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Volumn 193, Issue 11, 2011, Pages 2838-2850

The L-arabinan utilization system of Geobacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ABNE PROTEIN; ABNEFJ PROTEIN; ALPHA ARABINOFURANOSIDASE; ARABINAN; ARABINASE; ARABINOSE; ARAP PROTEIN; ARAS PROTEIN; BACTERIAL PROTEIN; BETA LEVO ARABINOPYRANOSIDASE; CARBOHYDRATE BINDING PROTEIN; GLUCOSE; GLYCOSIDASE; LIPOPROTEIN; OLIGOSACCHARIDE; POLYSACCHARIDE; UNCLASSIFIED DRUG; XYLOSE;

EID: 79958097056     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00222-11     Document Type: Article
Times cited : (52)

References (80)
  • 1
    • 1542376954 scopus 로고    scopus 로고
    • DNA interaction and phosphotransfer of the C4-dicarboxylate-responsive DcuS-DcuR two-component regulatory system from Escherichia coli
    • Abo-Amer, A. E., et al. 2004. DNA interaction and phosphotransfer of the C4-dicarboxylate-responsive DcuS-DcuR two-component regulatory system from Escherichia coli. J. Bacteriol. 186:1879-1889.
    • (2004) J. Bacteriol. , vol.186 , pp. 1879-1889
    • Abo-Amer, A.E.1
  • 3
    • 68749112865 scopus 로고    scopus 로고
    • Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate
    • Alhassid, A., et al. 2009. Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with ts substrate. Biochem. J. 422:73-82.
    • (2009) Biochem. J. , vol.422 , pp. 73-82
    • Alhassid, A.1
  • 4
    • 70349281876 scopus 로고    scopus 로고
    • Engineering for biofuels: exploiting innate microbial capacity or importing biosynthetic potential
    • Alper, H., and G. Stephanopoulos. 2009. Engineering for biofuels: exploiting innate microbial capacity or importing biosynthetic potential. Nat. Rev. icrobiol. 7:715-723.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 715-723
    • Alper, H.1    Stephanopoulos, G.2
  • 6
    • 0034326854 scopus 로고    scopus 로고
    • CaChe-a signaling domain common to animal Ca(2)-channel subunits and a class of prokaryotic chemotaxis receptors
    • Anantharaman, V., and L. Aravind. 2000. CaChe-a signaling domain common to animal Ca(2)-channel subunits and a class of prokaryotic hemotaxis receptors. Trends Biochem. Sci. 25:535-537.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 535-537
    • Anantharaman, V.1    Aravind, L.2
  • 7
    • 33845977388 scopus 로고    scopus 로고
    • TorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli
    • Baraquet, C., et al. 2006. TorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli. J. Biol. Chem. 281:38189-38199.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38189-38199
    • Baraquet, C.1
  • 8
    • 1842506160 scopus 로고    scopus 로고
    • Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes
    • Barnard, A., A. Wolfe, and S. Busby. 2004. Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce ifferent regulatory outcomes. Curr. Opin. Microbiol. 7:102-108.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 102-108
    • Barnard, A.1    Wolfe, A.2    Busby, S.3
  • 9
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer, E. A., J. P. Belaich, Y. Shoham, and R. Lamed. 2004. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annu. Rev. Microbiol. 58:521-554.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.P.2    Shoham, Y.3    Lamed, R.4
  • 10
    • 0036583638 scopus 로고    scopus 로고
    • Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
    • Blanco, A. G., M. Sola, F. X. Gomis-Ruth, and M. Coll. 2002. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 10:701-713.
    • (2002) Structure , vol.10 , pp. 701-713
    • Blanco, A.G.1    Sola, M.2    Gomis-Ruth, F.X.3    Coll, M.4
  • 11
    • 3042777765 scopus 로고    scopus 로고
    • Genes regulated by TorR, the trimethylamine oxide response regulator of Shewanella oneidensis
    • Bordi, C., et al. 2004. Genes regulated by TorR, the trimethylamine oxide response regulator of Shewanella oneidensis. J. Bacteriol. 186:4502-509.
    • (2004) J. Bacteriol. , vol.186 , pp. 4502-4509
    • Bordi, C.1
  • 12
    • 0041816478 scopus 로고    scopus 로고
    • Detailed kinetic analysis of a family 52 glycoside hydrolase: a beta-xylosidase from Geobacillus stearothermophilus
    • Bravman, T., et al. 2003. Detailed kinetic analysis of a family 52 glycoside hydrolase: a beta-xylosidase from Geobacillus stearothermophilus. iochemistry 42:10528-10536.
    • (2003) Biochemistry , vol.42 , pp. 10528-10536
    • Bravman, T.1
  • 13
    • 33646165074 scopus 로고    scopus 로고
    • The structure of an inverting GH43 beta-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues
    • Brüx, C., et al. 2006. The structure of an inverting GH43 beta-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role f the three catalytic residues. J. Mol. Biol. 359:97-109.
    • (2006) J. Mol. Biol. , vol.359 , pp. 97-109
    • Brüx, C.1
  • 14
    • 26844535502 scopus 로고    scopus 로고
    • Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus
    • Czjzek, M., et al. 2005. Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus. J. Mol. Biol. 53:838-846.
    • (2005) J. Mol. Biol. , vol.353 , pp. 838-846
    • Czjzek, M.1
  • 15
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms
    • Dassa, E., and P. Bouige. 2001. The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 52:211-229.
    • (2001) Res. Microbiol. , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 17
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries, R. P., and J. Visser. 2001. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 5:497-522.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • de Vries, R.P.1    Visser, J.2
  • 18
    • 0026545567 scopus 로고
    • Assay of reducing end-groups in oligosaccharide homologues with 2,2'-bicinchoninate
    • Doner, L. W., and P. L. Irwin. 1992. Assay of reducing end-groups in oligosaccharide homologues with 2,2'-bicinchoninate. Anal. Biochem. 202:50-3.
    • (1992) Anal. Biochem. , vol.202 , pp. 50-53
    • Doner, L.W.1    Irwin, P.L.2
  • 19
    • 77956632119 scopus 로고    scopus 로고
    • Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions
    • Eitinger, T., D. A. Rodionov, M. Grote, and E. Schneider. 2011. Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions. FEMS Microbiol. Rev. 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
  • 20
    • 0029807051 scopus 로고    scopus 로고
    • Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry
    • Faergeman, N. J., B. W. Sigurskjold, B. B. Kragelund, K. V. Andersen, and J. Knudsen. 1996. Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry. Biochemistry 35:14118-14126.
    • (1996) Biochemistry , vol.35 , pp. 14118-14126
    • Faergeman, N.J.1    Sigurskjold, B.W.2    Kragelund, B.B.3    Andersen, K.V.4    Knudsen, J.5
  • 21
    • 31544462628 scopus 로고    scopus 로고
    • Ethanol can contribute to energy and environmental goals
    • Farrell, A. E., et al. 2006. Ethanol can contribute to energy and environmental goals. Science 311:506-508.
    • (2006) Science , vol.311 , pp. 506-508
    • Farrell, A.E.1
  • 22
    • 77957846779 scopus 로고    scopus 로고
    • A multitask ATPase serving different ABC-type sugar importers in Bacillus subtilis
    • Ferreira, M. J., and I. de Sa-Nogueíra. 2010. A multitask ATPase serving different ABC-type sugar importers in Bacillus subtilis. J. Bacteriol. 92: 5312-5318.
    • (2010) J. Bacteriol. , vol.192 , pp. 5312-5318
    • Ferreira, M.J.1    de Sa-Nogueíra, I.2
  • 23
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes, C. M., and H. J. Gilbert. 2010. Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. nnu. Rev. Biochem. 79:655-681.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 655-681
    • Fontes, C.M.1    Gilbert, H.J.2
  • 24
    • 0035026466 scopus 로고    scopus 로고
    • The molecular puzzle of two-component signaling cascades
    • Foussard, M., et al. 2001. The molecular puzzle of two-component signaling cascades. Microbes Infect. 3:417-424.
    • (2001) Microbes Infect , vol.3 , pp. 417-424
    • Foussard, M.1
  • 25
    • 77957347059 scopus 로고    scopus 로고
    • Cellodextrin transport in yeast for improved biofuel production
    • Galazka, J. M., et al. 2010. Cellodextrin transport in yeast for improved biofuel production. Science 330:84-86.
    • (2010) Science , vol.330 , pp. 84-86
    • Galazka, J.M.1
  • 27
    • 0028305577 scopus 로고
    • Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase
    • Gat, O., A. Lapidot, I. Alchanati, C. Regueros, and Y. Shoham. 1994. Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase. Appl. Environ. Microbiol. 60:1889-1896.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1889-1896
    • Gat, O.1    Lapidot, A.2    Alchanati, I.3    Regueros, C.4    Shoham, Y.5
  • 28
    • 77953219138 scopus 로고    scopus 로고
    • The biochemistry and structural biology of plant cell wall deconstruction
    • Gilbert, H. J. 2010. The biochemistry and structural biology of plant cell wall deconstruction. Plant Physiol. 153:444-455.
    • (2010) Plant Physiol , vol.153 , pp. 444-455
    • Gilbert, H.J.1
  • 29
    • 0024198129 scopus 로고
    • Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma
    • Gilson, E., et al. 1988. Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma. EMBO. 7:3971-3974.
    • (1988) EMBO J , vol.7 , pp. 3971-3974
    • Gilson, E.1
  • 30
    • 77949873448 scopus 로고    scopus 로고
    • Hemicelluloses for fuel ethanol: a review
    • Gírio, F. M., et al. 2010. Hemicelluloses for fuel ethanol: a review. Bioresour. Technol. 101:4775-4800.
    • (2010) Bioresour. Technol. , vol.101 , pp. 4775-4800
    • Gírio, F.M.1
  • 31
    • 0029041524 scopus 로고
    • Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA
    • Helmann, J. D. 1995. Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA. Nucleic Acids Res. 23: 2351-2360.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2351-2360
    • Helmann, J.D.1
  • 32
    • 0025023940 scopus 로고
    • Binding protein-dependent transport systems
    • Higgins, C. F., et al. 1990. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 22:571-592.
    • (1990) J. Bioenerg. Biomembr. , vol.22 , pp. 571-592
    • Higgins, C.F.1
  • 33
    • 17644434949 scopus 로고    scopus 로고
    • Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase
    • Hövel, K., et al. 2003. Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J. 22:4922-932.
    • (2003) EMBO J , vol.22 , pp. 4922-4932
    • Hövel, K.1
  • 34
    • 69949118732 scopus 로고    scopus 로고
    • A beta-l-arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27
    • Ichinose, H., et al. 2009. A beta-l-arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27. J. Biol. hem. 284:25097-25106.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25097-25106
    • Ichinose, H.1
  • 35
    • 53449083444 scopus 로고    scopus 로고
    • Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis
    • Inácio, J. M., I. L. Correia, and I. de Sa-Nogueíra. 2008. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in acillus subtilis. Microbiology 154:2719-2729.
    • (2008) Microbiology , vol.154 , pp. 2719-2729
    • Inácio, J.M.1    Correia, I.L.2    de Sa-Nogueíra, I.3
  • 36
    • 44949133209 scopus 로고    scopus 로고
    • Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabinopolysaccharide degradation
    • Inácio, J. M., and I. de Sa-Nogueíra. 2008. Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabinopolysaccharide degradation. J. Bacteriol. 190:4272-4280.
    • (2008) J. Bacteriol. , vol.190 , pp. 4272-4280
    • Inácio, J.M.1    de Sa-Nogueíra, I.2
  • 37
    • 0034813268 scopus 로고    scopus 로고
    • Sigma A recognition sites in the Bacillus subtilis genome
    • Jarmer, H., et al. 2001. Sigma A recognition sites in the Bacillus subtilis genome. Microbiology 147:2417-2424.
    • (2001) Microbiology , vol.147 , pp. 2417-2424
    • Jarmer, H.1
  • 38
    • 0000686520 scopus 로고
    • Genetic characterization
    • P. Gerhardt, R. G. E. Murray, E. W. Costilow, W. A. Nester, N. R. Wood, R. Krieg, and G. B. Philips (ed.). American Society for Microbiology, Washington, DC
    • Johnson, J. L. 1981. Genetic characterization, p. 450-472. In P. Gerhardt, R. G. E. Murray, E. W. Costilow, W. A. Nester, N. R. Wood, R. Krieg, and G. B. Philips (ed.), Manual of methods for general bacteriology. American Society for Microbiology, Washington, DC.
    • (1981) Manual of methods for general bacteriology , pp. 450-472
    • Johnson, J.L.1
  • 39
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin, A., I. Alchanati, and Y. Shoham. 1993. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-. Appl. Environ. Microbiol. 59:1725-1730.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Shoham, Y.3
  • 40
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives
    • Kumar, R., S. Singh, and O. V. Singh. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J. Ind. Microbiol. iotechnol. 35:377-391.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 42
    • 34547201058 scopus 로고    scopus 로고
    • Li, M., et al. 2007. Gram-positive three-component antimicrobial peptidesensing system. Proc. Natl. Acad. Sci. U. S. A. 104:9469-9474.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9469-9474
    • Li, M.1
  • 43
    • 24044455869 scopus 로고    scopus 로고
    • Genome sequencing in microfabricated highdensity picolitre reactors
    • Margulies, M., et al. 2005. Genome sequencing in microfabricated highdensity picolitre reactors. Nature 437:376-380.
    • (2005) Nature , vol.437 , pp. 376-380
    • Margulies, M.1
  • 44
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 45
    • 0030899835 scopus 로고    scopus 로고
    • Catabolite repression of the Bacillus subtilis gnt operon exerted by two catabolite-responsive elements
    • Miwa, Y., et al. 1997. Catabolite repression of the Bacillus subtilis gnt operon exerted by two catabolite-responsive elements. Mol. Microbiol. 23:1203-1213.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1203-1213
    • Miwa, Y.1
  • 46
    • 43849099222 scopus 로고    scopus 로고
    • Pectin structure and biosynthesis
    • Mohnen, D. 2008. Pectin structure and biosynthesis. Curr. Opin. Plant Biol. 11:266-277.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 266-277
    • Mohnen, D.1
  • 47
    • 0002597929 scopus 로고
    • Measuring gene expression in Bacillus
    • C. R. Harwood and S. M. Cutting (ed.),. John Wiley & Sons, Chichester, United Kingdom
    • Moran, C. P. 1990. Measuring gene expression in Bacillus, p. 267-293. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for acillus. John Wiley & Sons, Chichester, United Kingdom.
    • (1990) Molecular biological methods for bacillus , pp. 267-293
    • Moran, C.P.1
  • 48
    • 0020384747 scopus 로고
    • Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis
    • Moran, C. P., Jr., et al. 1982. Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis. Mol. Gen. Genet. 86: 339-346.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 339-346
    • Moran Jr., C.P.1
  • 49
    • 0034977070 scopus 로고    scopus 로고
    • Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: crucial roles of operators, cooperativity, and DNA looping
    • Mota, L. J., L. M. Sarmento, and I. de Sa-Nogueíra. 2001. Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: crucial roles of operators, cooperativity, and DNA looping. J. Bacteriol. 183:4190-4201.
    • (2001) J. Bacteriol. , vol.183 , pp. 4190-4201
    • Mota, L.J.1    Sarmento, L.M.2    de Sa-Nogueíra, I.3
  • 50
    • 0036716744 scopus 로고    scopus 로고
    • The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan
    • Nagy, T., et al. 2002. The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan. J. Bacteriol. 184:4925-4929.
    • (2002) J. Bacteriol. , vol.184 , pp. 4925-4929
    • Nagy, T.1
  • 51
    • 78649889018 scopus 로고    scopus 로고
    • Clostridium thermocellum cellulosomal genes are regulated by extracytoplasmic polysaccharides via alternative sigma factors
    • Nataf, Y., et al. 2010. Clostridium thermocellum cellulosomal genes are regulated by extracytoplasmic polysaccharides via alternative sigma actors. Proc. Natl. Acad. Sci. U. S. A. 107:18646-18651.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18646-18651
    • Nataf, Y.1
  • 52
    • 58149479219 scopus 로고    scopus 로고
    • Cellodextrin and laminaribiose ABC transporters in Clostridium thermocellum
    • Nataf, Y., et al. 2009. Cellodextrin and laminaribiose ABC transporters in Clostridium thermocellum. J. Bacteriol. 191:203-209.
    • (2009) J. Bacteriol. , vol.191 , pp. 203-209
    • Nataf, Y.1
  • 53
    • 39049186224 scopus 로고    scopus 로고
    • A complete protein pattern of cellulase and hemicellulase genes in the filamentous fungus Trichoderma reesei
    • Ouyang, J., M. Yan, D. Kong, and L. Xu. 2006. A complete protein pattern of cellulase and hemicellulase genes in the filamentous fungus richoderma reesei. Biotechnol. J. 1:1266-1274.
    • (2006) Biotechnol. J. , vol.1 , pp. 1266-1274
    • Ouyang, J.1    Yan, M.2    Kong, D.3    Xu, L.4
  • 54
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. U. S. A. 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 55
    • 31544452808 scopus 로고    scopus 로고
    • The path forward for biofuels and biomaterials
    • Ragauskas, A. J., et al. 2006. The path forward for biofuels and biomaterials. Science 311:484-489.
    • (2006) Science , vol.311 , pp. 484-489
    • Ragauskas, A.J.1
  • 56
    • 70349771942 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass to hydrogen: potential and challenges
    • Ren, N., A. Wang, G. Cao, J. Xu, and L. Gao. 2009. Bioconversion of lignocellulosic biomass to hydrogen: potential and challenges. Biotechnol. Adv. 7:1051-1060.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 1051-1060
    • Ren, N.1    Wang, A.2    Cao, G.3    Xu, J.4    Gao, L.5
  • 57
    • 0032035329 scopus 로고    scopus 로고
    • Positive activation of gene expression
    • Rhodius, V. A., and S. J. Busby. 1998. Positive activation of gene expression. Curr. Opin. Microbiol. 1:152-159.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 152-159
    • Rhodius, V.A.1    Busby, S.J.2
  • 58
    • 0033887436 scopus 로고    scopus 로고
    • A tale of two components: a novel kinase and a regulatory switch
    • Robinson, V. L., D. R. Buckler, and A. M. Stock. 2000. A tale of two components: a novel kinase and a regulatory switch. Nat. Struct. Biol. 7:626-33.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 626-633
    • Robinson, V.L.1    Buckler, D.R.2    Stock, A.M.3
  • 61
    • 0035010435 scopus 로고    scopus 로고
    • Schneider, E. 2001. ABC transporters catalyzing carbohydrate uptake. Res. Microbiol. 152:303-310.
    • (2001) Res. Microbiol. , vol.152 , pp. 303-310
    • Schneider, E.1
  • 62
    • 0346319022 scopus 로고    scopus 로고
    • Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom, D., et al. 2002. Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J. Biol. Chem. 277:43667-43673.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43667-43673
    • Shallom, D.1
  • 63
    • 19944427947 scopus 로고    scopus 로고
    • Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6
    • Shallom, D., et al. 2005. Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus tearothermophilus T-6. Biochemistry 44:387-397.
    • (2005) Biochemistry , vol.44 , pp. 387-397
    • Shallom, D.1
  • 65
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham, Y., R. Lamed, and E. A. Bayer. 1999. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol. 7:275-281.
    • (1999) Trends Microbiol , vol.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 66
    • 33846912842 scopus 로고
    • Delignification of wood pulp by a thermostable xylanase
    • Shoham, Y., et al. 1992. Delignification of wood pulp by a thermostable xylanase. Biodegradation 3:161-170.
    • (1992) Biodegradation , vol.3 , pp. 161-170
    • Shoham, Y.1
  • 67
    • 0032980767 scopus 로고    scopus 로고
    • The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6
    • Shulami, S., O. Gat, A. L. Sonenshein, and Y. Shoham. 1999. The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6. Bacteriol. 181:3695-3704.
    • (1999) J. Bacteriol. , vol.181 , pp. 3695-3704
    • Shulami, S.1    Gat, O.2    Sonenshein, A.L.3    Shoham, Y.4
  • 68
    • 33846932041 scopus 로고    scopus 로고
    • A two-component system regulates the expression of an ABC transporter for xylo-oligosaccharides in Geobacillus stearothermophilus
    • Shulami, S., et al. 2007. A two-component system regulates the expression of an ABC transporter for xylo-oligosaccharides in Geobacillus stearothermophilus. Appl. Environ. Microbiol. 73:874-884.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 874-884
    • Shulami, S.1
  • 69
    • 33744771680 scopus 로고    scopus 로고
    • Complete cellulase system in the marine bacterium Saccharophagus degradans strain 2-40T
    • Taylor, L. E., II, et al. 2006. Complete cellulase system in the marine bacterium Saccharophagus degradans strain 2-40T. J. Bacteriol. 88:3849-3861.
    • (2006) J. Bacteriol. , vol.188 , pp. 3849-3861
    • Taylor II, L.E.1
  • 70
    • 34748917914 scopus 로고    scopus 로고
    • Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein
    • Tian, Y., et al. 2007. Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein. Protein ci. 16:2240-2250.
    • (2007) Protein Sci , vol.16 , pp. 2240-2250
    • Tian, Y.1
  • 71
    • 0022431952 scopus 로고
    • Complete sequence of IS3
    • Timmerman, K. P., and C. P. Tu. 1985. Complete sequence of IS3. Nucleic Acids Res. 13:2127-2139.
    • (1985) Nucleic Acids Res , vol.13 , pp. 2127-2139
    • Timmerman, K.P.1    Tu, C.P.2
  • 72
    • 1142286471 scopus 로고    scopus 로고
    • Molecular characterization of a high-affinity xylobiose transporter of Streptomyces thermoviolaceus OPC-520 and its transcriptional regulation
    • Tsujibo, H., et al. 2004. Molecular characterization of a high-affinity xylobiose transporter of Streptomyces thermoviolaceus OPC-520 and its ranscriptional regulation. J. Bacteriol. 186:1029-1037.
    • (2004) J. Bacteriol. , vol.186 , pp. 1029-1037
    • Tsujibo, H.1
  • 73
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: one, two or four extracytoplasmic substrate-binding sites?
    • van der Heide, T., and B. Poolman. 2002. ABC transporters: one, two or four extracytoplasmic substrate-binding sites? EMBO Rep. 3:938-943.
    • (2002) EMBO Rep , vol.3 , pp. 938-943
    • van der Heide, T.1    Poolman, B.2
  • 74
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • Volz, K. 1993. Structural conservation in the CheY superfamily. Biochemistry 32:11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 75
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne, G. 1989. The structure of signal peptides from bacterial lipoproteins. Protein Eng. 2:531-534.
    • (1989) Protein Eng , vol.2 , pp. 531-534
    • von Heijne, G.1
  • 76
    • 36549000721 scopus 로고    scopus 로고
    • Metagenomic and functional analysis of hindgut microbiota of a wood-feeding higher termite
    • Warnecke, F., et al. 2007. Metagenomic and functional analysis of hindgut microbiota of a wood-feeding higher termite. Nature 450:560-565.
    • (2007) Nature , vol.450 , pp. 560-565
    • Warnecke, F.1
  • 77
    • 33646365379 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism
    • Watanabe, S., T. Kodaki, and K. Makino. 2006. Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism. J. Biol. Chem. 281:2612-2623.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2612-2623
    • Watanabe, S.1    Kodaki, T.2    Makino, K.3
  • 78
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., S. Williston, J. F. Brandts, and L. N. Lin. 1989. Rapid measurement of binding constants and heats of binding using a new titration alorimeter. Anal. Biochem. 179:131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 79
    • 35448975682 scopus 로고    scopus 로고
    • Microbial community succession and lignocellulose degradation during agricultural waste composting
    • Yu, H., et al. 2007. Microbial community succession and lignocellulose degradation during agricultural waste composting. Biodegradation 18:793-802.
    • (2007) Biodegradation , vol.18 , pp. 793-802
    • Yu, H.1
  • 80
    • 0034833426 scopus 로고    scopus 로고
    • Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6
    • Zaide, G., et al. 2001. Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus -6. Eur. J. Biochem. 268:3006-3016.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3006-3016
    • Zaide, G.1


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