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Volumn 77, Issue 4, 2011, Pages 1276-1283

Cytoplasmic and periplasmic proteomic signatures of exponentially growing cells of the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125

Author keywords

[No Author keywords available]

Indexed keywords

ACID DEGRADATION; CELLULAR COMPARTMENTS; COLD ACCLIMATIONS; COPIOTROPHIC BACTERIA; EXPONENTIAL GROWTH; FAST GROWTH RATE; HIGH CAPACITY; LOW TEMPERATURES; MARINE BACTERIUM; NATURAL ENVIRONMENTS; PERIPLASM; PERIPLASMIC PROTEINS; PROTEIN GEL; PROTEIN SYNTHESIS; PROTEOMES; PSEUDOALTEROMONAS HALOPLANKTIS; PSYCHROPHILIC BACTERIA; TRICARBOXYLIC ACIDS;

EID: 79953182010     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01750-10     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 0034821694 scopus 로고    scopus 로고
    • A proteomic view on genome-based signal peptide predictions
    • Antelmann, H., et al. 2001. A proteomic view on genome-based signal peptide predictions. Genome Res. 11:1484-1502.
    • (2001) Genome Res , vol.11 , pp. 1484-1502
    • Antelmann, H.1
  • 2
    • 0008298889 scopus 로고    scopus 로고
    • Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling
    • Birolo, L., et al. 2000. Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling. Eur. J. Biochem. 267:2790-2802.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2790-2802
    • Birolo, L.1
  • 3
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through tonBdependent receptors: a feature shared by phytopathogenic and aquatic bacteria
    • Blanvillain, S., et al. 2007. Plant carbohydrate scavenging through tonBdependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS One 2:e224.
    • (2007) PLoS One , vol.2
    • Blanvillain, S.1
  • 5
    • 0242657566 scopus 로고    scopus 로고
    • Diversity and structure of bacterial communities in Arctic versus Antarctic pack ice
    • Brinkmeyer, R., et al. 2003. Diversity and structure of bacterial communities in Arctic versus Antarctic pack ice. Appl. Environ. Microbiol. 69:6610-6619.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6610-6619
    • Brinkmeyer, R.1
  • 6
    • 77956310831 scopus 로고    scopus 로고
    • Mapping the subcellular proteome of Shewanella oneidensis MR-1 using sarkosyl-based fractionation and LC-MS/MS protein identification
    • Brown, R. N., M. F. Romine, A. A. Schepmoes, R. D. Smith, and M. S. Lipton. Mapping the subcellular proteome of Shewanella oneidensis MR-1 using sarkosyl-based fractionation and LC-MS/MS protein identification. J. Proteome Res. 9:4454-4463.
    • J. Proteome Res. , vol.9 , pp. 4454-4463
    • Brown, R.N.1    Romine, M.F.2    Schepmoes, A.A.3    Smith, R.D.4    Lipton, M.S.5
  • 7
    • 0034837018 scopus 로고    scopus 로고
    • A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis
    • Buttner, K., et al. 2001. A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22:2908-2935.
    • (2001) Electrophoresis , vol.22 , pp. 2908-2935
    • Buttner, K.1
  • 8
    • 0029061811 scopus 로고
    • Identification and characterization of a Bacteroides gene, csuF, which encodes an outer membrane protein that is essential for growth on chondroitin sulfate
    • Cheng, Q., M. C. Yu, A. R. Reeves, and A. A. Salyers. 1995. Identification and characterization of a Bacteroides gene, csuF, which encodes an outer membrane protein that is essential for growth on chondroitin sulfate. J. Bacteriol. 177:3721-3727.
    • (1995) J. Bacteriol. , vol.177 , pp. 3721-3727
    • Cheng, Q.1    Yu, M.C.2    Reeves, A.R.3    Salyers, A.A.4
  • 9
    • 77956401047 scopus 로고    scopus 로고
    • In-depth analysis of exoproteomes from marine bacteria by shotgun liquid chromatography-tandem mass spectrometry: the Ruegeria pomeroyi DSS-3 case-study
    • Christie-Oleza, J. A., and J. Armengaud. 2010. In-depth analysis of exoproteomes from marine bacteria by shotgun liquid chromatography-tandem mass spectrometry: the Ruegeria pomeroyi DSS-3 case-study. Mar. Drugs 8:2223-2239.
    • (2010) Mar. Drugs , vol.8 , pp. 2223-2239
    • Christie-Oleza, J.A.1    Armengaud, J.2
  • 10
    • 0037144574 scopus 로고    scopus 로고
    • A novel family 8 xylanase, functional and physicochemical characterization
    • Collins, T., et al. 2002. A novel family 8 xylanase, functional and physicochemical characterization. J. Biol. Chem. 277:35133-35139.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35133-35139
    • Collins, T.1
  • 11
  • 12
    • 33846573332 scopus 로고    scopus 로고
    • A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125
    • Cusano, A. M., E. Parrilli, G. Marino, and M. L. Tutino. 2006. A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125. Microb. Cell Fact. 5:40.
    • (2006) Microb. Cell Fact. , vol.5 , pp. 40
    • Cusano, A.M.1    Parrilli, E.2    Marino, G.3    Tutino, M.L.4
  • 13
    • 0031588599 scopus 로고    scopus 로고
    • Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP
    • Danchin, A. 1997. Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP. DNA Res. 4:9-18.
    • (1997) DNA Res , vol.4 , pp. 9-18
    • Danchin, A.1
  • 14
    • 43049159561 scopus 로고    scopus 로고
    • The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family
    • de Pascale, D., et al. 2008. The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family. Extremophiles 12:311-323.
    • (2008) Extremophiles , vol.12 , pp. 311-323
    • de Pascale, D.1
  • 15
    • 44549088305 scopus 로고    scopus 로고
    • Cloning, expression and physicochemical characterization of a di-heme cytochrome c (4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125
    • Di Rocco, G., et al. 2008. Cloning, expression and physicochemical characterization of a di-heme cytochrome c (4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125. J. Biol. Inorg. Chem. 13:789-799.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 789-799
    • Di Rocco, G.1
  • 16
    • 70350491086 scopus 로고    scopus 로고
    • Pseudoalteromonas bacteria are capable of degrading paralytic shellfish toxins
    • Donovan, C. J., et al. 2009. Pseudoalteromonas bacteria are capable of degrading paralytic shellfish toxins. Appl. Environ. Microbiol. 75:6919-6923.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6919-6923
    • Donovan, C.J.1
  • 17
    • 4644262701 scopus 로고    scopus 로고
    • Recombinant protein production in Antarctic Gram-negative bacteria
    • Duilio, A., M. L. Tutino, and G. Marino. 2004. Recombinant protein production in Antarctic Gram-negative bacteria. Methods Mol. Biol. 267:225-237.
    • (2004) Methods Mol. Biol. , vol.267 , pp. 225-237
    • Duilio, A.1    Tutino, M.L.2    Marino, G.3
  • 18
    • 69549127735 scopus 로고    scopus 로고
    • Molecular and functional characterization of polynucleotide phosphorylase from the Antarctic eubacterium Pseudoalteromonas haloplanktis
    • Evangelista, G., P. Falasca, I. Ruggiero, M. Masullo, and G. Raimo. 2009. Molecular and functional characterization of polynucleotide phosphorylase from the Antarctic eubacterium Pseudoalteromonas haloplanktis. Protein Pept. Lett. 16:999-1005.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 999-1005
    • Evangelista, G.1    Falasca, P.2    Ruggiero, I.3    Masullo, M.4    Raimo, G.5
  • 19
    • 33947588089 scopus 로고    scopus 로고
    • Profiling the secretome of the marine bacterium Pseudoalteromonas tunicata using amine-specific isobaric tagging (iTRAQ)
    • Evans, F. F., M. J. Raftery, S. Egan, and S. Kjelleberg. 2007. Profiling the secretome of the marine bacterium Pseudoalteromonas tunicata using amine-specific isobaric tagging (iTRAQ). J. Proteome Res. 6:967-975.
    • (2007) J. Proteome Res. , vol.6 , pp. 967-975
    • Evans, F.F.1    Raftery, M.J.2    Egan, S.3    Kjelleberg, S.4
  • 20
    • 5644302167 scopus 로고    scopus 로고
    • A comprehensive proteome map of growing Bacillus subtilis cells
    • Eymann, C., et al. 2004. A comprehensive proteome map of growing Bacillus subtilis cells. Proteomics 4:2849-2876.
    • (2004) Proteomics , vol.4 , pp. 2849-2876
    • Eymann, C.1
  • 21
    • 0032524655 scopus 로고    scopus 로고
    • Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis
    • Feller, G., et al. 1998. Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis. J. Biol. Chem. 273:12109-12115.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12109-12115
    • Feller, G.1
  • 22
    • 0035943737 scopus 로고    scopus 로고
    • Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E
    • Feng, Y., H. Huang, J. Liao, and S. N. Cohen. 2001. Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E. J. Biol. Chem. 276:31651-31656.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31651-31656
    • Feng, Y.1    Huang, H.2    Liao, J.3    Cohen, S.N.4
  • 23
    • 0033797930 scopus 로고    scopus 로고
    • Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations
    • Fulda, S., F. Huang, F. Nilsson, M. Hagemann, and B. Norling. 2000. Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations. Eur. J. Biochem. 267:5900-5907.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5900-5907
    • Fulda, S.1    Huang, F.2    Nilsson, F.3    Hagemann, M.4    Norling, B.5
  • 24
    • 0028799334 scopus 로고
    • Phylogenetic analysis of the genera Alteromonas, Shewanella, and Moritella using genes coding for small-subunit rRNA sequences and division of the genus Alteromonas into two genera, Alteromonas (emended) and Pseudoalteromonas gen. nov., and proposal of twelve new species combinations
    • Gauthier, G., M. Gauthier, and R. Christen. 1995. Phylogenetic analysis of the genera Alteromonas, Shewanella, and Moritella using genes coding for small-subunit rRNA sequences and division of the genus Alteromonas into two genera, Alteromonas (emended) and Pseudoalteromonas gen. nov., and proposal of twelve new species combinations. Int. J. Syst. Bacteriol. 45:755-761.
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 755-761
    • Gauthier, G.1    Gauthier, M.2    Christen, R.3
  • 25
    • 0033946342 scopus 로고    scopus 로고
    • A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
    • Georlette, D., et al. 2000. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur. J. Biochem. 267:3502-3512.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3502-3512
    • Georlette, D.1
  • 26
    • 42549127375 scopus 로고    scopus 로고
    • Detailed proteome analysis of growing cells of the planctomycete Rhodopirellula baltica SH1T
    • Hieu, C. X., et al. 2008. Detailed proteome analysis of growing cells of the planctomycete Rhodopirellula baltica SH1T. Proteomics 8:1608-1623.
    • (2008) Proteomics , vol.8 , pp. 1608-1623
    • Hieu, C.X.1
  • 27
    • 0024797460 scopus 로고
    • Simulation of bacterial attraction and adhesion to falling particles in an aquatic environment
    • Jackson, G. A. 1989. Simulation of bacterial attraction and adhesion to falling particles in an aquatic environment. Limnol. Oceanogr. 34:514-530.
    • (1989) Limnol. Oceanogr. , vol.34 , pp. 514-530
    • Jackson, G.A.1
  • 28
    • 0034074410 scopus 로고    scopus 로고
    • rRNA operon copy number reflects ecological strategies of bacteria
    • Klappenbach, J. A., J. M. Dunbar, and T. M. Schmidt. 2000. rRNA operon copy number reflects ecological strategies of bacteria. Appl. Environ. Microbiol. 66:1328-1333.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1328-1333
    • Klappenbach, J.A.1    Dunbar, J.M.2    Schmidt, T.M.3
  • 29
    • 72249097352 scopus 로고    scopus 로고
    • Growth rate-dependent global effects on gene expression in bacteria
    • Klumpp, S., Z. Zhang, and T. Hwa. 2009. Growth rate-dependent global effects on gene expression in bacteria. Cell 139:1366-1375.
    • (2009) Cell , vol.139 , pp. 1366-1375
    • Klumpp, S.1    Zhang, Z.2    Hwa, T.3
  • 30
    • 0029560596 scopus 로고
    • Quelling the red menace: haem capture by bacteria
    • Lee, B. C. 1995. Quelling the red menace: haem capture by bacteria. Mol. Microbiol. 18:383-390.
    • (1995) Mol. Microbiol. , vol.18 , pp. 383-390
    • Lee, B.C.1
  • 32
    • 25844462537 scopus 로고    scopus 로고
    • Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125
    • Medigue, C., et al. 2005. Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Res. 15:1325-1335.
    • (2005) Genome Res , vol.15 , pp. 1325-1335
    • Medigue, C.1
  • 33
    • 43549114985 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis
    • Merlino, A., et al. 2008. Crystallization and preliminary X-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis. Protein Pept. Lett. 15:415-418.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 415-418
    • Merlino, A.1
  • 34
    • 67649286245 scopus 로고    scopus 로고
    • Assessment of the microbial diversity at the surface of Livarot cheese using culture-dependent and independent approaches
    • Mounier, J., C. Monnet, N. Jacques, A. Antoinette, and F. Irlinger. 2009. Assessment of the microbial diversity at the surface of Livarot cheese using culture-dependent and independent approaches. Int. J. Food Microbiol. 133:31-37.
    • (2009) Int. J. Food Microbiol. , vol.133 , pp. 31-37
    • Mounier, J.1    Monnet, C.2    Jacques, N.3    Antoinette, A.4    Irlinger, F.5
  • 35
    • 36448975770 scopus 로고    scopus 로고
    • Characterization of RagA and RagB in Porphyromonas gingivalis: study using gene-deletion mutants
    • Nagano, K., et al. 2007. Characterization of RagA and RagB in Porphyromonas gingivalis: study using gene-deletion mutants. J. Med. Microbiol. 56: 1536-1548.
    • (2007) J. Med. Microbiol. , vol.56 , pp. 1536-1548
    • Nagano, K.1
  • 36
    • 28844503096 scopus 로고    scopus 로고
    • ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus
    • Neugebauer, H., et al. 2005. ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus. J. Bacteriol. 187:8300-8311.
    • (2005) J. Bacteriol. , vol.187 , pp. 8300-8311
    • Neugebauer, H.1
  • 37
    • 33751110612 scopus 로고    scopus 로고
    • Proteomic identification of a two-component regulatory system in Pseudoalteromonas haloplanktis TAC125
    • Papa, R., et al. 2006. Proteomic identification of a two-component regulatory system in Pseudoalteromonas haloplanktis TAC125. Extremophiles 10:483-491.
    • (2006) Extremophiles , vol.10 , pp. 483-491
    • Papa, R.1
  • 38
    • 77950281429 scopus 로고    scopus 로고
    • Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
    • Piette, F., et al. 2010. Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Mol. Microbiol. 76:120-132.
    • (2010) Mol. Microbiol. , vol.76 , pp. 120-132
    • Piette, F.1
  • 39
    • 0030066558 scopus 로고    scopus 로고
    • A Bacteroides thetaiotaomicron outer membrane protein that is essential for utilization of maltooligosaccharides and starch
    • Reeves, A. R., J. N. D'Elia, J. Frias, and A. A. Salyers. 1996. A Bacteroides thetaiotaomicron outer membrane protein that is essential for utilization of maltooligosaccharides and starch. J. Bacteriol. 178:823-830.
    • (1996) J. Bacteriol. , vol.178 , pp. 823-830
    • Reeves, A.R.1    D'Elia, J.N.2    Frias, J.3    Salyers, A.A.4
  • 40
    • 0015891782 scopus 로고
    • Change of the name Alteromonas marinopraesens (ZoBell and Upham) Baumann et al. to Alteromonas haloplanktis (ZoBell and Upham) comb. nov. and assignment of strain ATCC 23821 (Pseudomonas enalia) and strain c-A1 of De Voe and Oginsky to this species
    • Reichelt, J. L., and P. Baumann. 1973. Change of the name Alteromonas marinopraesens (ZoBell and Upham) Baumann et al. to Alteromonas haloplanktis (ZoBell and Upham) comb. nov. and assignment of strain ATCC 23821 (Pseudomonas enalia) and strain c-A1 of De Voe and Oginsky to this species. Int. J. Syst. Bacteriol. 23:438-441.
    • (1973) Int. J. Syst. Bacteriol. , vol.23 , pp. 438-441
    • Reichelt, J.L.1    Baumann, P.2
  • 41
    • 33846627273 scopus 로고    scopus 로고
    • Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery
    • Schauer, K., B. Gouget, M. Carriere, A. Labigne, and H. de Reuse. 2007. Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery. Mol. Microbiol. 63:1054-1068.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1054-1068
    • Schauer, K.1    Gouget, B.2    Carriere, M.3    Labigne, A.4    de Reuse, H.5
  • 43
    • 34248392177 scopus 로고    scopus 로고
    • Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis
    • Srimathi, S., G. Jayaraman, G. Feller, B. Danielsson, and P. R. Narayanan. 2007. Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis. Extremophiles 11:505-515.
    • (2007) Extremophiles , vol.11 , pp. 505-515
    • Srimathi, S.1    Jayaraman, G.2    Feller, G.3    Danielsson, B.4    Narayanan, P.R.5
  • 44
    • 41949138474 scopus 로고    scopus 로고
    • Rapid chemotactic response enables marine bacteria to exploit ephemeral microscale nutrient patches
    • Stocker, R., J. R. Seymour, A. Samadani, D. E. Hunt, and M. F. Polz. 2008. Rapid chemotactic response enables marine bacteria to exploit ephemeral microscale nutrient patches. Proc. Natl. Acad. Sci. U. S. A. 105:4209-4214.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 4209-4214
    • Stocker, R.1    Seymour, J.R.2    Samadani, A.3    Hunt, D.E.4    Polz, M.F.5
  • 45
    • 0037711318 scopus 로고    scopus 로고
    • GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: molecular characterization and gene cloning
    • Tosco, A., et al. 2003. GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: molecular characterization and gene cloning. Extremophiles 7:17-28.
    • (2003) Extremophiles , vol.7 , pp. 17-28
    • Tosco, A.1
  • 46
    • 69549097399 scopus 로고    scopus 로고
    • Coldadapted esterases and lipases: from fundamentals to application
    • Tutino, M. L., G. di Prisco, G. Marino, and D. de Pascale. 2009. Coldadapted esterases and lipases: from fundamentals to application. Protein Pept. Lett. 16:1172-1180.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 1172-1180
    • Tutino, M.L.1    di Prisco, G.2    Marino, G.3    de Pascale, D.4
  • 47
    • 0038455878 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis
    • Violot, S., et al. 2003. Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis. Acta Crystallogr. D Biol. Crystallogr. 59:1256-1258.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1256-1258
    • Violot, S.1
  • 48
    • 2442593658 scopus 로고    scopus 로고
    • A proteomic view of cell physiology of Bacillus licheniformis
    • Voigt, B., et al. 2004. A proteomic view of cell physiology of Bacillus licheniformis. Proteomics 4:1465-1490.
    • (2004) Proteomics , vol.4 , pp. 1465-1490
    • Voigt, B.1
  • 49
    • 13244249605 scopus 로고    scopus 로고
    • Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100
    • Watt, S. A., A. Wilke, T. Patschkowski, and K. Niehaus. 2005. Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100. Proteomics 5:153-167.
    • (2005) Proteomics , vol.5 , pp. 153-167
    • Watt, S.A.1    Wilke, A.2    Patschkowski, T.3    Niehaus, K.4
  • 50
    • 77956703910 scopus 로고    scopus 로고
    • Fed-batch process for the psychrotolerant marine bacterium Pseudoalteromonas haloplanktis
    • Wilmes, B., A. Hartung, M. Lalk, M. Liebeke, T. Schweder, and P. Neubauer. 2010. Fed-batch process for the psychrotolerant marine bacterium Pseudoalteromonas haloplanktis. Microb. Cell Fact. 9:72.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 72
    • Wilmes, B.1    Hartung, A.2    Lalk, M.3    Liebeke, M.4    Schweder, T.5    Neubauer, P.6
  • 51
    • 50249172221 scopus 로고    scopus 로고
    • Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus
    • Wolff, S., H. Hahne, M. Hecker, and D. Becher. 2008. Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus. Mol. Cell. Proteomics 7:1460-1468.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1460-1468
    • Wolff, S.1    Hahne, H.2    Hecker, M.3    Becher, D.4
  • 52
    • 0002685935 scopus 로고
    • Studies on marine bacteria. The cultural requirements of heterotrophic aerobes
    • Zobell, C. E. 1941. Studies on marine bacteria. The cultural requirements of heterotrophic aerobes. J. Mar. Res. 4:41-75.
    • (1941) J. Mar. Res. , vol.4 , pp. 41-75
    • Zobell, C.E.1


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