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Volumn 10, Issue 6, 2011, Pages 2767-2776

Analyses of soluble and membrane proteomes of Ralstonia eutropha H16 reveal major changes in the protein complement in adaptation to lithoautotrophy

Author keywords

15N metabolic labeling; chemotaxis; hydrogenase respiratory chain; lithoautotrophy; membrane proteins; PHB; Ralstonia eutropha; shotgun proteomics

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; HYDROGEN; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; OXIDOREDUCTASE; POLY(3 HYDROXYBUTYRIC ACID); PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SIGMA FACTOR; SUCCINIC ACID;

EID: 79958227262     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr101289v     Document Type: Article
Times cited : (29)

References (64)
  • 2
    • 0003188761 scopus 로고
    • Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas
    • Wilde, E. Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas Arch. Mikrobiol. 1962, 43, 109-137
    • (1962) Arch. Mikrobiol. , vol.43 , pp. 109-137
    • Wilde, E.1
  • 4
    • 55249110895 scopus 로고    scopus 로고
    • Genomic view of energy metabolism in Ralstonia eutropha H16
    • Cramm, R. Genomic view of energy metabolism in Ralstonia eutropha H16 J. Mol. Microbiol. Biotechnol. 2009, 16, 38-52
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.16 , pp. 38-52
    • Cramm, R.1
  • 6
    • 0029162190 scopus 로고
    • Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus
    • Kusian, B.; Bednarski, R.; Husemann, M.; Bowien, B. Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus J. Bacteriol. 1995, 177, 4442-4450
    • (1995) J. Bacteriol. , vol.177 , pp. 4442-4450
    • Kusian, B.1    Bednarski, R.2    Husemann, M.3    Bowien, B.4
  • 7
    • 79958232362 scopus 로고    scopus 로고
    • PCT/EP99/06154. PCT/EP99/06154.
    • Heumann, H. PCT/EP99/06154. PCT/EP99/06154, 1999.
    • (1999)
    • Heumann, H.1
  • 9
    • 0037374993 scopus 로고    scopus 로고
    • Polyhydroxyalkanoates: An overview
    • DOI 10.1016/S0960-8524(02)00212-2, PII S0960852402002122
    • Reddy, C. S.; Ghai, R.; Rashmi; Kalia, V. C. Polyhydroxyalkanoates: an overview Bioresour. Technol. 2003, 87, 137-146 (Pubitemid 35452650)
    • (2003) Bioresource Technology , vol.87 , Issue.2 , pp. 137-146
    • Reddy, C.S.K.1    Ghai, R.2    Rashmi3    Kalia, V.C.4
  • 11
    • 0026033649 scopus 로고
    • Physiology and molecular genetics of poly(β-hydroxyalkanoic acid) synthesis in Alcaligenes eutrophus
    • Steinbüchel, A.; Schlegel, H. G. Physiology and molecular genetics of poly(β-hydroxy-alkanoic acid) synthesis in Alcaligenes eutrophus Mol. Microbiol. 1991, 5, 535-542 (Pubitemid 21896075)
    • (1991) Molecular Microbiology , vol.5 , Issue.3 , pp. 535-542
    • Steinbuchel, A.1    Schlegel, H.G.2
  • 12
    • 0000694310 scopus 로고
    • Genus Alcaligenes Castellani and Chalmers 1919
    • In;;, Eds.; The Williams & Wilkins Co.: Baltimore, MD,; Vol., pp.
    • Kersters, K.; De Ley, J. Genus Alcaligenes Castellani and Chalmers 1919. In Bergey's manual of systematic bacteriology; Krieg, N. R.; Holt, J. G., Eds.; The Williams & Wilkins Co.: Baltimore, MD, 1984; Vol. 1, pp 381-373.
    • (1984) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 381-373
    • Kersters, K.1    De Ley, J.2    Krieg, N.R.3    Holt, J.G.4
  • 15
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur Kultur Wasserstoffoxydierender Bakterien-Wachstumsphysiologische Untersuchungen
    • Schlegel, H. G.; Kaltwasser, H.; Gottschalk, G. Ein Submersverfahren zur Kultur Wasserstoffoxydierender Bakterien-Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 1961, 38, 209-222
    • (1961) Arch. Mikrobiol. , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 16
    • 0016279265 scopus 로고
    • Rhodopseudomonas globiformis, sp. n., a new species of the Rhodospirillaceae
    • Pfennig, N. Rhodopseudomonas globiformis, sp. n., a new species of the Rhodospirillaceae Arch. Microbiol. 1974, 100, 197-206
    • (1974) Arch. Microbiol. , vol.100 , pp. 197-206
    • Pfennig, N.1
  • 17
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • DOI 10.1083/jcb.93.1.97
    • Fujiki, Y.; Hubbard, A. L.; Fowler, S.; Lazarow, P. B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum J. Cell Biol. 1982, 93, 97-102 (Pubitemid 12117045)
    • (1982) Journal of Cell Biology , vol.93 , Issue.1 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 18
    • 0020687017 scopus 로고
    • Staining of proteins on gels: Comparisons of dyes and procedures
    • Wilson, C. M. Staining of proteins on gels: comparisons of dyes and procedures Methods Enzymol. 1983, 91, 236-247
    • (1983) Methods Enzymol. , vol.91 , pp. 236-247
    • Wilson, C.M.1
  • 20
    • 50249172221 scopus 로고    scopus 로고
    • Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus
    • Wolff, S.; Hahne, H.; Hecker, M.; Becher, D. Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus Mol. Cell. Proteomics 2008, 7, 1460-1468
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1460-1468
    • Wolff, S.1    Hahne, H.2    Hecker, M.3    Becher, D.4
  • 22
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K.; McCormack, A. L.; Yates, J. R., 3rd An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 1994, 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 23
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L.; McDonald, W. H.; Yates, J. R., 3rd DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics J. Proteome Res. 2002, 1, 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 24
    • 33749062913 scopus 로고    scopus 로고
    • ProRata: A quantitative proteomics program for accurate protein abundance ratio estimation with confidence interval evaluation
    • DOI 10.1021/ac060654b
    • Pan, C.; Kora, G.; McDonald, W. H.; Tabb, D. L.; VerBerkmoes, N. C.; Hurst, G. B.; Pelletier, D. A.; Samatova, N. F.; Hettich, R. L. ProRata: A quantitative proteomics program for accurate protein abundance ratio estimation with confidence interval evaluation Anal. Chem. 2006, 78, 7121-7131 (Pubitemid 44607553)
    • (2006) Analytical Chemistry , vol.78 , Issue.20 , pp. 7121-7131
    • Pan, C.1    Kora, G.2    McDonald, W.H.3    Tabb, D.L.4    VerBerkmoes, N.C.5    Hurst, G.B.6    Pelletier, D.A.7    Samatova, N.F.8    Hettich, R.L.9
  • 25
    • 34548431062 scopus 로고    scopus 로고
    • Capture and analysis of quantitative proteomic data
    • DOI 10.1002/pmic.200700127
    • Lau, K. W.; Jones, A. R.; Swainston, N.; Siepen, J. A.; Hubbard, S. J. Capture and analysis of quantitative proteomic data Proteomics 2007, 7, 2787-2799 (Pubitemid 47359921)
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2787-2799
    • King, W.L.1    Jones, A.R.2    Swainston, N.3    Siepen, J.A.4    Hubbard, S.J.5
  • 26
    • 33748878164 scopus 로고    scopus 로고
    • Methods for predicting bacterial protein subcellular localization
    • DOI 10.1038/nrmicro1494, PII NRMICRO1494
    • Gardy, J. L.; Brinkman, F. S. Methods for predicting bacterial protein subcellular localization Nat. Rev. Microbiol. 2006, 4, 741-751 (Pubitemid 44420125)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.10 , pp. 741-751
    • Gardy, J.L.1    Brinkman, F.S.L.2
  • 27
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • DOI 10.1110/ps.0303703
    • Juncker, A. S.; Willenbrock, H.; Von Heijne, G.; Brunak, S.; Nielsen, H.; Krogh, A. Prediction of lipoprotein signal peptides in Gram-negative bacteria Protein Sci. 2003, 12, 1652-1662 (Pubitemid 36910046)
    • (2003) Protein Science , vol.12 , Issue.8 , pp. 1652-1662
    • Juncker, A.S.1    Willenbrock, H.2    Von Heijne, G.3    Brunak, S.4    Nielsen, H.5    Krogh, A.6
  • 28
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305, 567-580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 33
    • 18844464043 scopus 로고    scopus 로고
    • Global analysis of the Ralstonia metallidurans proteome: Prelude for the large-scale study of heavy metal response
    • DOI 10.1002/pmic.200300551
    • Noel-Georis, I.; Vallaeys, T.; Chauvaux, R.; Monchy, S.; Falmagne, P.; Mergeay, M.; Wattiez, R. Global analysis of the Ralstonia metallidurans proteome: prelude for the large-scale study of heavy metal response Proteomics 2004, 4, 151-179 (Pubitemid 38140882)
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 151-179
    • Noel-Georis, I.1    Vallaeys, T.2    Chauvaux, R.3    Monchy, S.4    Falmagne, P.5    Mergeay, M.6    Wattiez, R.7
  • 35
    • 0030968506 scopus 로고    scopus 로고
    • 2-activating subunit, HoxH, directs maturation of the NAD-reducing hydrogenase in alcaligenes eutrophus
    • 2-activating subunit, HoxH, directs maturation of the NAD-reducing hydrogenase in Alcaligenes eutrophus Eur. J. Biochem. 1997, 245, 441-448 (Pubitemid 27171271)
    • (1997) European Journal of Biochemistry , vol.245 , Issue.2 , pp. 441-448
    • Massanz, C.1    Fernandez, V.M.2    Friedrich, B.3
  • 36
    • 0031747821 scopus 로고    scopus 로고
    • Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes
    • Schwartz, E.; Gerischer, U.; Friedrich, B. Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes J. Bacteriol. 1998, 180, 3197-3204 (Pubitemid 28285035)
    • (1998) Journal of Bacteriology , vol.180 , Issue.12 , pp. 3197-3204
    • Schwartz, E.1    Gerischer, U.2    Friedrich, B.3
  • 37
    • 0034859205 scopus 로고    scopus 로고
    • Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha
    • Burgdorf, T.; Bommer, D.; Bowien, B. Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha J. Mol. Microbiol. Biotechnol. 2001, 3, 619-629 (Pubitemid 32791422)
    • (2001) Journal of Molecular Microbiology and Biotechnology , vol.3 , Issue.4 , pp. 619-629
    • Burgdorf, T.1    Bommer, D.2    Bowien, B.3
  • 38
    • 0036318686 scopus 로고    scopus 로고
    • 2 assimilation in the chemoautotroph Ralstonia eutropha
    • DOI 10.1007/s00203-002-0441-3
    • 2 assimilation in the chemoautotroph Ralstonia eutropha Arch. Microbiol. 2002, 178, 85-93 (Pubitemid 34762249)
    • (2002) Archives of Microbiology , vol.178 , Issue.2 , pp. 85-93
    • Bowien, B.1    Kusian, B.2
  • 39
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • DOI 10.1016/S0005-2728(97)00046-7, PII S0005272897000467
    • Jünemann, S. Cytochrome bd terminal oxidase Biochim. Biophys. Acta 1997, 1321, 107-127 (Pubitemid 27390501)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1321 , Issue.2 , pp. 107-127
    • Junemann, S.1
  • 40
    • 0025898632 scopus 로고
    • The electron transport system of Alcaligenes eutrophus H16. II. Respiratory activities and effect of specific inhibitors
    • Kömen, R.; Zannoni, D.; Schmidt, K. The electron transport system of Alcaligenes eutrophus H16. II. Respiratory activities and effect of specific inhibitors Arch. Microbiol. 1991, 155, 436-443
    • (1991) Arch. Microbiol. , vol.155 , pp. 436-443
    • Kömen, R.1    Zannoni, D.2    Schmidt, K.3
  • 41
    • 0021272743 scopus 로고
    • Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome b 558- d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems
    • Kita, K.; Konishi, K.; Anraku, Y. Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome b 558- d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems J. Biol. Chem. 1984, 259, 3375-3378
    • (1984) J. Biol. Chem. , vol.259 , pp. 3375-3378
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 44
    • 0027183518 scopus 로고
    • The Alcaligenes eutrophus ldh structural gene encodes a novel type of lactate dehydrogenase
    • DOI 10.1016/0378-1097(93)90169-3
    • Jendrossek, D.; Kratzin, H. D.; Steinbüchel, A. The Alcaligenes eutrophus ldh structural gene encodes a novel type of lactate dehydrogenase FEMS Microbiol. Lett. 1993, 112, 229-235 (Pubitemid 23268367)
    • (1993) FEMS Microbiology Letters , vol.112 , Issue.2 , pp. 229-235
    • Jendrossek, D.1    Kratzin, H.D.2    Steinbuchel, A.3
  • 45
    • 0024997269 scopus 로고
    • Characterization of alcohol dehydrogenase genes of derepressible wild-type Alcaligenes eutrophus H16 and constitutive mutants
    • Jendrossek, D.; Kruger, N.; Steinbüchel, A. Characterization of alcohol dehydrogenase genes of derepressible wild-type Alcaligenes eutrophus H16 and constitutive mutants J. Bacteriol. 1990, 172, 4844-4851 (Pubitemid 20281929)
    • (1990) Journal of Bacteriology , vol.172 , Issue.9 , pp. 4844-4851
    • Jendrossek, D.1    Kruger, N.2    Steinbuchel, A.3
  • 46
    • 0020639432 scopus 로고
    • Fermentation enzymes in strictly aerobic bacteria: Comparative studies on strains of the genus Alcaligenes and on Nocardia opaca and Xanthobacter autotrophicus
    • Steinbüchel, A.; Kuhn, M.; Niedrig, M.; Schlegel, H. G. Fermentation enzymes in strictly aerobic bacteria: Comparative studies on strains of the genus Alcaligenes and on Nocardia opaca and Xanthobacter autotrophicus J. Gen. Microbiol. 1983, 129, 2825-2835 (Pubitemid 13024820)
    • (1983) Journal of General Microbiology , vol.129 , Issue.9 , pp. 2825-2835
    • Steinbuchel, A.1    Kuhn, M.2    Niedrig, M.3    Schlegel, H.G.4
  • 47
    • 57049133445 scopus 로고    scopus 로고
    • Proton-translocating transhydrogenase: An update of unsolved and controversial issues
    • Pedersen, A.; Karlsson, G. B.; Rydström, J. Proton-translocating transhydrogenase: an update of unsolved and controversial issues J. Bioenerg. Biomembr. 2008, 40, 463-473
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 463-473
    • Pedersen, A.1    Karlsson, G.B.2    Rydström, J.3
  • 48
    • 55249098183 scopus 로고    scopus 로고
    • Ralstonia eutropha strain H16 as model organism for PHA metabolism and for biotechnological production of technically interesting biopolymers
    • Reinecke, F.; Steinbüchel, A. Ralstonia eutropha strain H16 as model organism for PHA metabolism and for biotechnological production of technically interesting biopolymers J. Mol. Microbiol. Biotechnol. 2009, 16, 91-108
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.16 , pp. 91-108
    • Reinecke, F.1    Steinbüchel, A.2
  • 49
    • 0018133572 scopus 로고
    • Metabolite concentrations in Alcaligenes eutrophus H 16 and a mutant defective in poly-β-hydroxybutyrate synthesis
    • Cook, A. M.; Schlegel, H. G. Metabolite concentrations in Alcaligenes eutrophus H16 and a mutant defective in poly-β-hydroxybutyrate synthesis Arch. Microbiol. 1978, 119, 231-235 (Pubitemid 9077863)
    • (1978) Archives of Microbiology , vol.119 , Issue.3 , pp. 231-235
    • Cook, A.M.1    Schlegel, H.G.2
  • 51
    • 0024291372 scopus 로고
    • Multiple principal sigma factor homologs in eubacteria: Identification of the " rpoD box
    • Tanaka, K.; Shiina, T.; Takahashi, H. Multiple principal sigma factor homologs in eubacteria: identification of the " rpoD box Science 1988, 242, 1040-1042
    • (1988) Science , vol.242 , pp. 1040-1042
    • Tanaka, K.1    Shiina, T.2    Takahashi, H.3
  • 52
    • 0024727149 scopus 로고
    • e subunit of Escherichia coli RNA polymerase: A second alternate σ factor involved in high-temperature gene expression
    • E subunit of Escherichia coli RNA polymerase: a second alternate σ factor involved in high-temperature gene expression Genes Dev. 1989, 3, 1462-1471
    • (1989) Genes Dev. , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 53
    • 0030947960 scopus 로고    scopus 로고
    • A mycobacterial extracytoplasmic function sigma factor involved in survival following stress
    • Wu, Q. L.; Kong, D.; Lam, K.; Husson, R. N. A mycobacterial extracytoplasmic function sigma factor involved in survival following stress J. Bacteriol. 1997, 179, 2922-2929 (Pubitemid 27194440)
    • (1997) Journal of Bacteriology , vol.179 , Issue.9 , pp. 2922-2929
    • Wu, Q.-L.1    Kong, D.2    Lam, K.3    Husson, R.N.4
  • 54
    • 2442563573 scopus 로고    scopus 로고
    • E-dependent envelope stress response
    • DOI 10.1111/j.1365-2958.2003.03982.x
    • Alba, B. M.; Gross, C. A. Regulation of the Escherichia coli sigma-dependent envelope stress response Mol. Microbiol. 2004, 52 (3) 613-619 (Pubitemid 38621733)
    • (2004) Molecular Microbiology , vol.52 , Issue.3 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 55
    • 45249100907 scopus 로고    scopus 로고
    • e, is required to maintain cell envelope integrity in Escherichia coli
    • E, is required to maintain cell envelope integrity in Escherichia coli PLoS One 2008, 3 (2) e1573
    • (2008) PLoS One , vol.3 , Issue.2 , pp. 1573
    • Hayden, J.D.1    Ades, S.E.2
  • 56
    • 14844309359 scopus 로고    scopus 로고
    • E- dependent response of Escherichia coli
    • DOI 10.1111/j.1365-2958.2005.04497.x
    • E-dependent response of Escherichia coli Mol. Microbiol. 2005, 55, 1403-1412 (Pubitemid 40342068)
    • (2005) Molecular Microbiology , vol.55 , Issue.5 , pp. 1403-1412
    • Tam, C.1    Missiakas, D.2
  • 58
    • 59849101362 scopus 로고    scopus 로고
    • The type VI secretion system: Translocation of effectors and effector-domains
    • Pukatzki, S.; McAuley, S. B.; Miyata, S. T. The type VI secretion system: translocation of effectors and effector-domains Curr. Opin. Microbiol. 2009, 12, 11-17
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 11-17
    • Pukatzki, S.1    McAuley, S.B.2    Miyata, S.T.3
  • 59
    • 62249186821 scopus 로고    scopus 로고
    • Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis
    • Pieper, R.; Huang, S. T.; Robinson, J. M.; Clark, D. J.; Alami, H.; Parmar, P. P.; Perry, R. D.; Fleischmann, R. D.; Peterson, S. N. Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis Microbiology 2009, 155, 498-5102
    • (2009) Microbiology , vol.155 , pp. 498-5102
    • Pieper, R.1    Huang, S.T.2    Robinson, J.M.3    Clark, D.J.4    Alami, H.5    Parmar, P.P.6    Perry, R.D.7    Fleischmann, R.D.8    Peterson, S.N.9
  • 60
    • 77956632119 scopus 로고    scopus 로고
    • Canonical and ECF-type ATP-binding cassette importers in prokaryotes: Diversity in modular organization and cellular functions
    • Eitinger, T.; Rodionov, D. A.; Grote, M.; Schneider, E. Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions FEMS Microbiol. Rev. 2011, 35, 3-67
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 3-67
    • Eitinger, T.1    Rodionov, D.A.2    Grote, M.3    Schneider, E.4
  • 61
    • 0141852840 scopus 로고    scopus 로고
    • The tripartite tricarboxylate transporter (TTT) family
    • DOI 10.1016/S0923-2508(03)00126-8
    • Winnen, B.; Hvorup, R. N.; Saier, M. H., Jr. The tripartite tricarboxylate transporter (TTT) family Res. Microbiol. 2003, 154, 457-465 (Pubitemid 37130247)
    • (2003) Research in Microbiology , vol.154 , Issue.7 , pp. 457-465
    • Winnen, B.1    Hvorup, R.N.2    Saier Jr., M.H.3
  • 62
    • 78649982124 scopus 로고    scopus 로고
    • Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea
    • Mulligan, C.; Fischer, M.; Thomas, G. H. Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea FEMS Microbiol. Rev. 2011, 35, 68-86
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 68-86
    • Mulligan, C.1    Fischer, M.2    Thomas, G.H.3
  • 63
    • 34548356914 scopus 로고    scopus 로고
    • Aer on the inside looking out: Paradigm for a PAS-HAMP role in sensing oxygen, redox and energy
    • DOI 10.1111/j.1365-2958.2007.05889.x
    • Taylor, B. L. Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy Mol. Microbiol. 2007, 65, 1415-1424 (Pubitemid 47347836)
    • (2007) Molecular Microbiology , vol.65 , Issue.6 , pp. 1415-1424
    • Taylor, B.L.1
  • 64
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • DOI 10.1146/annurev.micro.56.012302.160938
    • Mattick, J. S. Type IV pili and twitching motility Annu. Rev. Microbiol. 2002, 56, 289-314 (Pubitemid 35217457)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 289-314
    • Mattick, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.