메뉴 건너뛰기




Volumn 11, Issue 10, 2012, Pages 4927-4938

Oxidative stress acts on special membrane proteins to reduce the viability of pseudomonas syringae pv tomato

Author keywords

cell viability; membrane subproteomics; oxidative stress; Pseudomonas syringae; transporters

Indexed keywords

50S RIBOSOMAL PROTEIN L2; ABC TRANSPORTER; ABC TRANSPORTER ATP BINDING PROTEIN; AMINO ACID ABC TRANSPORTER ATP BINDING PROTEIN; CARRIER PROTEIN; CYSTINE ABC TRANSPORTER ATP BINDING PROTEIN; ELONGATION FACTOR TU; FERRIC DICITRATE TRANSPORT PROTEIN FECA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE TYPE 1; LIPOPROTEIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; PORIN; PROTEIN OPRB; PROTEIN OPRD; PROTEIN OPRF; REACTIVE OXYGEN METABOLITE; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; TONB DEPENDENT SIDEROPHORE RECEPTOR; UNCLASSIFIED DRUG;

EID: 84867464212     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300446g     Document Type: Article
Times cited : (20)

References (69)
  • 1
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller, R. A.; Britigan, B. E. Role of oxidants in microbial pathophysiology Clin. Microbiol. Rev. 1997, 10 (1) 1-18
    • (1997) Clin. Microbiol. Rev. , vol.10 , Issue.1 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 2
    • 0033180574 scopus 로고    scopus 로고
    • Role of active oxygen species and NO in plant defence responses
    • Bolwell, G. P. Role of active oxygen species and NO in plant defence responses Curr. Opin. Plant. Biol. 1999, 2 (4) 287-294
    • (1999) Curr. Opin. Plant. Biol. , vol.2 , Issue.4 , pp. 287-294
    • Bolwell, G.P.1
  • 3
    • 0013431036 scopus 로고    scopus 로고
    • The Arabidopsis thaliana-Pseudomonas syringae interaction
    • Katagiri, F.; Thilmony, R.; He, S. Y. The Arabidopsis thaliana-Pseudomonas syringae interaction Arabidopsis Book 2002, 1, e0039
    • (2002) Arabidopsis Book , vol.1 , pp. 0039
    • Katagiri, F.1    Thilmony, R.2    He, S.Y.3
  • 4
    • 0033514307 scopus 로고    scopus 로고
    • The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi
    • Hassouni, M. E.; Chambost, J. P.; Expert, D.; Van Gijsegem, F.; Barras, F. The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi Proc. Natl. Acad. Sci. U.S.A. 1999, 96 (3) 887-892
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.3 , pp. 887-892
    • Hassouni, M.E.1    Chambost, J.P.2    Expert, D.3    Van Gijsegem, F.4    Barras, F.5
  • 5
    • 77957739593 scopus 로고    scopus 로고
    • Emerging complexity in reactive oxygen species production and signaling during the response of plants to pathogens
    • Vellosillo, T.; Vicente, J.; Kulasekaran, S.; Hamberg, M.; Castresana, C. Emerging complexity in reactive oxygen species production and signaling during the response of plants to pathogens Plant Physiol. 2010, 154 (2) 444-448
    • (2010) Plant Physiol. , vol.154 , Issue.2 , pp. 444-448
    • Vellosillo, T.1    Vicente, J.2    Kulasekaran, S.3    Hamberg, M.4    Castresana, C.5
  • 6
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. Pathways of oxidative damage Annu. Rev. Microbiol. 2003, 57, 395-418
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 7
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. Cellular defenses against superoxide and hydrogen peroxide Annu. Rev. Biochem. 2008, 77, 755-776
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 8
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • Avery, S. V. Molecular targets of oxidative stress Biochem. J. 2011, 434 (2) 201-210
    • (2011) Biochem. J. , vol.434 , Issue.2 , pp. 201-210
    • Avery, S.V.1
  • 9
    • 1942455710 scopus 로고    scopus 로고
    • Oxidative stress triggers thiol oxidation in the glyceraldehyde-3- phosphate dehydrogenase of Staphylococcus aureus
    • Weber, H.; Engelmann, S.; Becher, D.; Hecker, M. Oxidative stress triggers thiol oxidation in the glyceraldehyde-3-phosphate dehydrogenase of Staphylococcus aureus Mol. Microbiol. 2004, 52 (1) 133-140
    • (2004) Mol. Microbiol. , vol.52 , Issue.1 , pp. 133-140
    • Weber, H.1    Engelmann, S.2    Becher, D.3    Hecker, M.4
  • 10
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling, J.; Söll, D. Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site Proc. Natl. Acad. Sci. U.S.A. 2010, 107 (9) 4028-4033
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.9 , pp. 4028-4033
    • Ling, J.1    Söll, D.2
  • 11
    • 66749083834 scopus 로고    scopus 로고
    • Oxidative damage of mitochondrial proteins contributes to fruit senescence: A redox proteomics analysis
    • Qin, G.; Meng, X.; Wang, Q.; Tian, S. Oxidative damage of mitochondrial proteins contributes to fruit senescence: a redox proteomics analysis J. Proteome Res. 2009, 8 (5) 2449-2462
    • (2009) J. Proteome Res. , vol.8 , Issue.5 , pp. 2449-2462
    • Qin, G.1    Meng, X.2    Wang, Q.3    Tian, S.4
  • 12
    • 79960027526 scopus 로고    scopus 로고
    • Hydrogen peroxide acts on sensitive mitochondrial proteins to induce death of a fungal pathogen revealed by proteomic analysis
    • Qin, G.; Liu, J.; Cao, B.; Li, B.; Tian, S. Hydrogen peroxide acts on sensitive mitochondrial proteins to induce death of a fungal pathogen revealed by proteomic analysis PLoS One 2011, 6 (7) e21945
    • (2011) PLoS One , vol.6 , Issue.7 , pp. 21945
    • Qin, G.1    Liu, J.2    Cao, B.3    Li, B.4    Tian, S.5
  • 14
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response Cell 1994, 79 (4) 583-593
    • (1994) Cell , vol.79 , Issue.4 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 15
    • 0032549798 scopus 로고    scopus 로고
    • Reactive oxygen intermediates mediate a systemic signal network in the establishment of plant immunity
    • Alvarez, M. E.; Pennell, R. I.; Meijer, P. J.; Ishikawa, A.; Dixon, R. A.; Lamb, C. Reactive oxygen intermediates mediate a systemic signal network in the establishment of plant immunity Cell 1998, 92 (6) 773-784
    • (1998) Cell , vol.92 , Issue.6 , pp. 773-784
    • Alvarez, M.E.1    Pennell, R.I.2    Meijer, P.J.3    Ishikawa, A.4    Dixon, R.A.5    Lamb, C.6
  • 16
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited Microbiol. Mol. Biol. Rev. 2003, 67 (4) 593-656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 17
    • 55749092578 scopus 로고    scopus 로고
    • Bacterial membrane proteomics
    • Poetsch, A.; Wolters, D. Bacterial membrane proteomics Proteomics 2008, 8 (19) 4100-4122
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 4100-4122
    • Poetsch, A.1    Wolters, D.2
  • 18
    • 2442563573 scopus 로고    scopus 로고
    • E-dependent envelope stress response
    • E-dependent envelope stress response Mol. Microbiol. 2004, 52 (3) 613-619
    • (2004) Mol. Microbiol. , vol.52 , Issue.3 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 19
    • 53549100745 scopus 로고    scopus 로고
    • Signal integration in bacterial two-component regulatory systems
    • Mitrophanov, A. Y.; Groisman, E. A. Signal integration in bacterial two-component regulatory systems Genes Dev. 2008, 22 (19) 2601-2611
    • (2008) Genes Dev. , vol.22 , Issue.19 , pp. 2601-2611
    • Mitrophanov, A.Y.1    Groisman, E.A.2
  • 20
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L.; Dassa, E.; Orelle, C.; Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems Microbiol. Mol. Biol. Rev. 2008, 72 (2) 317-364
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , Issue.2 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 21
    • 55749112976 scopus 로고    scopus 로고
    • Membrane proteins and membrane proteomics
    • Tan, S.; Tan, H. T.; Chung, M. C. Membrane proteins and membrane proteomics Proteomics 2008, 8 (19) 3924-3932
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3924-3932
    • Tan, S.1    Tan, H.T.2    Chung, M.C.3
  • 22
    • 0025159306 scopus 로고
    • A 59 kiloDalton outer membrane protein of Salmonella typhimurium protects against oxidative intraleukocytic killing due to human neutrophils
    • Stinavage, P. S.; Martin, L. E.; Spitznagel, J. K. A 59 kiloDalton outer membrane protein of Salmonella typhimurium protects against oxidative intraleukocytic killing due to human neutrophils Mol. Microbiol. 1990, 4 (2) 283-293
    • (1990) Mol. Microbiol. , vol.4 , Issue.2 , pp. 283-293
    • Stinavage, P.S.1    Martin, L.E.2    Spitznagel, J.K.3
  • 23
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem, A.; Varghese, S.; Imlay, J. A. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli Mol. Microbiol. 2009, 72 (4) 844-858
    • (2009) Mol. Microbiol. , vol.72 , Issue.4 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 24
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt, B. F.; Simon, G. M.; Yates, J. R., III The biological impact of mass-spectrometry-based proteomics Nature 2007, 450 (7172) 991-1000
    • (2007) Nature , vol.450 , Issue.7172 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates III, J.R.3
  • 25
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz, J.; Scharf, C.; Hecker, M.; Homuth, G. Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress Microbiology 2004, 150 (2) 497-512
    • (2004) Microbiology , vol.150 , Issue.2 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 26
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert, L. I.; Jakob, U. Protein thiol modifications visualized in vivo PLoS Biol. 2004, 2 (11) e333
    • (2004) PLoS Biol. , vol.2 , Issue.11 , pp. 333
    • Leichert, L.I.1    Jakob, U.2
  • 27
    • 0018224280 scopus 로고
    • Trans-complementation-dependent replication of a low molecular weight origin fragment from plasmid R6K
    • Kolter, R.; Inuzuka, M.; Helinski, D. R. Trans-complementation-dependent replication of a low molecular weight origin fragment from plasmid R6K Cell 1978, 15 (4) 1199-1208
    • (1978) Cell , vol.15 , Issue.4 , pp. 1199-1208
    • Kolter, R.1    Inuzuka, M.2    Helinski, D.R.3
  • 28
    • 0022595516 scopus 로고
    • Generation and Characterization of Tn5 Insertion Mutations in Pseudomonas syringae pv. tomato
    • Cuppels, D. A. Generation and Characterization of Tn5 Insertion Mutations in Pseudomonas syringae pv. tomato Appl. Environ. Microbiol. 1986, 51 (2) 323-327
    • (1986) Appl. Environ. Microbiol. , vol.51 , Issue.2 , pp. 323-327
    • Cuppels, D.A.1
  • 29
    • 0033932228 scopus 로고    scopus 로고
    • Identification and subcellular localization of the Legionella pneumophila IcmX protein: A factor essential for establishment of a replicative organelle in eukaryotic host cells
    • Matthews, M.; Roy, C. R. Identification and subcellular localization of the Legionella pneumophila IcmX protein: a factor essential for establishment of a replicative organelle in eukaryotic host cells Infect. Immun. 2000, 68 (7) 3971-3982
    • (2000) Infect. Immun. , vol.68 , Issue.7 , pp. 3971-3982
    • Matthews, M.1    Roy, C.R.2
  • 30
    • 0036156940 scopus 로고    scopus 로고
    • Regulatory RNA as mediator in GacA/RsmA-dependent global control of exoproduct formation in Pseudomonas fluorescens CHA0
    • Heeb, S.; Blumer, C.; Haas, D. Regulatory RNA as mediator in GacA/RsmA-dependent global control of exoproduct formation in Pseudomonas fluorescens CHA0 J. Bacteriol. 2002, 184 (4) 1046-1056
    • (2002) J. Bacteriol. , vol.184 , Issue.4 , pp. 1046-1056
    • Heeb, S.1    Blumer, C.2    Haas, D.3
  • 31
    • 0022474397 scopus 로고
    • Second symbiotic megaplasmid in Rhizobium meliloti carrying exopolysaccharide and thiamine synthesis genes
    • Finan, T. M.; Kunkel, B.; De Vos, G. F.; Signer, E. R. Second symbiotic megaplasmid in Rhizobium meliloti carrying exopolysaccharide and thiamine synthesis genes J. Bacteriol. 1986, 167 (1) 66-72
    • (1986) J. Bacteriol. , vol.167 , Issue.1 , pp. 66-72
    • Finan, T.M.1    Kunkel, B.2    De Vos, G.F.3    Signer, E.R.4
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 34248338745 scopus 로고    scopus 로고
    • Proteomic and immunoblot analyses of Bartonella quintana total membrane proteins identify antigens recognized by sera from infected patients
    • Boonjakuakul, J. K.; Gerns, H. L.; Chen, Y. T.; Hicks, L. D.; Minnick, M. F.; Dixon, S. E.; Hall, S. C.; Koehler, J. E. Proteomic and immunoblot analyses of Bartonella quintana total membrane proteins identify antigens recognized by sera from infected patients Infect. Immun. 2007, 75 (5) 2548-2561
    • (2007) Infect. Immun. , vol.75 , Issue.5 , pp. 2548-2561
    • Boonjakuakul, J.K.1    Gerns, H.L.2    Chen, Y.T.3    Hicks, L.D.4    Minnick, M.F.5    Dixon, S.E.6    Hall, S.C.7    Koehler, J.E.8
  • 37
    • 34547637894 scopus 로고    scopus 로고
    • Uropathogenic Escherichia coli outer membrane antigens expressed during urinary tract infection
    • Hagan, E. C.; Mobley, H. L. Uropathogenic Escherichia coli outer membrane antigens expressed during urinary tract infection Infect. Immun. 2007, 75 (8) 3941-3949
    • (2007) Infect. Immun. , vol.75 , Issue.8 , pp. 3941-3949
    • Hagan, E.C.1    Mobley, H.L.2
  • 38
    • 34147147652 scopus 로고    scopus 로고
    • Crucial role of antioxidant proteins and hydrolytic enzymes in pathogenicity of Penicillium expansum: Analysis based on proteomics approach
    • Qin, G.; Tian, S.; Chan, Z.; Li, B. Crucial role of antioxidant proteins and hydrolytic enzymes in pathogenicity of Penicillium expansum: analysis based on proteomics approach Mol. Cell. Proteomics 2007, 6 (3) 425-438
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.3 , pp. 425-438
    • Qin, G.1    Tian, S.2    Chan, Z.3    Li, B.4
  • 39
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nyström, T. Role of oxidative carbonylation in protein quality control and senescence EMBO J. 2005, 24 (7) 1311-1317
    • (2005) EMBO J. , vol.24 , Issue.7 , pp. 1311-1317
    • Nyström, T.1
  • 40
    • 34249881603 scopus 로고    scopus 로고
    • Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine
    • Alteri, C. J.; Mobley, H. L. Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine Infect. Immun. 2007, 75 (6) 2679-2688
    • (2007) Infect. Immun. , vol.75 , Issue.6 , pp. 2679-2688
    • Alteri, C.J.1    Mobley, H.L.2
  • 41
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn, E. M.; Patel, D. R.; Lepore, B. W.; Indic, M.; van den Berg, B. Transmembrane passage of hydrophobic compounds through a protein channel wall Nature 2009, 458 (7236) 367-370
    • (2009) Nature , vol.458 , Issue.7236 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    Van Den Berg, B.5
  • 42
    • 33845382343 scopus 로고    scopus 로고
    • Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins
    • Huang, C. Z.; Lin, X. M.; Wu, L. N.; Zhang, D. F.; Liu, D.; Wang, S. Y.; Peng, X. X. Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins J. Proteome Res. 2006, 5 (12) 3268-3276
    • (2006) J. Proteome Res. , vol.5 , Issue.12 , pp. 3268-3276
    • Huang, C.Z.1    Lin, X.M.2    Wu, L.N.3    Zhang, D.F.4    Liu, D.5    Wang, S.Y.6    Peng, X.X.7
  • 43
    • 0022824157 scopus 로고
    • Cotranslational and posttranslational protein translocation in prokaryotic systems
    • Lee, C.; Beckwith, J. Cotranslational and posttranslational protein translocation in prokaryotic systems Annu. Rev. Cell Biol. 1986, 2, 315-336
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 315-336
    • Lee, C.1    Beckwith, J.2
  • 44
    • 55949087672 scopus 로고    scopus 로고
    • Comparison of the membrane subproteomes during growth of a new Pseudomonas strain on lysogeny broth medium, glucose, and phenol
    • Papasotiriou, D. G.; Markoutsa, S.; Meyer, B.; Papadioti, A.; Karas, M.; Tsiotis, G. Comparison of the membrane subproteomes during growth of a new Pseudomonas strain on lysogeny broth medium, glucose, and phenol J. Proteome Res. 2008, 7 (10) 4278-4288
    • (2008) J. Proteome Res. , vol.7 , Issue.10 , pp. 4278-4288
    • Papasotiriou, D.G.1    Markoutsa, S.2    Meyer, B.3    Papadioti, A.4    Karas, M.5    Tsiotis, G.6
  • 45
    • 0032911908 scopus 로고    scopus 로고
    • Long-chain fatty acid transport in bacteria and yeast. Paradigms for defining the mechanism underlying this protein-mediated process
    • DiRusso, C. C.; Black, P. N. Long-chain fatty acid transport in bacteria and yeast. Paradigms for defining the mechanism underlying this protein-mediated process Mol. Cell. Biochem. 1999, 192 (1-2) 41-52
    • (1999) Mol. Cell. Biochem. , vol.192 , Issue.1-2 , pp. 41-52
    • Dirusso, C.C.1    Black, P.N.2
  • 46
    • 23044513554 scopus 로고    scopus 로고
    • The FadL family: Unusual transporters for unusual substrates
    • van den Berg, B. The FadL family: unusual transporters for unusual substrates Curr. Opin. Struct. Biol. 2005, 15 (4) 401-407
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , Issue.4 , pp. 401-407
    • Van Den Berg, B.1
  • 47
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: An early plant response to pathogen infection
    • Wojtaszek, P. Oxidative burst: an early plant response to pathogen infection Biochem. J. 1997, 322 (3) 681-692
    • (1997) Biochem. J. , vol.322 , Issue.3 , pp. 681-692
    • Wojtaszek, P.1
  • 48
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan, C.; Shiloh, M. U. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (16) 8841-8848
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.16 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 49
    • 79960442941 scopus 로고    scopus 로고
    • Proteomics of the oxidative stress response induced by hydrogen peroxide and paraquat reveals a novel AhpC-like protein in Pseudomonas aeruginosa
    • Hare, N. J.; Scott, N. E.; Shin, E. H.; Connolly, A. M.; Larsen, M. R.; Palmisano, G.; Cordwell, S. J. Proteomics of the oxidative stress response induced by hydrogen peroxide and paraquat reveals a novel AhpC-like protein in Pseudomonas aeruginosa Proteomics 2011, 11 (15) 3056-3069
    • (2011) Proteomics , vol.11 , Issue.15 , pp. 3056-3069
    • Hare, N.J.1    Scott, N.E.2    Shin, E.H.3    Connolly, A.M.4    Larsen, M.R.5    Palmisano, G.6    Cordwell, S.J.7
  • 50
    • 0026458015 scopus 로고
    • Transport proteins in bacteria: Common themes in their design
    • Nikaido, H.; Saier, M. H., Jr. Transport proteins in bacteria: common themes in their design Science 1992, 258 (5084) 936-942
    • (1992) Science , vol.258 , Issue.5084 , pp. 936-942
    • Nikaido, H.1    Saier Jr., M.H.2
  • 51
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins, C. F. ABC transporters: from microorganisms to man Annu. Rev. Cell Biol. 1992, 8, 67-113
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 52
    • 55249089247 scopus 로고    scopus 로고
    • Identification and network of outer membrane proteins regulating streptomysin resistance in Escherichia coli
    • Li, H.; Wang, B. C.; Xu, W. J.; Lin, X. M.; Peng, X. X. Identification and network of outer membrane proteins regulating streptomysin resistance in Escherichia coli J. Proteome Res. 2008, 7 (9) 4040-4049
    • (2008) J. Proteome Res. , vol.7 , Issue.9 , pp. 4040-4049
    • Li, H.1    Wang, B.C.2    Xu, W.J.3    Lin, X.M.4    Peng, X.X.5
  • 53
    • 49849089764 scopus 로고    scopus 로고
    • Proteomic analysis of nalidixic acid resistance in Escherichia coli: Identification and functional characterization of OM proteins
    • Lin, X. M.; Li, H.; Wang, C.; Peng, X. X. Proteomic analysis of nalidixic acid resistance in Escherichia coli: identification and functional characterization of OM proteins J. Proteome Res. 2008, 7 (6) 2399-2405
    • (2008) J. Proteome Res. , vol.7 , Issue.6 , pp. 2399-2405
    • Lin, X.M.1    Li, H.2    Wang, C.3    Peng, X.X.4
  • 54
    • 61849139041 scopus 로고    scopus 로고
    • From proteome to genome for functional characterization of pH-dependent outer membrane proteins in Escherichia coli
    • Wu, L.; Lin, X. M.; Peng, X. X. From proteome to genome for functional characterization of pH-dependent outer membrane proteins in Escherichia coli J. Proteome Res. 2009, 8 (2) 1059-1070
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 1059-1070
    • Wu, L.1    Lin, X.M.2    Peng, X.X.3
  • 55
    • 21444455372 scopus 로고    scopus 로고
    • Novel approach to mapping of resistance mutations in whole genomes by using restriction enzyme modulation of transformation efficiency
    • Lerner, C. G.; Kakavas, S. J.; Wagner, C.; Chang, R. T.; Merta, P. J.; Ruan, X.; Metzger, R. E.; Beutel, B. A. Novel approach to mapping of resistance mutations in whole genomes by using restriction enzyme modulation of transformation efficiency Antimicrob. Agents Chemother. 2005, 49 (7) 2767-2777
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.7 , pp. 2767-2777
    • Lerner, C.G.1    Kakavas, S.J.2    Wagner, C.3    Chang, R.T.4    Merta, P.J.5    Ruan, X.6    Metzger, R.E.7    Beutel, B.A.8
  • 56
    • 79959708037 scopus 로고    scopus 로고
    • Autotransporters with GDSL passenger domains: Molecular physiology and biotechnological applications
    • Wilhelm, S.; Rosenau, F.; Kolmar, H.; Jaeger, K. E. Autotransporters with GDSL passenger domains: molecular physiology and biotechnological applications ChemBioChem 2011, 12 (10) 1476-1485
    • (2011) Chem Bio Chem , vol.12 , Issue.10 , pp. 1476-1485
    • Wilhelm, S.1    Rosenau, F.2    Kolmar, H.3    Jaeger, K.E.4
  • 57
    • 4744367501 scopus 로고    scopus 로고
    • Recognition of iron-free siderophores by TonB-dependent iron transporters
    • Schalk, I. J.; Yue, W. W.; Buchanan, S. K. Recognition of iron-free siderophores by TonB-dependent iron transporters Mol. Microbiol. 2004, 54 (1) 14-22
    • (2004) Mol. Microbiol. , vol.54 , Issue.1 , pp. 14-22
    • Schalk, I.J.1    Yue, W.W.2    Buchanan, S.K.3
  • 58
    • 42549102413 scopus 로고    scopus 로고
    • Characterization of the PvdS-regulated promoter motif in Pseudomonas syringae pv. tomato DC3000 reveals regulon members and insights regarding PvdS function in other pseudomonads
    • Swingle, B.; Thete, D.; Moll, M.; Myers, C. R.; Schneider, D. J.; Cartinhour, S. Characterization of the PvdS-regulated promoter motif in Pseudomonas syringae pv. tomato DC3000 reveals regulon members and insights regarding PvdS function in other pseudomonads Mol. Microbiol. 2008, 68 (4) 871-889
    • (2008) Mol. Microbiol. , vol.68 , Issue.4 , pp. 871-889
    • Swingle, B.1    Thete, D.2    Moll, M.3    Myers, C.R.4    Schneider, D.J.5    Cartinhour, S.6
  • 59
    • 0036403720 scopus 로고    scopus 로고
    • Function of Pseudomonas porins in uptake and efflux
    • Hancock, R. E.; Brinkman, F. S. Function of Pseudomonas porins in uptake and efflux Annu. Rev. Microbiol. 2002, 56, 17-38
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 17-38
    • Hancock, R.E.1    Brinkman, F.S.2
  • 60
    • 0029056666 scopus 로고
    • The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa
    • Wylie, J. L.; Worobec, E. A. The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa J. Bacteriol. 1995, 177 (11) 3021-3026
    • (1995) J. Bacteriol. , vol.177 , Issue.11 , pp. 3021-3026
    • Wylie, J.L.1    Worobec, E.A.2
  • 61
    • 33644903806 scopus 로고    scopus 로고
    • Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa
    • Tamber, S.; Ochs, M. M.; Hancock, R. E. Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa J. Bacteriol. 2006, 188 (1) 45-54
    • (2006) J. Bacteriol. , vol.188 , Issue.1 , pp. 45-54
    • Tamber, S.1    Ochs, M.M.2    Hancock, R.E.3
  • 62
    • 9244241532 scopus 로고    scopus 로고
    • ATP-binding cassette transporters are targets for the development of antibacterial vaccines and therapies
    • Garmory, H. S.; Titball, R. W. ATP-binding cassette transporters are targets for the development of antibacterial vaccines and therapies Infect. Immun. 2004, 72 (12) 6757-6763
    • (2004) Infect. Immun. , vol.72 , Issue.12 , pp. 6757-6763
    • Garmory, H.S.1    Titball, R.W.2
  • 63
    • 0035024005 scopus 로고    scopus 로고
    • Bacterial ABC transporters of amino acids
    • Hosie, A. H.; Poole, P. S. Bacterial ABC transporters of amino acids Res. Microbiol. 2001, 152 (3-4) 259-270
    • (2001) Res. Microbiol. , vol.152 , Issue.3-4 , pp. 259-270
    • Hosie, A.H.1    Poole, P.S.2
  • 64
    • 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.; Giffard, P. M. The bspA locus of Lactobacillus fermentum BR11 encodes an L-cystine uptake system J. Bacteriol. 1999, 181 (7) 2192-2198
    • (1999) J. Bacteriol. , vol.181 , Issue.7 , pp. 2192-2198
    • Turner, M.S.1    Woodberry, T.2    Hafner, L.M.3    Giffard, P.M.4
  • 65
    • 14944364669 scopus 로고    scopus 로고
    • BspA (CyuC) in Lactobacillus fermentum BR11 is a highly expressed high-affinity L-cystine-binding protein
    • Hung, J.; Turner, M. S.; Walsh, T.; Giffard, P. M. BspA (CyuC) in Lactobacillus fermentum BR11 is a highly expressed high-affinity L-cystine-binding protein Curr. Microbiol. 2005, 50 (1) 33-37
    • (2005) Curr. Microbiol. , vol.50 , Issue.1 , pp. 33-37
    • Hung, J.1    Turner, M.S.2    Walsh, T.3    Giffard, P.M.4
  • 66
    • 0034596998 scopus 로고    scopus 로고
    • Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer
    • Diedrich, G.; Spahn, C. M.; Stelzl, U.; Schäfer, M. A.; Wooten, T.; Bochkariov, D. E.; Cooperman, B. S.; Traut, R. R.; Nierhaus, K. H. Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer EMBO J. 2000, 19 (19) 5241-5250
    • (2000) EMBO J. , vol.19 , Issue.19 , pp. 5241-5250
    • Diedrich, G.1    Spahn, C.M.2    Stelzl, U.3    Schäfer, M.A.4    Wooten, T.5    Bochkariov, D.E.6    Cooperman, B.S.7    Traut, R.R.8    Nierhaus, K.H.9
  • 67
    • 0026573455 scopus 로고
    • Localization of two glycolytic enzymes in guinea-pig taenia coli
    • Hardin, C. D.; Paul, R. J. Localization of two glycolytic enzymes in guinea-pig taenia coli Biochim. Biophys. Acta 1992, 1134 (3) 256-259
    • (1992) Biochim. Biophys. Acta , vol.1134 , Issue.3 , pp. 256-259
    • Hardin, C.D.1    Paul, R.J.2
  • 69
    • 14044251591 scopus 로고    scopus 로고
    • Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
    • Campanella, M. E.; Chu, H.; Low, P. S. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane Proc. Natl. Acad. Sci. U.S.A. 2005, 102 (7) 2402-2407
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.7 , pp. 2402-2407
    • Campanella, M.E.1    Chu, H.2    Low, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.