtmeyer, N., Baek, K.T., Oyarzabal, O.A., etal. (2012) Rapid paracellular transmigration of Campylobacter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin. Gut Pathog 4: 3.
    • (2012) Gut Pathog , vol.4 , pp. 3
    • Boehm, M.1    Hoy, B.2    Rohde, M.3    Tegtmeyer, N.4    Baek, K.T.5    Oyarzabal, O.A.6
  • 13
    • 20444380287 scopus 로고    scopus 로고
    • The HtrA protease of Campylobacter jejuni is required for heat and oxygen tolerance and for optimal interaction with human epithelial cells
    • Brondsted, L., Andersen, M.T., Parker, M., Jorgensen, K., and Ingmer, H. (2005) The HtrA protease of Campylobacter jejuni is required for heat and oxygen tolerance and for optimal interaction with human epithelial cells. Appl Environ Microbiol 71: 3205-3212.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3205-3212
    • Brondsted, L.1    Andersen, M.T.2    Parker, M.3    Jorgensen, K.4    Ingmer, H.5
  • 14
    • 3543019723 scopus 로고    scopus 로고
    • AtOPT6 transports glutathione derivatives and is induced by primisulfuron
    • Cagnac, O., Bourbouloux, A., Chakrabarty, D., Zhang, M.Y., and Delrot, S. (2004) AtOPT6 transports glutathione derivatives and is induced by primisulfuron. Plant Physiol 135: 1378-1387.
    • (2004) Plant Physiol , vol.135 , pp. 1378-1387
    • Cagnac, O.1    Bourbouloux, A.2    Chakrabarty, D.3    Zhang, M.Y.4    Delrot, S.5
  • 16
    • 0036180411 scopus 로고    scopus 로고
    • Role of glutathione metabolism of Treponema denticola in bacterial growth and virulence expression
    • Chu, L., Dong, Z., Xu, X., Cochran, D.L., and Ebersole, J.L. (2002) Role of glutathione metabolism of Treponema denticola in bacterial growth and virulence expression. Infect Immun 70: 1113-1120.
    • (2002) Infect Immun , vol.70 , pp. 1113-1120
    • Chu, L.1    Dong, Z.2    Xu, X.3    Cochran, D.L.4    Ebersole, J.L.5
  • 17
    • 50349095675 scopus 로고    scopus 로고
    • A 52-kDa leucyl aminopeptidase from Treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism
    • Chu, L., Lai, Y., Xu, X., Eddy, S., Yang, S., Song, L., and Kolodrubetz, D. (2008) A 52-kDa leucyl aminopeptidase from Treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism. J Biol Chem 283: 19351-19358.
    • (2008) J Biol Chem , vol.283 , pp. 19351-19358
    • Chu, L.1    Lai, Y.2    Xu, X.3    Eddy, S.4    Yang, S.5    Song, L.6    Kolodrubetz, D.7
  • 18
    • 80555127486 scopus 로고    scopus 로고
    • Redox biology of the intestine
    • Circu, M.L., and Aw, T.Y. (2011) Redox biology of the intestine. Free Radic Res 45: 1245-1266.
    • (2011) Free Radic Res , vol.45 , pp. 1245-1266
    • Circu, M.L.1    Aw, T.Y.2
  • 19
    • 37349055095 scopus 로고    scopus 로고
    • Contribution of conserved ATP-dependent proteases of Campylobacter jejuni to stress tolerance and virulence
    • Cohn, M.T., Ingmer, H., Mulholland, F., Jorgensen, K., Wells, J.M., and Brondsted, L. (2007) Contribution of conserved ATP-dependent proteases of Campylobacter jejuni to stress tolerance and virulence. Appl Environ Microbiol 73: 7803-7813.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7803-7813
    • Cohn, M.T.1    Ingmer, H.2    Mulholland, F.3    Jorgensen, K.4    Wells, J.M.5    Brondsted, L.6
  • 20
    • 84875802555 scopus 로고    scopus 로고
    • Salmonella enterica: a surprisingly well-adapted intracellular lifestyle
    • Dandekar, T., Astrid, F., Jasmin, P., and Hensel, M. (2012) Salmonella enterica: a surprisingly well-adapted intracellular lifestyle. Front Microbiol 3: 164.
    • (2012) Front Microbiol , vol.3 , pp. 164
    • Dandekar, T.1    Astrid, F.2    Jasmin, P.3    Hensel, M.4
  • 21
    • 33646720881 scopus 로고    scopus 로고
    • From bacteria to man: archaic proton-dependent peptide transporters at work
    • Daniel, H., Spanier, B., Kottra, G., and Weitz, D. (2006) From bacteria to man: archaic proton-dependent peptide transporters at work. Physiology (Bethesda) 21: 93-102.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 93-102
    • Daniel, H.1    Spanier, B.2    Kottra, G.3    Weitz, D.4
  • 22
    • 22644444206 scopus 로고    scopus 로고
    • Specificity and selectivity determinants of peptide transport in Lactococcus lactis and other microorganisms
    • Doeven, M.K., Kok, J., and Poolman, B. (2005) Specificity and selectivity determinants of peptide transport in Lactococcus lactis and other microorganisms. Mol Microbiol 57: 640-649.
    • (2005) Mol Microbiol , vol.57 , pp. 640-649
    • Doeven, M.K.1    Kok, J.2    Poolman, B.3
  • 23
    • 77749246046 scopus 로고    scopus 로고
    • In Helicobacter pylori, LuxS is a key enzyme in cysteine provision through a reverse transsulfuration pathway
    • Doherty, N.C., Shen, F., Halliday, N.M., Barrett, D.A., Hardie, K.R., Winzer, K., and Atherton, J.C. (2010) In Helicobacter pylori, LuxS is a key enzyme in cysteine provision through a reverse transsulfuration pathway. J Bacteriol 192: 1184-1192.
    • (2010) J Bacteriol , vol.192 , pp. 1184-1192
    • Doherty, N.C.1    Shen, F.2    Halliday, N.M.3    Barrett, D.A.4    Hardie, K.R.5    Winzer, K.6    Atherton, J.C.7
  • 24
    • 33746622949 scopus 로고    scopus 로고
    • Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria
    • Dominy, J.E., Jr, Simmons, C.R., Karplus, P.A., Gehring, A.M., and Stipanuk, M.H. (2006) Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria. J Bacteriol 188: 5561-5569.
    • (2006) J Bacteriol , vol.188 , pp. 5561-5569
    • Dominy Jr, J.E.1    Simmons, C.R.2    Karplus, P.A.3    Gehring, A.M.4    Stipanuk, M.H.5
  • 25
    • 40749150035 scopus 로고    scopus 로고
    • Comparison of carbon nutrition for pathogenic and commensal Escherichia coli strains in the mouse intestine
    • Fabich, A.J., Jones, S.A., Chowdhury, F.Z., Cernosek, A., Anderson, A., Smalley, D., etal. (2008) Comparison of carbon nutrition for pathogenic and commensal Escherichia coli strains in the mouse intestine. Infect Immun 76: 1143-1152.
    • (2008) Infect Immun , vol.76 , pp. 1143-1152
    • Fabich, A.J.1    Jones, S.A.2    Chowdhury, F.Z.3    Cernosek, A.4    Anderson, A.5    Smalley, D.6
  • 26
    • 20044387762 scopus 로고    scopus 로고
    • Major structural differences and novel potential virulence mechanisms from the genomes of multiple campylobacter species
    • Fouts, D.E., Mongodin, E.F., Mandrell, R.E., Miller, W.G., Rasko, D.A., Ravel, J., etal. (2005) Major structural differences and novel potential virulence mechanisms from the genomes of multiple campylobacter species. PLoS Biol 3: e15.
    • (2005) PLoS Biol , vol.3 , pp. e15
    • Fouts, D.E.1    Mongodin, E.F.2    Mandrell, R.E.3    Miller, W.G.4    Rasko, D.A.5    Ravel, J.6
  • 27
    • 84861214451 scopus 로고    scopus 로고
    • Peptidoglycan-modifying enzyme Pgp1 is required for helical cell shape and pathogenicity traits in Campylobacter jejuni
    • Frirdich, E., Biboy, J., Adams, C., Lee, J., Ellermeier, J., Gielda, L.D., etal. (2012) Peptidoglycan-modifying enzyme Pgp1 is required for helical cell shape and pathogenicity traits in Campylobacter jejuni. PLoS Pathog 8: e1002602.
    • (2012) PLoS Pathog , vol.8 , pp. e1002602
    • Frirdich, E.1    Biboy, J.2    Adams, C.3    Lee, J.4    Ellermeier, J.5    Gielda, L.D.6
  • 28
    • 84897014355 scopus 로고    scopus 로고
    • Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties, and provides the substrate for the DL-carboxypeptidase Pgp1
    • Frirdich, E., Vermeulen, J., Biboy, J., Soares, F., Taveirne, M.E., Johnson, J.G., etal. (2014) Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties, and provides the substrate for the DL-carboxypeptidase Pgp1. J Biol Chem 289: 8007-8018.
    • (2014) J Biol Chem , vol.289 , pp. 8007-8018
    • Frirdich, E.1    Vermeulen, J.2    Biboy, J.3    Soares, F.4    Taveirne, M.E.5    Johnson, J.G.6
  • 29
    • 0031024840 scopus 로고    scopus 로고
    • Identification of a functional homolog of the Escherichia coli and Salmonella typhimurium cysM gene encoding O-acetylserine sulfhydrylase B in Campylobacter jejuni
    • Garvis, S.G., Tipton, S.L., and Konkel, M.E. (1997) Identification of a functional homolog of the Escherichia coli and Salmonella typhimurium cysM gene encoding O-acetylserine sulfhydrylase B in Campylobacter jejuni. Gene 185: 63-67.
    • (1997) Gene , vol.185 , pp. 63-67
    • Garvis, S.G.1    Tipton, S.L.2    Konkel, M.E.3
  • 30
    • 79952379428 scopus 로고    scopus 로고
    • Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter
    • Gilbreath, J.J., Cody, W.L., Merrell, D.S., and Hendrixson, D.R. (2011) Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter. Microbiol Mol Biol Rev 75: 84-132.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 84-132
    • Gilbreath, J.J.1    Cody, W.L.2    Merrell, D.S.3    Hendrixson, D.R.4
  • 31
    • 79953697080 scopus 로고    scopus 로고
    • Evolution of the oligopeptide transporter family
    • Gomolplitinant, K.M., and Saier, M.H., Jr (2011) Evolution of the oligopeptide transporter family. J Membr Biol 240: 89-110.
    • (2011) J Membr Biol , vol.240 , pp. 89-110
    • Gomolplitinant, K.M.1    Saier Jr, M.H.2
  • 32
    • 82155168575 scopus 로고    scopus 로고
    • Closely related Campylobacter jejuni strains from different sources reveal a generalist rather than a specialist lifestyle
    • Gripp, E., Hlahla, D., Didelot, X., Kops, F., Maurischat, S., Tedin, K., etal. (2011) Closely related Campylobacter jejuni strains from different sources reveal a generalist rather than a specialist lifestyle. BMC Genomics 12: 584.
    • (2011) BMC Genomics , vol.12 , pp. 584
    • Gripp, E.1    Hlahla, D.2    Didelot, X.3    Kops, F.4    Maurischat, S.5    Tedin, K.6
  • 33
    • 45149111730 scopus 로고    scopus 로고
    • Amino acid-dependent growth of Campylobacter jejuni: key roles for aspartase (AspA) under microaerobic and oxygen-limited conditions and identification of AspB (Cj0762), essential for growth on glutamate
    • Guccione, E., Leon-Kempis Mdel, R., Pearson, B.M., Hitchin, E., Mulholland, F., van Diemen, P.M., etal. (2008) Amino acid-dependent growth of Campylobacter jejuni: key roles for aspartase (AspA) under microaerobic and oxygen-limited conditions and identification of AspB (Cj0762), essential for growth on glutamate. Mol Microbiol 69: 77-93.
    • (2008) Mol Microbiol , vol.69 , pp. 77-93
    • Guccione, E.1    Leon-Kempis Mdel, R.2    Pearson, B.M.3    Hitchin, E.4    Mulholland, F.5    van Diemen, P.M.6
  • 34
    • 1942532926 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract
    • Hendrixson, D.R., and DiRita, V.J. (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
  • 35
    • 33746630455 scopus 로고    scopus 로고
    • Unique features of a highly pathogenic Campylobacter jejuni strain
    • Hofreuter, D., Tsai, J., Watson, R.O., Novik, V., Altman, B., Benitez, M., etal. (2006) Unique features of a highly pathogenic Campylobacter jejuni strain. Infect Immun 74: 4694-4707.
    • (2006) Infect Immun , vol.74 , pp. 4694-4707
    • Hofreuter, D.1    Tsai, J.2    Watson, R.O.3    Novik, V.4    Altman, B.5    Benitez, M.6
  • 36
    • 55249102409 scopus 로고    scopus 로고
    • Metabolic diversity in Campylobacter jejuni enhances specific tissue colonization
    • Hofreuter, D., Novik, V., and Galan, J.E. (2008) Metabolic diversity in Campylobacter jejuni enhances specific tissue colonization. Cell Host Microbe 4: 425-433.
    • (2008) Cell Host Microbe , vol.4 , pp. 425-433
    • Hofreuter, D.1    Novik, V.2    Galan, J.E.3
  • 37
    • 84870619710 scopus 로고    scopus 로고
    • Contribution of amino acid catabolism to the tissue specific persistence of Campylobacter jejuni in a murine colonization model
    • Hofreuter, D., Mohr, J., Wensel, O., Rademacher, S., Schreiber, K., Schomburg, D., etal. (2012) Contribution of amino acid catabolism to the tissue specific persistence of Campylobacter jejuni in a murine colonization model. PLoS ONE 7: e50699.
    • (2012) PLoS ONE , vol.7 , pp. e50699
    • Hofreuter, D.1    Mohr, J.2    Wensel, O.3    Rademacher, S.4    Schreiber, K.5    Schomburg, D.6
  • 38
    • 84861912744 scopus 로고    scopus 로고
    • Hydrogenase activity in the food-borne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikLMNOP) and is SlyD independent
    • Howlett, R.M., Hughes, B.M., Hitchcock, A., and Kelly, D.J. (2012) Hydrogenase activity in the food-borne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikLMNOP) and is SlyD independent. Microbiology 158: 1645-1655.
    • (2012) Microbiology , vol.158 , pp. 1645-1655
    • Howlett, R.M.1    Hughes, B.M.2    Hitchcock, A.3    Kelly, D.J.4
  • 39
    • 0023880696 scopus 로고
    • Chemotactic behavior of Campylobacter jejuni
    • Hugdahl, M.B., Beery, J.T., and Doyle, M.P. (1988) Chemotactic behavior of Campylobacter jejuni. Infect Immun 56: 1560-1566.
    • (1988) Infect Immun , vol.56 , pp. 1560-1566
    • Hugdahl, M.B.1    Beery, J.T.2    Doyle, M.P.3
  • 40
    • 0037298773 scopus 로고    scopus 로고
    • Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver
    • Josch, C., Klotz, L.O., and Sies, H. (2003) Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver. Biol Chem 384: 213-218.
    • (2003) Biol Chem , vol.384 , pp. 213-218
    • Josch, C.1    Klotz, L.O.2    Sies, H.3
  • 41
    • 67649756725 scopus 로고    scopus 로고
    • Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases
    • Kaur, H., Kumar, C., Junot, C., Toledano, M.B., and Bachhawat, A.K. (2009) Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases. J Biol Chem 284: 14493-14502.
    • (2009) J Biol Chem , vol.284 , pp. 14493-14502
    • Kaur, H.1    Kumar, C.2    Junot, C.3    Toledano, M.B.4    Bachhawat, A.K.5
  • 42
    • 79551680796 scopus 로고    scopus 로고
    • Enteric pathogen exploitation of the microbiota-generated nutrient environment of the gut
    • Keeney, K.M., and Finlay, B.B. (2011) Enteric pathogen exploitation of the microbiota-generated nutrient environment of the gut. Curr Opin Microbiol 14: 92-98.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 92-98
    • Keeney, K.M.1    Finlay, B.B.2
  • 43
    • 84898059539 scopus 로고    scopus 로고
    • Hemerythrins in the microaerophilic bacterium Campylobacter jejuni help protect key iron-sulphur cluster enzymes from oxidative damage
    • Kendall, J.J., Barrero-Tobon, A.M., Hendrixson, D.R., and Kelly, D.J. (2014) Hemerythrins in the microaerophilic bacterium Campylobacter jejuni help protect key iron-sulphur cluster enzymes from oxidative damage. Environ Microbiol 16: 1105-1121.
    • (2014) Environ Microbiol , vol.16 , pp. 1105-1121
    • Kendall, J.J.1    Barrero-Tobon, A.M.2    Hendrixson, D.R.3    Kelly, D.J.4
  • 44
    • 0035015118 scopus 로고    scopus 로고
    • Bacterial transporters for sulfate and organosulfur compounds
    • Kertesz, M.A. (2001) Bacterial transporters for sulfate and organosulfur compounds. Res Microbiol 152: 279-290.
    • (2001) Res Microbiol , vol.152 , pp. 279-290
    • Kertesz, M.A.1
  • 45
  • 46
    • 0015523888 scopus 로고
    • The purification and subunit structure of cysteine desulfhydrase from Salmonella typhimurium
    • Kredich, N.M., Keenan, B.S., and Foote, L.J. (1972) The purification and subunit structure of cysteine desulfhydrase from Salmonella typhimurium. J Biol Chem 247: 7157-7162.
    • (1972) J Biol Chem , vol.247 , pp. 7157-7162
    • Kredich, N.M.1    Keenan, B.S.2    Foote, L.J.3
  • 47
    • 33745275142 scopus 로고    scopus 로고
    • The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids
    • Leon-Kempis Mdel, R., Guccione, E., Mulholland, F., Williamson, M.P., and Kelly, D.J. (2006) The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids. Mol Microbiol 60: 1262-1275.
    • (2006) Mol Microbiol , vol.60 , pp. 1262-1275
    • Leon-Kempis Mdel, R.1    Guccione, E.2    Mulholland, F.3    Williamson, M.P.4    Kelly, D.J.5
  • 48
    • 70350458737 scopus 로고    scopus 로고
    • Atypical roles for Campylobacter jejuni amino acid ATP binding cassette transporter components PaqP and PaqQ in bacterial stress tolerance and pathogen-host cell dynamics
    • Lin, A.E., Krastel, K., Hobb, R.I., Thompson, S.A., Cvitkovitch, D.G., and Gaynor, E.C. (2009) Atypical roles for Campylobacter jejuni amino acid ATP binding cassette transporter components PaqP and PaqQ in bacterial stress tolerance and pathogen-host cell dynamics. Infect Immun 77: 4912-4924.
    • (2009) Infect Immun , vol.77 , pp. 4912-4924
    • Lin, A.E.1    Krastel, K.2    Hobb, R.I.3    Thompson, S.A.4    Cvitkovitch, D.G.5    Gaynor, E.C.6
  • 50
    • 84875618987 scopus 로고    scopus 로고
    • Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria
    • Liu, Y.W., Denkmann, K., Kosciow, K., Dahl, C., and Kelly, D.J. (2013) Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria. Mol Microbiol 88: 173-188.
    • (2013) Mol Microbiol , vol.88 , pp. 173-188
    • Liu, Y.W.1    Denkmann, K.2    Kosciow, K.3    Dahl, C.4    Kelly, D.J.5
  • 51
    • 84890103984 scopus 로고    scopus 로고
    • Modification of intestinal microbiota and its consequences for innate immune response in the pathogenesis of campylobacteriosis
    • Masanta, W.O., Heimesaat, M.M., Bereswill, S., Tareen, A.M., Lugert, R., Gross, U., and Zautner, A.E. (2013) Modification of intestinal microbiota and its consequences for innate immune response in the pathogenesis of campylobacteriosis. Clin Dev Immunol 2013: 526860.
    • (2013) Clin Dev Immunol , vol.2013 , pp. 526860
    • Masanta, W.O.1    Heimesaat, M.M.2    Bereswill, S.3    Tareen, A.M.4    Lugert, R.5    Gross, U.6    Zautner, A.E.7
  • 53
    • 0030932839 scopus 로고    scopus 로고
    • Pyruvate metabolism in Campylobacter spp.
    • Mendz, G.L., Ball, G.E., and Meek, D.J. (1997) Pyruvate metabolism in Campylobacter spp. Biochim Biophys Acta 1334: 291-302.
    • (1997) Biochim Biophys Acta , vol.1334 , pp. 291-302
    • Mendz, G.L.1    Ball, G.E.2    Meek, D.J.3
  • 54
    • 43349108455 scopus 로고    scopus 로고
    • The complete genome sequence and analysis of the epsilonproteobacterium Arcobacter butzleri
    • Miller, W.G., Parker, C.T., Rubenfield, M., Mendz, G.L., Wosten, M.M., Ussery, D.W., etal. (2007) The complete genome sequence and analysis of the epsilonproteobacterium Arcobacter butzleri. PLoS ONE 2: e1358.
    • (2007) PLoS ONE , vol.2 , pp. e1358
    • Miller, W.G.1    Parker, C.T.2    Rubenfield, M.3    Mendz, G.L.4    Wosten, M.M.5    Ussery, D.W.6
  • 55
    • 4444376017 scopus 로고    scopus 로고
    • The pattern and kinetics of substrate metabolism of Campylobacter jejuni and Campylobacter coli
    • Mohammed, K.A., Miles, R.J., and Halablab, M.A. (2004) The pattern and kinetics of substrate metabolism of Campylobacter jejuni and Campylobacter coli. Lett Appl Microbiol 39: 261-266.
    • (2004) Lett Appl Microbiol , vol.39 , pp. 261-266
    • Mohammed, K.A.1    Miles, R.J.2    Halablab, M.A.3
  • 56
    • 21244445047 scopus 로고    scopus 로고
    • An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein
    • Müller, A., Thomas, G.H., Horler, R., Brannigan, J.A., Blagova, E., Levdikov, V.M., etal. (2005) An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein. Mol Microbiol 57: 143-155.
    • (2005) Mol Microbiol , vol.57 , pp. 143-155
    • Müller, A.1    Thomas, G.H.2    Horler, R.3    Brannigan, J.A.4    Blagova, E.5    Levdikov, V.M.6
  • 57
    • 79951635444 scopus 로고    scopus 로고
    • Phenotypic and genotypic evidence for L-fucose utilization by Campylobacter jejuni
    • Muraoka, W.T., and Zhang, Q. (2011) Phenotypic and genotypic evidence for L-fucose utilization by Campylobacter jejuni. J Bacteriol 193: 1065-1075.
    • (2011) J Bacteriol , vol.193 , pp. 1065-1075
    • Muraoka, W.T.1    Zhang, Q.2
  • 58
    • 13444259982 scopus 로고    scopus 로고
    • A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni
    • Myers, J.D., and Kelly, D.J. (2005) A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni. Microbiology 151: 233-242.
    • (2005) Microbiology , vol.151 , pp. 233-242
    • Myers, J.D.1    Kelly, D.J.2
  • 59
    • 77955294240 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells
    • Novik, V., Hofreuter, D., and Galan, J.E. (2010) Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells. Infect Immun 78: 3540-3553.
    • (2010) Infect Immun , vol.78 , pp. 3540-3553
    • Novik, V.1    Hofreuter, D.2    Galan, J.E.3
  • 60
    • 77952905782 scopus 로고    scopus 로고
    • The L-cysteine/L-cystine shuttle system provides reducing equivalents to the periplasm in Escherichia coli
    • Ohtsu, I., Wiriyathanawudhiwong, N., Morigasaki, S., Nakatani, T., Kadokura, H., and Takagi, H. (2010) The L-cysteine/L-cystine shuttle system provides reducing equivalents to the periplasm in Escherichia coli. J Biol Chem 285: 17479-17487.
    • (2010) J Biol Chem , vol.285 , pp. 17479-17487
    • Ohtsu, I.1    Wiriyathanawudhiwong, N.2    Morigasaki, S.3    Nakatani, T.4    Kadokura, H.5    Takagi, H.6
  • 61
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences
    • Parkhill, J., Wren, B.W., Mungall, K., Ketley, J.M., Churcher, C., Basham, D., etal. (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403: 665-668.
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1    Wren, B.W.2    Mungall, K.3    Ketley, J.M.4    Churcher, C.5    Basham, D.6
  • 62
    • 0031909560 scopus 로고    scopus 로고
    • Campylobacter jejuni 72Dz/92 cjaC gene coding 28 kDa immunopositive protein, a homologue of the solute-binding components of the ABC transport system
    • Pawelec, D., Jakubowska-Mroz, J., and Jagusztyn-Krynicka, E.K. (1998) Campylobacter jejuni 72Dz/92 cjaC gene coding 28 kDa immunopositive protein, a homologue of the solute-binding components of the ABC transport system. Lett Appl Microbiol 26: 69-76.
    • (1998) Lett Appl Microbiol , vol.26 , pp. 69-76
    • Pawelec, D.1    Jakubowska-Mroz, J.2    Jagusztyn-Krynicka, E.K.3
  • 63
    • 0027293062 scopus 로고
    • PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog of the binding component in gram-negative nutrient transport systems
    • Pei, Z., and Blaser, M.J. (1993) PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog of the binding component in gram-negative nutrient transport systems. J Biol Chem 268: 18717-18725.
    • (1993) J Biol Chem , vol.268 , pp. 18717-18725
    • Pei, Z.1    Blaser, M.J.2
  • 64
    • 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., Burucoa, C., Grignon, B., Baqar, S., Huang, X.Z., Kopecko, D.J., etal. (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
  • 65
    • 33846036912 scopus 로고    scopus 로고
    • Growth of Campylobacter jejuni on nitrate and nitrite: electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress
    • Pittman, M.S., Elvers, K.T., Lee, L., Jones, M.A., Poole, R.K., Park, S.F., and Kelly, D.J. (2007) Growth of Campylobacter jejuni on nitrate and nitrite: electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress. Mol Microbiol 63: 575-590.
    • (2007) Mol Microbiol , vol.63 , pp. 575-590
    • Pittman, M.S.1    Elvers, K.T.2    Lee, L.3    Jones, M.A.4    Poole, R.K.5    Park, S.F.6    Kelly, D.J.7
  • 66
    • 84880293371 scopus 로고    scopus 로고
    • Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells
    • Rasmussen, J.J., Vegge, C.S., Frokiaer, H., Howlett, R.M., Krogfelt, K.A., Kelly, D.J., and Ingmer, H. (2013) Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells. J Med Microbiol 62: 1135-1143.
    • (2013) J Med Microbiol , vol.62 , pp. 1135-1143
    • Rasmussen, J.J.1    Vegge, C.S.2    Frokiaer, H.3    Howlett, R.M.4    Krogfelt, K.A.5    Kelly, D.J.6    Ingmer, H.7
  • 67
    • 0028046168 scopus 로고
    • Characteristics of Helicobacter pylori growth in a defined medium and determination of its amino acid requirements
    • Reynolds, D.J., and Penn, C.W. (1994) Characteristics of Helicobacter pylori growth in a defined medium and determination of its amino acid requirements. Microbiology 140: 2649-2656.
    • (1994) Microbiology , vol.140 , pp. 2649-2656
    • Reynolds, D.J.1    Penn, C.W.2
  • 68
    • 80655125458 scopus 로고    scopus 로고
    • Analysis of the LIV system of Campylobacter jejuni reveals alternative roles for LivJ and LivK in commensalism beyond branched-chain amino acid transport
    • Ribardo, D.A., and Hendrixson, D.R. (2011) Analysis of the LIV system of Campylobacter jejuni reveals alternative roles for LivJ and LivK in commensalism beyond branched-chain amino acid transport. J Bacteriol 193: 6233-6243.
    • (2011) J Bacteriol , vol.193 , pp. 6233-6243
    • Ribardo, D.A.1    Hendrixson, D.R.2
  • 70
    • 0025980680 scopus 로고
    • Molecular and functional characterization of a carbon starvation gene of Escherichia coli
    • Schultz, J.E., and Matin, A. (1991) Molecular and functional characterization of a carbon starvation gene of Escherichia coli. J Mol Biol 218: 129-140.
    • (1991) J Mol Biol , vol.218 , pp. 129-140
    • Schultz, J.E.1    Matin, A.2
  • 71
    • 0035191633 scopus 로고    scopus 로고
    • Methionine-to-cysteine recycling in Klebsiella aerogenes
    • Seiflein, T.A., and Lawrence, J.G. (2001) Methionine-to-cysteine recycling in Klebsiella aerogenes. J Bacteriol 183: 336-346.
    • (2001) J Bacteriol , vol.183 , pp. 336-346
    • Seiflein, T.A.1    Lawrence, J.G.2
  • 72
    • 0033995794 scopus 로고    scopus 로고
    • Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction
    • Sekowska, A., Kung, H.F., and Danchin, A. (2000) Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction. J Mol Microbiol Biotechnol 2: 145-177.
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 145-177
    • Sekowska, A.1    Kung, H.F.2    Danchin, A.3
  • 73
    • 0031894921 scopus 로고    scopus 로고
    • Import and metabolism of glutathione by Streptococcus mutans
    • Sherrill, C., and Fahey, R.C. (1998) Import and metabolism of glutathione by Streptococcus mutans. J Bacteriol 180: 1454-1459.
    • (1998) J Bacteriol , vol.180 , pp. 1454-1459
    • Sherrill, C.1    Fahey, R.C.2
  • 76
    • 84878464404 scopus 로고    scopus 로고
    • Nutrient acquisition and metabolism by Campylobacter jejuni
    • Stahl, M., Butcher, J., and Stintzi, A. (2012) Nutrient acquisition and metabolism by Campylobacter jejuni. Front Cell Infect Microbiol 2: 5.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 5
    • Stahl, M.1    Butcher, J.2    Stintzi, A.3
  • 77
    • 79551687271 scopus 로고    scopus 로고
    • Mechanisms controlling pathogen colonization of the gut
    • Stecher, B., and Hardt, W.D. (2011) Mechanisms controlling pathogen colonization of the gut. Curr Opin Microbiol 14: 82-91.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 82-91
    • Stecher, B.1    Hardt, W.D.2
  • 78
    • 84876826859 scopus 로고    scopus 로고
    • Parallel exploitation of diverse host nutrients enhances Salmonella virulence
    • Steeb, B., Claudi, B., Burton, N.A., Tienz, P., Schmidt, A., Farhan, H., etal. (2013) Parallel exploitation of diverse host nutrients enhances Salmonella virulence. PLoS Pathog 9: e1003301.
    • (2013) PLoS Pathog , vol.9 , pp. e1003301
    • Steeb, B.1    Claudi, B.2    Burton, N.A.3    Tienz, P.4    Schmidt, A.5    Farhan, H.6
  • 79
    • 0027203198 scopus 로고
    • Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential
    • Suzuki, H., Hashimoto, W., and Kumagai, H. (1993) Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. J Bacteriol 175: 6038-6040.
    • (1993) J Bacteriol , vol.175 , pp. 6038-6040
    • Suzuki, H.1    Hashimoto, W.2    Kumagai, H.3
  • 80
    • 0035142004 scopus 로고    scopus 로고
    • Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12
    • Suzuki, H., Kamatani, S., Kim, E.S., and Kumagai, H. (2001) Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12. J Bacteriol 183: 1489-1490.
    • (2001) J Bacteriol , vol.183 , pp. 1489-1490
    • Suzuki, H.1    Kamatani, S.2    Kim, E.S.3    Kumagai, H.4
  • 81
    • 24344468705 scopus 로고    scopus 로고
    • The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette
    • Suzuki, H., Koyanagi, T., Izuka, S., Onishi, A., and Kumagai, H. (2005) The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J Bacteriol 187: 5861-5867.
    • (2005) J Bacteriol , vol.187 , pp. 5861-5867
    • Suzuki, H.1    Koyanagi, T.2    Izuka, S.3    Onishi, A.4    Kumagai, H.5
  • 82
    • 84866452259 scopus 로고    scopus 로고
    • How a sugary bug gets through the day: recent developments in understanding fundamental processes impacting Campylobacter jejuni pathogenesis
    • Szymanski, C.M., and Gaynor, E.C. (2012) How a sugary bug gets through the day: recent developments in understanding fundamental processes impacting Campylobacter jejuni pathogenesis. Gut Microbes 3: 135-144.
    • (2012) Gut Microbes , vol.3 , pp. 135-144
    • Szymanski, C.M.1    Gaynor, E.C.2
  • 83
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and Saier, M.H., Jr (1993) Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 57: 320-346.
    • (1993) Microbiol Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr, M.H.2
  • 84
    • 0023260148 scopus 로고
    • Naturally occurring auxotrophs of Campylobacter jejuni and Campylobacter coli
    • Tenover, F.C., and Patton, C.M. (1987) Naturally occurring auxotrophs of Campylobacter jejuni and Campylobacter coli. J Clin Microbiol 25: 1659-1661.
    • (1987) J Clin Microbiol , vol.25 , pp. 1659-1661
    • Tenover, F.C.1    Patton, C.M.2
  • 85
    • 78650800583 scopus 로고    scopus 로고
    • Two respiratory enzyme systems in Campylobacter jejuni NCTC 11168 contribute to growth on L-lactate
    • Thomas, M.T., Shepherd, M., Poole, R.K., van Vliet, A.H., Kelly, D.J., and Pearson, B.M. (2011) Two respiratory enzyme systems in Campylobacter jejuni NCTC 11168 contribute to growth on L-lactate. Environ Microbiol 13: 48-61.
    • (2011) Environ Microbiol , vol.13 , pp. 48-61
    • Thomas, M.T.1    Shepherd, M.2    Poole, R.K.3    van Vliet, A.H.4    Kelly, D.J.5    Pearson, B.M.6
  • 86
    • 0032914778 scopus 로고    scopus 로고
    • The bspA locus of Lactobacillus fermentum BR11 encodes an L-cystine uptake system
    • Turner, M.S., Woodberry, T., Hafner, L.M., and Giffard, P.M. (1999) The bspA locus of Lactobacillus fermentum BR11 encodes an L-cystine uptake system. J Bacteriol 181: 2192-2198.
    • (1999) J Bacteriol , vol.181 , pp. 2192-2198
    • Turner, M.S.1    Woodberry, T.2    Hafner, L.M.3    Giffard, P.M.4
  • 87
    • 68549120983 scopus 로고    scopus 로고
    • Energy taxis drives Campylobacter jejuni toward the most favorable conditions for growth
    • Vegge, C.S., Brondsted, L., Li, Y.P., Bang, D.D., and Ingmer, H. (2009) Energy taxis drives Campylobacter jejuni toward the most favorable conditions for growth. Appl Environ Microbiol 75: 5308-5314.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5308-5314
    • Vegge, C.S.1    Brondsted, L.2    Li, Y.P.3    Bang, D.D.4    Ingmer, H.5
  • 88
    • 0036126078 scopus 로고    scopus 로고
    • Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: an essential role for phosphoenolpyruvate carboxykinase
    • Velayudhan, J., and Kelly, D.J. (2002) Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: an essential role for phosphoenolpyruvate carboxykinase. Microbiology 148: 685-694.
    • (2002) Microbiology , vol.148 , pp. 685-694
    • Velayudhan, J.1    Kelly, D.J.2
  • 89
    • 0346881405 scopus 로고    scopus 로고
    • L-serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni
    • Velayudhan, J., Jones, M.A., Barrow, P.A., and Kelly, D.J. (2004) L-serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni. Infect Immun 72: 260-268.
    • (2004) Infect Immun , vol.72 , pp. 260-268
    • Velayudhan, J.1    Jones, M.A.2    Barrow, P.A.3    Kelly, D.J.4
  • 90
    • 77955828073 scopus 로고    scopus 로고
    • Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA
    • Vergauwen, B., Elegheert, J., Dansercoer, A., Devreese, B., and Savvides, S.N. (2010) Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA. Proc Natl Acad Sci USA 107: 13270-13275.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13270-13275
    • Vergauwen, B.1    Elegheert, J.2    Dansercoer, A.3    Devreese, B.4    Savvides, S.N.5
  • 91
    • 84880136182 scopus 로고    scopus 로고
    • Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans
    • Vergauwen, B., Verstraete, K., Senadheera, D.B., Dansercoer, A., Cvitkovitch, D.G., Guedon, E., and Savvides, S.N. (2013) Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans. Mol Microbiol 89: 288-303.
    • (2013) Mol Microbiol , vol.89 , pp. 288-303
    • Vergauwen, B.1    Verstraete, K.2    Senadheera, D.B.3    Dansercoer, A.4    Cvitkovitch, D.G.5    Guedon, E.6    Savvides, S.N.7
  • 92
    • 0032836048 scopus 로고    scopus 로고
    • Pathways of assimilative sulfur metabolism in Pseudomonas putida
    • Vermeij, P., and Kertesz, M.A. (1999) Pathways of assimilative sulfur metabolism in Pseudomonas putida. J Bacteriol 181: 5833-5837.
    • (1999) J Bacteriol , vol.181 , pp. 5833-5837
    • Vermeij, P.1    Kertesz, M.A.2
  • 93
    • 0035868449 scopus 로고    scopus 로고
    • The iron-induced ferredoxin FdxA of Campylobacter jejuni is involved in aerotolerance
    • van Vliet, A.H., Baillon, M.A., Penn, C.W., and Ketley, J.M. (2001) The iron-induced ferredoxin FdxA of Campylobacter jejuni is involved in aerotolerance. FEMS Microbiol Lett 196: 189-193.
    • (2001) FEMS Microbiol Lett , vol.196 , pp. 189-193
    • van Vliet, A.H.1    Baillon, M.A.2    Penn, C.W.3    Ketley, J.M.4
  • 94
    • 84860117196 scopus 로고    scopus 로고
    • Physiological implications of hydrogen sulfide: a whiff exploration that blossomed
    • Wang, R. (2012) Physiological implications of hydrogen sulfide: a whiff exploration that blossomed. Physiol Rev 92: 791-896.
    • (2012) Physiol Rev , vol.92 , pp. 791-896
    • Wang, R.1
  • 95
    • 67349169333 scopus 로고    scopus 로고
    • The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology
    • Weerakoon, D.R., Borden, N.J., Goodson, C.M., Grimes, J., and Olson, J.W. (2009) The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology. Microb Pathog 47: 8-15.
    • (2009) Microb Pathog , vol.47 , pp. 8-15
    • Weerakoon, D.R.1    Borden, N.J.2    Goodson, C.M.3    Grimes, J.4    Olson, J.W.5
  • 96
    • 14844327782 scopus 로고    scopus 로고
    • Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic Mycobacteria
    • Wheeler, P.R., Coldham, N.G., Keating, L., Gordon, S.V., Wooff, E.E., Parish, T., and Hewinson, R.G. (2005) Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic Mycobacteria. J Biol Chem 280: 8069-8078.
    • (2005) J Biol Chem , vol.280 , pp. 8069-8078
    • Wheeler, P.R.1    Coldham, N.G.2    Keating, L.3    Gordon, S.V.4    Wooff, E.E.5    Parish, T.6    Hewinson, R.G.7
  • 98
    • 61449258411 scopus 로고    scopus 로고
    • Metabolite and transcriptome analysis of Campylobacter jejuni in vitro growth reveals a stationary-phase physiological switch
    • Wright, J.A., Grant, A.J., Hurd, D., Harrison, M., Guccione, E.J., Kelly, D.J., and Maskell, D.J. (2009) Metabolite and transcriptome analysis of Campylobacter jejuni in vitro growth reveals a stationary-phase physiological switch. Microbiology 155: 80-94.
    • (2009) Microbiology , vol.155 , pp. 80-94
    • Wright, J.A.1    Grant, A.J.2    Hurd, D.3    Harrison, M.4    Guccione, E.J.5    Kelly, D.J.6    Maskell, D.J.7
  • 99
    • 48349133003 scopus 로고    scopus 로고
    • The Campylobacter jejuni/coli cjaA (cj0982c) gene encodes an N-glycosylated lipoprotein localized in the inner membrane
    • Wyszynska, A., Zycka, J., Godlewska, R., and Jagusztyn-Krynicka, E.K. (2008) The Campylobacter jejuni/coli cjaA (cj0982c) gene encodes an N-glycosylated lipoprotein localized in the inner membrane. Curr Microbiol 57: 181-188.
    • (2008) Curr Microbiol , vol.57 , pp. 181-188
    • Wyszynska, A.1    Zycka, J.2    Godlewska, R.3    Jagusztyn-Krynicka, E.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.