메뉴 건너뛰기




Volumn 160, Issue PART 3, 2014, Pages 635-645

Extracellular gluco-oligosaccharide degradation by Caulobacter crescentus

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSIDASE; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; CELLOBIOSE; CELLULOSE; GLUCOSE; GLUCOSE OLIGOSACCHARIDE; OLIGOSACCHARIDE; OUTER MEMBRANE PROTEIN; TONB DEPENDENT RECEPTOR; UNCLASSIFIED DRUG;

EID: 84896822364     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.072314-0     Document Type: Article
Times cited : (9)

References (69)
  • 1
    • 0033306554 scopus 로고    scopus 로고
    • Multiple environmental factors regulate the expression of the carbohydrate-selective OprB porin of Pseudomonas aeruginosa
    • Adewoye, L. O. & Worobec, E. A. (1999). Multiple environmental factors regulate the expression of the carbohydrate-selective OprB porin of Pseudomonas aeruginosa. Can J Microbiol 45, 1033-1042.
    • (1999) Can J Microbiol , vol.45 , pp. 1033-1042
    • Adewoye, L.O.1    Worobec, E.A.2
  • 2
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames, G. F., Prody, C. & Kustu, S. (1984). Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol 160, 1181-1183.
    • (1984) J Bacteriol , vol.160 , pp. 1181-1183
    • Ames, G.F.1    Prody, C.2    Kustu, S.3
  • 3
    • 77951528613 scopus 로고    scopus 로고
    • Identification of a dehydrogenase required for lactose metabolism in Caulobacter crescentus
    • Arellano, B. H., Ortiz, J. D., Manzano, J. & Chen, J. C. (2010). Identification of a dehydrogenase required for lactose metabolism in Caulobacter crescentus. Appl Environ Microbiol 76, 3004-3014.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3004-3014
    • Arellano, B.H.1    Ortiz, J.D.2    Manzano, J.3    Chen, J.C.4
  • 4
    • 84455204799 scopus 로고    scopus 로고
    • Signal peptidase I: Cleaving the way to mature proteins
    • Auclair, S. M., Bhanu, M. K. & Kendall, D. A. (2012). Signal peptidase I: cleaving the way to mature proteins. Protein Sci 21, 13-25.
    • (2012) Protein Sci , vol.21 , pp. 13-25
    • Auclair, S.M.1    Bhanu, M.K.2    Kendall, D.A.3
  • 5
  • 6
    • 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. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 36549000742 scopus 로고    scopus 로고
    • Harnessing energy from plant biomass
    • Chang, M. C. (2007). Harnessing energy from plant biomass. Curr Opin Chem Biol 11, 677-684.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 677-684
    • Chang, M.C.1
  • 10
    • 0023234346 scopus 로고
    • Metabolism of aromatic compounds by Caulobacter crescentus
    • Chatterjee, D. K. & Bourquin, A. W. (1987). Metabolism of aromatic compounds by Caulobacter crescentus. J Bacteriol 169, 1993-1996.
    • (1987) J Bacteriol , vol.169 , pp. 1993-1996
    • Chatterjee, D.K.1    Bourquin, A.W.2
  • 11
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • In, Edited by H. J. Gilbert, G. Davies, B. Henrissat & B. Svensson. Cambridge: Royal Society of Chemistry
    • Coutinho, P. M. & Henrissat, B. (1999). Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering, pp. 3-12. Edited by H. J. Gilbert, G. Davies, B. Henrissat & B. Svensson. Cambridge: Royal Society of Chemistry.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 12
    • 84863111753 scopus 로고    scopus 로고
    • PePPER: A webserver for prediction of prokaryote promoter elements and regulons
    • de Jong, A., Pietersma, H., Cordes, M., Kuipers, O. P. & Kok, J. (2012). PePPER: a webserver for prediction of prokaryote promoter elements and regulons. BMC Genomics 13, 299.
    • (2012) BMC Genomics , vol.13 , pp. 299
    • de Jong, A.1    Pietersma, H.2    Cordes, M.3    Kuipers, O.P.4    Kok, J.5
  • 13
    • 67149137783 scopus 로고    scopus 로고
    • Role of gluconic acid production in the regulation of biocontrol traits of Pseudomonas fluorescens CHA0
    • de Werra, P., Péchy-Tarr, M., Keel, C. & Maurhofer, M. (2009). Role of gluconic acid production in the regulation of biocontrol traits of Pseudomonas fluorescens CHA0. Appl Environ Microbiol 75, 4162-4174.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 4162-4174
    • de Werra, P.1    Péchy-Tarr, M.2    Keel, C.3    Maurhofer, M.4
  • 14
    • 78651112208 scopus 로고    scopus 로고
    • Xylan degradation, a metabolic property shared by rumen and human colonic Bacteroidetes
    • Dodd, D., Mackie, R. I. & Cann, I. K. (2011). Xylan degradation, a metabolic property shared by rumen and human colonic Bacteroidetes. Mol Microbiol 79, 292-304.
    • (2011) Mol Microbiol , vol.79 , pp. 292-304
    • Dodd, D.1    McKie, R.I.2    Cann, I.K.3
  • 15
    • 48149089820 scopus 로고    scopus 로고
    • NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus
    • Eisenbeis, S., Lohmiller, S., Valdebenito, M., Leicht, S. & Braun, V. (2008). NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus. J Bacteriol 190, 5230-5238.
    • (2008) J Bacteriol , vol.190 , pp. 5230-5238
    • Eisenbeis, S.1    Lohmiller, S.2    Valdebenito, M.3    Leicht, S.4    Braun, V.5
  • 16
    • 0025888266 scopus 로고
    • Genetics of Caulobacter crescentus
    • Ely, B. (1991). Genetics of Caulobacter crescentus. Methods Enzymol 204, 372-384.
    • (1991) Methods Enzymol , vol.204 , pp. 372-384
    • Ely, B.1
  • 17
    • 0019190802 scopus 로고
    • Protein D1-a glucoseinducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa
    • Hancock, R. E. W. & Carey, A. M. (1980). Protein D1-a glucoseinducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa. FEMS Microbiol Lett 8, 105-109.
    • (1980) FEMS Microbiol Lett , vol.8 , pp. 105-109
    • Hancock, R.E.W.1    Carey, A.M.2
  • 18
    • 0034333059 scopus 로고    scopus 로고
    • Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases
    • Harvey, A. J., Hrmova, M., De Gori, R., Varghese, J. N. & Fincher, G. B. (2000). Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins 41, 257-269.
    • (2000) Proteins , vol.41 , pp. 257-269
    • Harvey, A.J.1    Hrmova, M.2    De Gori, R.3    Varghese, J.N.4    Fincher, G.B.5
  • 19
    • 0023039710 scopus 로고
    • Microbial life at extremely low nutrient levels
    • Hirsch, P. (1986). Microbial life at extremely low nutrient levels. Adv Space Res 6, 287-298.
    • (1986) Adv Space Res , vol.6 , pp. 287-298
    • Hirsch, P.1
  • 20
    • 1342325451 scopus 로고    scopus 로고
    • Transcriptional profiling of Caulobacter crescentus during growth on complex and minimal media
    • Hottes, A. K., Meewan, M., Yang, D., Arana, N., Romero, P., McAdams, H. H. & Stephens, C. (2004). Transcriptional profiling of Caulobacter crescentus during growth on complex and minimal media. J Bacteriol 186, 1448-1461.
    • (2004) J Bacteriol , vol.186 , pp. 1448-1461
    • Hottes, A.K.1    Meewan, M.2    Yang, D.3    Arana, N.4    Romero, P.5    McAdams, H.H.6    Stephens, C.7
  • 21
    • 0027439791 scopus 로고
    • Purification and properties of three (1A3)-b-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • Hrmova, M. & Fincher, G. B. (1993). Purification and properties of three (1A3)-b-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare). Biochem J 289, 453-461.
    • (1993) Biochem J , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 22
    • 0032079561 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of a barley b-D-glucosidase/(1,4)-b-D-glucan exohydrolase
    • Hrmova, M., MacGregor, E. A., Biely, P., Stewart, R. J. & Fincher, G. B. (1998). Substrate binding and catalytic mechanism of a barley b-D-glucosidase/(1,4)-b-D-glucan exohydrolase. J Biol Chem 273, 11134-11143.
    • (1998) J Biol Chem , vol.273 , pp. 11134-11143
    • Hrmova, M.1    McGregor, E.A.2    Biely, P.3    Stewart, R.J.4    Fincher, G.B.5
  • 23
    • 0036037333 scopus 로고    scopus 로고
    • Proteomic analysis of the Caulobacter crescentus stalk indicates competence for nutrient uptake
    • Ireland, M. M., Karty, J. A., Quardokus, E. M., Reilly, J. P. & Brun, Y. V. (2002). Proteomic analysis of the Caulobacter crescentus stalk indicates competence for nutrient uptake. Mol Microbiol 45, 1029-1041.
    • (2002) Mol Microbiol , vol.45 , pp. 1029-1041
    • Ireland, M.M.1    Karty, J.A.2    Quardokus, E.M.3    Reilly, J.P.4    Brun, Y.V.5
  • 24
    • 0026085431 scopus 로고
    • Direct evidence of the Entner-Doudoroff pathway operating in the metabolism of D-glucosamine in bacteria
    • Iwamoto, R. & Imanaga, Y. (1991). Direct evidence of the Entner-Doudoroff pathway operating in the metabolism of D-glucosamine in bacteria. J Biochem 109, 66-69.
    • (1991) J Biochem , vol.109 , pp. 66-69
    • Iwamoto, R.1    Imanaga, Y.2
  • 26
    • 0030237081 scopus 로고    scopus 로고
    • Cloning and characterization of a xylanase gene from corn strains of Erwinia chrysanthemi
    • Keen, N. T., Boyd, C. & Henrissat, B. (1996). Cloning and characterization of a xylanase gene from corn strains of Erwinia chrysanthemi. Mol Plant Microbe Interact 9, 651-657.
    • (1996) Mol Plant Microbe Interact , vol.9 , pp. 651-657
    • Keen, N.T.1    Boyd, C.2    Henrissat, B.3
  • 27
    • 0033151643 scopus 로고    scopus 로고
    • Ribosomal DNA sequencing as a tool for identification of bacterial pathogens
    • Kolbert, C. P. & Persing, D. H. (1999). Ribosomal DNA sequencing as a tool for identification of bacterial pathogens. Curr Opin Microbiol 2, 299-305.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 299-305
    • Kolbert, C.P.1    Persing, D.H.2
  • 28
    • 0001452722 scopus 로고
    • Colorimetric methods with glucose oxidase and peroxidase
    • In, 3rd edn, Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie
    • Kunst, A., Draeger, B. & Ziegenhorn, J. (1984). Colorimetric methods with glucose oxidase and peroxidase. In Methods of Enzymatic Analysis, 3rd edn, pp. 178-185. Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie.
    • (1984) Methods of Enzymatic Analysis , pp. 178-185
    • Kunst, A.1    Draeger, B.2    Ziegenhorn, J.3
  • 29
    • 0027438886 scopus 로고
    • Isolation and characterization of the outer membrane proteins of Serratia marcescens W225
    • Larsen, B. S. & Biedermann, K. (1993). Isolation and characterization of the outer membrane proteins of Serratia marcescens W225. Anal Biochem 214, 212-221.
    • (1993) Anal Biochem , vol.214 , pp. 212-221
    • Larsen, B.S.1    Biedermann, K.2
  • 31
    • 0033775823 scopus 로고    scopus 로고
    • Periplasmic localization of a GroES homologue in Escherichia coli transformed with groESx cloned from Legionella-like endosymbionts in Amoeba proteus
    • Lee, J. E. & Ahn, T. I. (2000). Periplasmic localization of a GroES homologue in Escherichia coli transformed with groESx cloned from Legionella-like endosymbionts in Amoeba proteus. Res Microbiol 151, 605-618.
    • (2000) Res Microbiol , vol.151 , pp. 605-618
    • Lee, J.E.1    Ahn, T.I.2
  • 32
    • 0021119496 scopus 로고
    • Alternative pathways of carbohydrate utilization in pseudomonads
    • Lessie, T. G. & Phibbs, P. V., Jr (1984). Alternative pathways of carbohydrate utilization in pseudomonads. Annu Rev Microbiol 38, 359-388.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 359-388
    • Lessie, T.G.1    Phibbs Jr., P.V.2
  • 33
    • 34249740743 scopus 로고    scopus 로고
    • Processivity, substrate binding, and mechanism of cellulose hydrolysis by Thermobifida fusca Cel9A
    • Li, Y., Irwin, D. C. & Wilson, D. B. (2007). Processivity, substrate binding, and mechanism of cellulose hydrolysis by Thermobifida fusca Cel9A. Appl Environ Microbiol 73, 3165-3172.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3165-3172
    • Li, Y.1    Irwin, D.C.2    Wilson, D.B.3
  • 34
    • 48149098237 scopus 로고    scopus 로고
    • TonBdependent maltose transport by Caulobacter crescentus
    • Lohmiller, S., Hantke, K., Patzer, S. I. & Braun, V. (2008). TonBdependent maltose transport by Caulobacter crescentus. Microbiology 154, 1748-1754.
    • (2008) Microbiology , vol.154 , pp. 1748-1754
    • Lohmiller, S.1    Hantke, K.2    Patzer, S.I.3    Braun, V.4
  • 35
    • 0029122231 scopus 로고
    • Purification and characterization of a cellulose-binding b-glucosidase from cellulosedegrading cultures of Phanerochaete chrysosporium
    • Lymar, E. S., Li, B. & Renganathan, V. (1995). Purification and characterization of a cellulose-binding b-glucosidase from cellulosedegrading cultures of Phanerochaete chrysosporium. Appl Environ Microbiol 61, 2976-2980.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2976-2980
    • Lymar, E.S.1    Li, B.2    Renganathan, V.3
  • 36
    • 0009135497 scopus 로고
    • Microflora participating in the decomposition of carboxymethyl cellulose continuously added to the soil
    • Mašková, H. P., Vasilyeva, L. V., Kofroňova, O. & Kunc, F. (1988). Microflora participating in the decomposition of carboxymethyl cellulose continuously added to the soil. Folia Microbiol (Prague) 33, 482-490.
    • (1988) Folia Microbiol (Prague) , vol.33 , pp. 482-490
    • Mašková, H.P.1    Vasilyeva, L.V.2    Kofroňova, O.3    Kunc, F.4
  • 37
    • 0020390361 scopus 로고
    • D-Gluconate dehydrogenase from bacteria, 2-keto-D-gluconate-yielding, membrane-bound
    • Matsushita, K., Shinagawa, E. & Ameyama, M. (1982). D-Gluconate dehydrogenase from bacteria, 2-keto-D-gluconate-yielding, membrane-bound. Methods Enzymol 89, 187-193.
    • (1982) Methods Enzymol , vol.89 , pp. 187-193
    • Matsushita, K.1    Shinagawa, E.2    Ameyama, M.3
  • 39
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu, H. C. & Heppel, L. A. (1965). The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem 240, 3685-3692.
    • (1965) J Biol Chem , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 40
    • 28844503096 scopus 로고    scopus 로고
    • ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus
    • Neugebauer, H., Herrmann, C., Kammer, W., Schwarz, G., Nordheim, A. & Braun, V. (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    Herrmann, C.2    Kammer, W.3    Schwarz, G.4    Nordheim, A.5    Braun, V.6
  • 42
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • Nikaido, H. (1994). Porins and specific diffusion channels in bacterial outer membranes. J Biol Chem 269, 3905-3908.
    • (1994) J Biol Chem , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 43
    • 37348999824 scopus 로고    scopus 로고
    • A novel vector for positive selection of inserts harboring an open reading frame by translational coupling
    • Ohashi-Kunihiro, S., Yohda, M., Masaki, H. & Machida, M. (2007). A novel vector for positive selection of inserts harboring an open reading frame by translational coupling. Biotechniques 43, 751-752, 754.
    • (2007) Biotechniques , vol.43
    • Ohashi-Kunihiro, S.1    Yohda, M.2    Masaki, H.3    McHida, M.4
  • 45
    • 0032464663 scopus 로고    scopus 로고
    • What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli
    • Peekhaus, N. & Conway, T. (1998). What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli. J Bacteriol 180, 3495-3502.
    • (1998) J Bacteriol , vol.180 , pp. 3495-3502
    • Peekhaus, N.1    Conway, T.2
  • 46
    • 0031056355 scopus 로고    scopus 로고
    • Characterization of a novel transporter family that includes multiple Escherichia coli gluconate transporters and their homologues
    • Peekhaus, N., Tong, S., Reizer, J., Saier, M. H., Jr, Murray, E. & Conway, T. (1997). Characterization of a novel transporter family that includes multiple Escherichia coli gluconate transporters and their homologues. FEMS Microbiol Lett 147, 233-238.
    • (1997) FEMS Microbiol Lett , vol.147 , pp. 233-238
    • Peekhaus, N.1    Tong, S.2    Reizer, J.3    Saier Jr., M.H.4    Murray, E.5    Conway, T.6
  • 47
    • 0000552888 scopus 로고
    • Biological properties and classification of the Caulobacter group
    • Poindexter, J. S. (1964). Biological properties and classification of the Caulobacter group. Bacteriol Rev 28, 231-295.
    • (1964) Bacteriol Rev , vol.28 , pp. 231-295
    • Poindexter, J.S.1
  • 48
    • 34248647893 scopus 로고    scopus 로고
    • TonB-dependent energy transduction between outer and cytoplasmic membranes
    • Postle, K. & Larsen, R. A. (2007). TonB-dependent energy transduction between outer and cytoplasmic membranes. Biometals 20, 453-465.
    • (2007) Biometals , vol.20 , pp. 453-465
    • Postle, K.1    Larsen, R.A.2
  • 49
    • 58149110766 scopus 로고    scopus 로고
    • Translational coupling controls expression and function of the DrrAB drug efflux pump
    • Pradhan, P., Li, W. & Kaur, P. (2009). Translational coupling controls expression and function of the DrrAB drug efflux pump. J Mol Biol 385, 831-842.
    • (2009) J Mol Biol , vol.385 , pp. 831-842
    • Pradhan, P.1    Li, W.2    Kaur, P.3
  • 51
    • 0017210105 scopus 로고
    • Pathway of glucose catabolism in Caulobacter crescentus
    • Riley, R. G. & Kolodziej, B. J. (1976). Pathway of glucose catabolism in Caulobacter crescentus. Microbios 16, 219-226.
    • (1976) Microbios , vol.16 , pp. 219-226
    • Riley, R.G.1    Kolodziej, B.J.2
  • 53
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • Sakon, J., Irwin, D., Wilson, D. B. & Karplus, P. A. (1997). Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nat Struct Biol 4, 810-818.
    • (1997) Nat Struct Biol , vol.4 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Karplus, P.A.4
  • 54
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonB-dependent transport: Do we only see the 'tip of the iceberg'?
    • Schauer, K., Rodionov, D. A. & de Reuse, H. (2008). New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? Trends Biochem Sci 33, 330-338.
    • (2008) Trends Biochem Sci , vol.33 , pp. 330-338
    • Schauer, K.1    Rodionov, D.A.2    de Reuse, H.3
  • 55
    • 77951652612 scopus 로고    scopus 로고
    • Gneg-mPLoc: A top-down strategy to enhance the quality of predicting subcellular localization of Gramnegative bacterial proteins
    • Shen, H. B. & Chou, K. C. (2010). Gneg-mPLoc: a top-down strategy to enhance the quality of predicting subcellular localization of Gramnegative bacterial proteins. J Theor Biol 264, 326-333.
    • (2010) J Theor Biol , vol.264 , pp. 326-333
    • Shen, H.B.1    Chou, K.C.2
  • 56
    • 79955756112 scopus 로고    scopus 로고
    • Repression of the glucose-inducible outermembrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86
    • Shrivastava, R., Basu, B., Godbole, A., Mathew, M. K., Apte, S. K. & Phale, P. S. (2011). Repression of the glucose-inducible outermembrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86. Microbiology 157, 1531-1540.
    • (2011) Microbiology , vol.157 , pp. 1531-1540
    • Shrivastava, R.1    Basu, B.2    Godbole, A.3    Mathew, M.K.4    Apte, S.K.5    Phale, P.S.6
  • 57
    • 16544376249 scopus 로고    scopus 로고
    • Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies
    • Sigdel, T. K., Cilliers, R., Gursahaney, P. R. & Crowder, M. W. (2004). Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies. J Biomol Tech 15, 199-207.
    • (2004) J Biomol Tech , vol.15 , pp. 199-207
    • Sigdel, T.K.1    Cilliers, R.2    Gursahaney, P.R.3    Crowder, M.W.4
  • 58
    • 84872912493 scopus 로고    scopus 로고
    • Cellulose degradation by one mesophilic strain Caulobacter sp. FMC1 under both aerobic and anaerobic conditions
    • Song, N., Cai, H. Y., Yan, Z. S. & Jiang, H. L. (2013). Cellulose degradation by one mesophilic strain Caulobacter sp. FMC1 under both aerobic and anaerobic conditions. Bioresour Technol 131, 281-287.
    • (2013) Bioresour Technol , vol.131 , pp. 281-287
    • Song, N.1    Cai, H.Y.2    Yan, Z.S.3    Jiang, H.L.4
  • 59
    • 37449012593 scopus 로고    scopus 로고
    • Regulation of D-xylose metabolism in Caulobacter crescentus by a LacI-type repressor
    • Stephens, C., Christen, B., Watanabe, K., Fuchs, T. & Jenal, U. (2007). Regulation of D-xylose metabolism in Caulobacter crescentus by a LacI-type repressor. J Bacteriol 189, 8828-8834.
    • (2007) J Bacteriol , vol.189 , pp. 8828-8834
    • Stephens, C.1    Christen, B.2    Watanabe, K.3    Fuchs, T.4    Jenal, U.5
  • 60
    • 1542673165 scopus 로고    scopus 로고
    • On the mechanism of solute uptake in Pseudomonas
    • Tamber, S. & Hancock, R. E. (2003). On the mechanism of solute uptake in Pseudomonas. Front Biosci 8, s472-s483.
    • (2003) Front Biosci , vol.8
    • Tamber, S.1    Hancock, R.E.2
  • 61
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in Gram-negative bacteria
    • Tokuda, H. (2009). Biogenesis of outer membranes in Gram-negative bacteria. Biosci Biotechnol Biochem 73, 465-473.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 62
    • 13844318282 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda, H. & Matsuyama, S. (2004). Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 1694, IN1-IN9.
    • (2004) Biochim Biophys Acta , vol.1694
    • Tokuda, H.1    Matsuyama, S.2
  • 63
    • 59149106674 scopus 로고    scopus 로고
    • Probing mechanisms of axonopathy. Part II: Protein targets of 2,5-hexanedione, the neurotoxic metabolite of the aliphatic solvent n-hexane
    • Tshala-Katumbay, D., Monterroso, V., Kayton, R., Lasarev, M., Sabri, M. & Spencer, P. (2009). Probing mechanisms of axonopathy. Part II: protein targets of 2,5-hexanedione, the neurotoxic metabolite of the aliphatic solvent n-hexane. Toxicol Sci 107, 482-489.
    • (2009) Toxicol Sci , vol.107 , pp. 482-489
    • Tshala-Katumbay, D.1    Monterroso, V.2    Kayton, R.3    Lasarev, M.4    Sabri, M.5    Spencer, P.6
  • 64
    • 84870354012 scopus 로고    scopus 로고
    • Structural basis for outer membrane sugar uptake in pseudomonads
    • van den Berg, B. (2012). Structural basis for outer membrane sugar uptake in pseudomonads. J Biol Chem 287, 41044-41052.
    • (2012) J Biol Chem , vol.287 , pp. 41044-41052
    • van den Berg, B.1
  • 65
    • 79955133850 scopus 로고    scopus 로고
    • The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol
    • Wu, X., Lei, L., Gong, S., Chen, D., Flores, R. & Zhong, G. (2011). The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol. BMC Microbiol 11, 87-102.
    • (2011) BMC Microbiol , vol.11 , pp. 87-102
    • Wu, X.1    Lei, L.2    Gong, S.3    Chen, D.4    Flores, R.5    Zhong, G.6
  • 66
    • 0029056666 scopus 로고
    • The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa
    • Wylie, J. L. & Worobec, E. A. (1995). The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa. J Bacteriol 177, 3021-3026.
    • (1995) J Bacteriol , vol.177 , pp. 3021-3026
    • Wylie, J.L.1    Worobec, E.A.2
  • 67
    • 6344235016 scopus 로고    scopus 로고
    • Nature's many mechanisms for the degradation of oligosaccharides
    • Yip, V. L. & Withers, S. G. (2004). Nature's many mechanisms for the degradation of oligosaccharides. Org Biomol Chem 2, 2707-2713.
    • (2004) Org Biomol Chem , vol.2 , pp. 2707-2713
    • Yip, V.L.1    Withers, S.G.2
  • 68
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • other authors
    • Yu, N. Y., Wagner, J. R., Laird, M. R., Melli, G., Rey, S., Lo, R., Dao, P., Sahinalp, S. C., Ester, M. & other authors (2010). PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26, 1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6    Dao, P.7    Sahinalp, S.C.8    Ester, M.9
  • 69
    • 3343001971 scopus 로고    scopus 로고
    • Kinetic studies of Thermobifida fusca Cel9A active site mutant enzymes
    • Zhou, W., Irwin, D. C., Escovar-Kousen, J. & Wilson, D. B. (2004). Kinetic studies of Thermobifida fusca Cel9A active site mutant enzymes. Biochemistry 43, 9655-9663.
    • (2004) Biochemistry , vol.43 , pp. 9655-9663
    • Zhou, W.1    Irwin, D.C.2    Escovar-Kousen, J.3    Wilson, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.