메뉴 건너뛰기




Volumn 77, Issue 14, 2011, Pages 4849-4858

Retraction: "Assembly of minicellulosomes on the surface of Bacillus subtilis" [Applied and Environmental Microbiology, 77, 14, (2011), (4849-4858)] doi 10.1128/AEM.02599-10;Assembly of minicellulosomes on the surface of Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BIODEGRADATION; BIOMASS; CELL MEMBRANES; CLOSTRIDIUM; ENZYMES; ESCHERICHIA COLI; IONS;

EID: 79961094174     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02429-17     Document Type: Erratum
Times cited : (42)

References (72)
  • 1
    • 0027984011 scopus 로고
    • The cellulosome-a treasuretrove for biotechnology
    • Bayer, E. A., E. Morag, and R. Lamed. 1994. The cellulosome-a treasuretrove for biotechnology. Trends Biotechnol. 12:379-386.
    • (1994) Trends Biotechnol , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 2
    • 0021855251 scopus 로고
    • Organization and distribution of the cellulosome in Clostridium thermocellum
    • Bayer, E. A., E. Setter, and R. Lamed. 1985. Organization and distribution of the cellulosome in Clostridium thermocellum. J. Bacteriol. 163:552-559.
    • (1985) J. Bacteriol. , vol.163 , pp. 552-559
    • Bayer, E.A.1    Setter, E.2    Lamed, R.3
  • 4
    • 0002492795 scopus 로고
    • Plasmids
    • C. R. Harwood and S. M. Cutting (ed.), John Wiley and Sons, Chichester, United Kingdom
    • Bron, S. 1990. Plasmids, p. 75-139. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for bacillus. John Wiley and Sons, Chichester, United Kingdom.
    • (1990) Molecular biological methods for bacillus , pp. 75-139
    • Bron, S.1
  • 5
    • 61349088032 scopus 로고    scopus 로고
    • Cell wall anchor structure of BcpA pili in Bacillus anthracis
    • Budzik, J. M., S. Y. Oh, and O. Schneewind. 2008. Cell wall anchor structure of BcpA pili in Bacillus anthracis. J. Biol. Chem. 283:36676-36686.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36676-36686
    • Budzik, J.M.1    Oh, S.Y.2    Schneewind, O.3
  • 7
    • 47249125226 scopus 로고    scopus 로고
    • Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: comparative impact on cellulose-degrading activity
    • Caspi, J., et al. 2008. Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: comparative impact on cellulose-degrading activity. J. Biotechnol. 135:351-357.
    • (2008) J. Biotechnol. , vol.135 , pp. 351-357
    • Caspi, J.1
  • 8
    • 36949013920 scopus 로고    scopus 로고
    • Effect of multiple copies of cohesins on cellulase and hemicellulase activities of Clostridium cellulovorans mini-cellulosomes
    • Cha, J., et al. 2007. Effect of multiple copies of cohesins on cellulase and hemicellulase activities of Clostridium cellulovorans mini-cellulosomes. J. Microbiol. Biotechnol. 17:1782-1788.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1782-1788
    • Cha, J.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
    • 34247176809 scopus 로고    scopus 로고
    • Isolating and engineering human antibodies using yeast surface display
    • Chao, G., et al. 2006. Isolating and engineering human antibodies using yeast surface display. Nat. Protoc. 1:755-768.
    • (2006) Nat. Protoc. , vol.1 , pp. 755-768
    • Chao, G.1
  • 11
    • 0032579455 scopus 로고    scopus 로고
    • Synergistic interaction of the cellulosome integrating protein (CipA) from Clostridium thermocellum with a cellulosomal endoglucanase
    • Ciruela, A., H. J. Gilbert, B. R. Ali, and G. P. Hazlewood. 1998. Synergistic interaction of the cellulosome integrating protein (CipA) from Clostridium thermocellum with a cellulosomal endoglucanase. FEBS Lett. 422:221-224.
    • (1998) FEBS Lett , vol.422 , pp. 221-224
    • Ciruela, A.1    Gilbert, H.J.2    Ali, B.R.3    Hazlewood, G.P.4
  • 12
    • 41349123095 scopus 로고    scopus 로고
    • Cellulases of mesophilic microorganisms: cellulosome and noncellulosome producers
    • Doi, R. H. 2008. Cellulases of mesophilic microorganisms: cellulosome and noncellulosome producers. Ann. N. Y. Acad. Sci. 1125:267-279.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1125 , pp. 267-279
    • Doi, R.H.1
  • 13
    • 13444304245 scopus 로고    scopus 로고
    • Bacillus subtilis as a tool for vaccine development: from antigen factories to delivery vectors
    • Ferreira, L. C., R. C. Ferreira, and W. Schumann. 2005. Bacillus subtilis as a tool for vaccine development: from antigen factories to delivery vectors. An. Acad. Bras. Cienc. 77:113-124.
    • (2005) An. Acad. Bras. Cienc. , vol.77 , pp. 113-124
    • Ferreira, L.C.1    Ferreira, R.C.2    Schumann, W.3
  • 14
    • 0347579849 scopus 로고    scopus 로고
    • Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components
    • Fierobe, H. P., et al. 2002. Degradation of cellulose substrates by cellulosome chimeras. Substrate targeting versus proximity of enzyme components. J. Biol. Chem. 277:49621-49630.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49621-49630
    • Fierobe, H.P.1
  • 15
    • 20944438012 scopus 로고    scopus 로고
    • Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin
    • Fierobe, H. P., et al. 2005. Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin. J. Biol. Chem. 280:16325-16334.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16325-16334
    • Fierobe, H.P.1
  • 16
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: highly efficient nano-machines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes, C. M., and H. J. Gilbert. 2010. Cellulosomes: highly efficient nano-machines designed to deconstruct plant cell wall complex carbohydrates. Annu. Rev. Biochem. 79:655-681.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 655-681
    • Fontes, C.M.1    Gilbert, H.J.2
  • 17
    • 14744300636 scopus 로고
    • Specific adhesion and hydrolysis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains
    • Francisco, J. A., C. Stathopoulos, R. A. Warren, D. G. Kilburn, and G. Georgiou. 1993. Specific adhesion and hydrolysis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains. Biotechnology (NY) 11:491-495.
    • (1993) Biotechnology (NY) , vol.11 , pp. 491-495
    • Francisco, J.A.1    Stathopoulos, C.2    Warren, R.A.3    Kilburn, D.G.4    Georgiou, G.5
  • 18
    • 21144451705 scopus 로고    scopus 로고
    • Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope
    • Gaspar, A. H., et al. 2005. Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope. J. Bacteriol. 187:4646-4655.
    • (2005) J. Bacteriol. , vol.187 , pp. 4646-4655
    • Gaspar, A.H.1
  • 19
    • 42249114507 scopus 로고    scopus 로고
    • Sustainable liquid biofuels from biomass: the writing's on the walls
    • Gomez, L. D., C. G. Steele-King, and S. J. McQueen-Mason. 2008. Sustainable liquid biofuels from biomass: the writing's on the walls. New Phytol. 178:473-485.
    • (2008) New Phytol , vol.178 , pp. 473-485
    • Gomez, L.D.1    Steele-King, C.G.2    McQueen-Mason, S.J.3
  • 20
    • 41149118473 scopus 로고    scopus 로고
    • Cohesin-dockerin microarray: diverse specificities between two complementary families of interacting protein modules
    • Haimovitz, R., et al. 2008. Cohesin-dockerin microarray: diverse specificities between two complementary families of interacting protein modules. Proteomics 8:968-979.
    • (2008) Proteomics , vol.8 , pp. 968-979
    • Haimovitz, R.1
  • 21
    • 77951051077 scopus 로고    scopus 로고
    • Synthesis, regulation and utilization of lignocellulosic biomass
    • Harris, D., and S. DeBolt. 2010. Synthesis, regulation and utilization of lignocellulosic biomass. Plant Biotechnol. J. 8:244-262.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 244-262
    • Harris, D.1    DeBolt, S.2
  • 22
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood, C. R., and R. Cranenburgh. 2008. Bacillus protein secretion: an unfolding story. Trends Microbiol. 16:73-79.
    • (2008) Trends Microbiol , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 23
    • 51349153711 scopus 로고    scopus 로고
    • Pretreatments to enhance the digestibility of lignocellulosic biomass
    • Hendriks, A. T., and G. Zeeman. 2009. Pretreatments to enhance the digestibility of lignocellulosic biomass. Bioresour. Technol. 100:10-18.
    • (2009) Bioresour. Technol. , vol.100 , pp. 10-18
    • Hendriks, A.T.1    Zeeman, G.2
  • 24
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: engineering plants and enzymes for biofuels production
    • Himmel, M. E., et al. 2007. Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 315:804-807.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1
  • 25
    • 33751499239 scopus 로고
    • Preparation and utilization of cellulose substrates regenerated after treatment with hydrochloric acid
    • Hsu, J. C., and M. H. Penner. 1991. Preparation and utilization of cellulose substrates regenerated after treatment with hydrochloric acid. J. Agric. Food Chem. 39:1444.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1444
    • Hsu, J.C.1    Penner, M.H.2
  • 26
    • 0024444794 scopus 로고
    • Inducible secretion of a cellulase from Clostridium thermocellum in Bacillus subtilis
    • Joliff, G., A. Edelman, A. Klier, and G. Rapoport. 1989. Inducible secretion of a cellulase from Clostridium thermocellum in Bacillus subtilis. Appl. Environ. Microbiol. 55:2739-2744.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2739-2744
    • Joliff, G.1    Edelman, A.2    Klier, A.3    Rapoport, G.4
  • 27
    • 0031729882 scopus 로고    scopus 로고
    • Integration and amplification of the Bacillus sp. 79-23 cellulase gene in the Bacillus subtilis 168 chromosome
    • Jung, K. H., D. H. Lee, K. H. Yoon, and S. H. Park. 1998. Integration and amplification of the Bacillus sp. 79-23 cellulase gene in the Bacillus subtilis 168 chromosome. J. Gen. Appl. Microbiol. 44:107-111.
    • (1998) J. Gen. Appl. Microbiol. , vol.44 , pp. 107-111
    • Jung, K.H.1    Lee, D.H.2    Yoon, K.H.3    Park, S.H.4
  • 28
    • 56749150065 scopus 로고    scopus 로고
    • Energy. World oil crunch looming?
    • Kerr, R. A. 2008. Energy. World oil crunch looming? Science 322:1178-1179.
    • (2008) Science , vol.322 , pp. 1178-1179
    • Kerr, R.A.1
  • 29
    • 23044500836 scopus 로고    scopus 로고
    • Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus subtilis
    • Kim, J. H., I. S. Park, and B. G. Kim. 2005. Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus subtilis. Biochem. Biophys. Res. Commun. 334:1248-1253.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1248-1253
    • Kim, J.H.1    Park, I.S.2    Kim, B.G.3
  • 30
    • 73949138090 scopus 로고    scopus 로고
    • Pretreatment of biomass by aqueous ammonia for bioethanol production
    • Kim, T. H., R. Gupta, and Y. Y. Lee. 2009. Pretreatment of biomass by aqueous ammonia for bioethanol production. Methods Mol. Biol. 581:79-91.
    • (2009) Methods Mol. Biol. , vol.581 , pp. 79-91
    • Kim, T.H.1    Gupta, R.2    Lee, Y.Y.3
  • 32
    • 0033961548 scopus 로고    scopus 로고
    • Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants
    • Kim, Y. S., H. C. Jung, and J. G. Pan. 2000. Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants. Appl. Environ. Microbiol. 66:788-793.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 788-793
    • Kim, Y.S.1    Jung, H.C.2    Pan, J.G.3
  • 33
    • 53849146360 scopus 로고    scopus 로고
    • Identification of residues important for cleavage of the extracellular signaling peptide CSF of Bacillus subtilis from its precursor protein
    • Lanigan-Gerdes, S., G. Briceno, A. N. Dooley, K. F. Faull, and B. A. Lazazzera. 2008. Identification of residues important for cleavage of the extracellular signaling peptide CSF of Bacillus subtilis from its precursor protein. J. Bacteriol. 190:6668-6675.
    • (2008) J. Bacteriol. , vol.190 , pp. 6668-6675
    • Lanigan-Gerdes, S.1    Briceno, G.2    Dooley, A.N.3    Faull, K.F.4    Lazazzera, B.A.5
  • 34
    • 34547879263 scopus 로고    scopus 로고
    • Identification of subtilisin, Epr and Vpr as enzymes that produce CSF, an extracellular signalling peptide of Bacillus subtilis
    • Lanigan-Gerdes, S., A. N. Dooley, K. F. Faull, and B. A. Lazazzera. 2007. Identification of subtilisin, Epr and Vpr as enzymes that produce CSF, an extracellular signalling peptide of Bacillus subtilis. Mol. Microbiol. 65:1321-1333.
    • (2007) Mol. Microbiol. , vol.65 , pp. 1321-1333
    • Lanigan-Gerdes, S.1    Dooley, A.N.2    Faull, K.F.3    Lazazzera, B.A.4
  • 35
    • 0001274582 scopus 로고    scopus 로고
    • Enhancement of secretion and extracellular stability of staphylokinase in Bacillus subtilis by wprA gene disruption
    • Lee, S. J., D. M. Kim, K. H. Bae, S. M. Byun, and J. H. Chung. 2000. Enhancement of secretion and extracellular stability of staphylokinase in Bacillus subtilis by wprA gene disruption. Appl. Environ. Microbiol. 66:476-480.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 476-480
    • Lee, S.J.1    Kim, D.M.2    Bae, K.H.3    Byun, S.M.4    Chung, J.H.5
  • 36
    • 70350553584 scopus 로고    scopus 로고
    • Heterologous expression of a Clostridium minicellulosome in Saccharomyces cerevisiae
    • Lilly, M., H. P. Fierobe, W. H. van Zyl, and H. Volschenk. 2009. Heterologous expression of a Clostridium minicellulosome in Saccharomyces cerevisiae. FEMS Yeast Res. 9:1236-1249.
    • (2009) FEMS Yeast Res , vol.9 , pp. 1236-1249
    • Lilly, M.1    Fierobe, H.P.2    van Zyl, W.H.3    Volschenk, H.4
  • 37
    • 33750838967 scopus 로고    scopus 로고
    • Enzyme-microbe synergy during cellulose hydrolysis by Clostridium thermocellum
    • Lu, Y., Y. H. Zhang, and L. R. Lynd. 2006. Enzyme-microbe synergy during cellulose hydrolysis by Clostridium thermocellum. Proc. Natl. Acad. Sci. U. S. A. 103:16165-16169.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16165-16169
    • Lu, Y.1    Zhang, Y.H.2    Lynd, L.R.3
  • 38
    • 70350455262 scopus 로고    scopus 로고
    • The prospects of cellulaseproducing bacteria for the bioconversion of lignocellulosic biomass
    • Maki, M., K. T. Leung, and W. Qin. 2009. The prospects of cellulaseproducing bacteria for the bioconversion of lignocellulosic biomass. Int. J. Biol. Sci. 5:500-516.
    • (2009) Int. J. Biol. Sci. , vol.5 , pp. 500-516
    • Maki, M.1    Leung, K.T.2    Qin, W.3
  • 40
    • 0030444419 scopus 로고    scopus 로고
    • The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease
    • Margot, P., and D. Karamata. 1996. The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease. Microbiology 142(Pt. 12):3437-3444.
    • (1996) Microbiology , vol.142 , Issue.PART 12 , pp. 3437-3444
    • Margot, P.1    Karamata, D.2
  • 41
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria
    • Marraffini, L. A., A. C. Dedent, and O. Schneewind. 2006. Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 70:192-221.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 42
    • 35048871939 scopus 로고    scopus 로고
    • Synergistic interaction of Clostridium cellulovorans cellulosomal cellulases and HbpA
    • Matsuoka, S., H. Yukawa, M. Inui, and R. H. Doi. 2007. Synergistic interaction of Clostridium cellulovorans cellulosomal cellulases and HbpA. J. Bacteriol. 189:7190-7194.
    • (2007) J. Bacteriol. , vol.189 , pp. 7190-7194
    • Matsuoka, S.1    Yukawa, H.2    Inui, M.3    Doi, R.H.4
  • 43
    • 77953708752 scopus 로고    scopus 로고
    • Extremophile-inspired strategies for enzymatic biomass saccharification
    • Miller, P. S., and P. H. Blum. 2010. Extremophile-inspired strategies for enzymatic biomass saccharification. Environ. Technol. 31:1005-1015.
    • (2010) Environ. Technol. , vol.31 , pp. 1005-1015
    • Miller, P.S.1    Blum, P.H.2
  • 45
    • 0037133275 scopus 로고    scopus 로고
    • Mapping by site-directed mutagenesis of the region responsible for cohesin-dockerin interaction on the surface of the seventh cohesin domain of Clostridium thermocellum CipA
    • Miras, I., F. Schaeffer, P. Beguin, and P. M. Alzari. 2002. Mapping by site-directed mutagenesis of the region responsible for cohesin-dockerin interaction on the surface of the seventh cohesin domain of Clostridium thermocellum CipA. Biochemistry 41:2115-2119.
    • (2002) Biochemistry , vol.41 , pp. 2115-2119
    • Miras, I.1    Schaeffer, F.2    Beguin, P.3    Alzari, P.M.4
  • 46
    • 33645333138 scopus 로고    scopus 로고
    • Establishment of an experimental system allowing immobilization of proteins on the surface of Bacillus subtilis cells
    • Nguyen, H. D., and W. Schumann. 2006. Establishment of an experimental system allowing immobilization of proteins on the surface of Bacillus subtilis cells. J. Biotechnol. 122:473-482.
    • (2006) J. Biotechnol. , vol.122 , pp. 473-482
    • Nguyen, H.D.1    Schumann, W.2
  • 47
    • 3843123048 scopus 로고    scopus 로고
    • Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure
    • Oussenko, I. A., R. Sanchez, and D. H. Bechhofer. 2004. Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure. J. Bacteriol. 186:5376-5383.
    • (2004) J. Bacteriol. , vol.186 , pp. 5376-5383
    • Oussenko, I.A.1    Sanchez, R.2    Bechhofer, D.H.3
  • 48
    • 0343229549 scopus 로고    scopus 로고
    • Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain
    • Pages, S., et al. 1997. Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain. Proteins 29:517-527.
    • (1997) Proteins , vol.29 , pp. 517-527
    • Pages, S.1
  • 49
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: screening and selection strategies
    • Percival Zhang, Y. H., M. E. Himmel, and J. R. Mielenz. 2006. Outlook for cellulase improvement: screening and selection strategies. Biotechnol. Adv. 24:452-481.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 452-481
    • Percival Zhang, Y.H.1    Himmel, M.E.2    Mielenz, J.R.3
  • 50
    • 0024118243 scopus 로고
    • Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis
    • Perego, M., G. B. Spiegelman, and J. A. Hoch. 1988. Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis. Mol. Microbiol. 2:689-699.
    • (1988) Mol. Microbiol. , vol.2 , pp. 689-699
    • Perego, M.1    Spiegelman, G.B.2    Hoch, J.A.3
  • 51
    • 73149122122 scopus 로고    scopus 로고
    • Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum
    • Pinheiro, B. A., et al. 2009. Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum. Biochem. J. 424:375-384.
    • (2009) Biochem. J. , vol.424 , pp. 375-384
    • Pinheiro, B.A.1
  • 52
    • 27744600973 scopus 로고    scopus 로고
    • Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface
    • Rincon, M. T., et al. 2005. Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface. J. Bacteriol. 187: 7569-7578.
    • (2005) J. Bacteriol. , vol.187 , pp. 7569-7578
    • Rincon, M.T.1
  • 53
    • 0021220779 scopus 로고
    • Characterization of the cellulolytic activity of a Bacillus isolate
    • Robson, L. M., and G. H. Chambliss. 1984. Characterization of the cellulolytic activity of a Bacillus isolate. Appl. Environ. Microbiol. 47:1039-1046.
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 1039-1046
    • Robson, L.M.1    Chambliss, G.H.2
  • 54
    • 49649106060 scopus 로고    scopus 로고
    • Genomics of cellulosic biofuels
    • Rubin, E. M. 2008. Genomics of cellulosic biofuels. Nature 454:841-845.
    • (2008) Nature , vol.454 , pp. 841-845
    • Rubin, E.M.1
  • 55
    • 0028225196 scopus 로고
    • Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome-integrating protein CipA
    • Salamitou, S., et al. 1994. Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome-integrating protein CipA. J. Bacteriol. 176:2822-2827.
    • (1994) J. Bacteriol. , vol.176 , pp. 2822-2827
    • Salamitou, S.1
  • 56
    • 0037133136 scopus 로고    scopus 로고
    • Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity
    • Schaeffer, F., et al. 2002. Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity. Biochemistry 41:2106-2114.
    • (2002) Biochemistry , vol.41 , pp. 2106-2114
    • Schaeffer, F.1
  • 57
    • 0014561152 scopus 로고
    • Phospho-beta-glucosidases and beta-glucoside permeases in Streptococcus, Bacillus, and Staphylococcus
    • Schaefler, S., A. Malamy, and I. Green. 1969. Phospho-beta-glucosidases and beta-glucoside permeases in Streptococcus, Bacillus, and Staphylococcus. J. Bacteriol. 99:434-440.
    • (1969) J. Bacteriol. , vol.99 , pp. 434-440
    • Schaefler, S.1    Malamy, A.2    Green, I.3
  • 58
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey, M., A. Singh, and O. P. Ward. 2004. Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 50:1-17.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 59
    • 0022510269 scopus 로고
    • Properties of a Clostridium thermocellum endoglucanse produced in Escherichia coli
    • Schwarz, W. H., F. Grabnitz, and W. L. Staudenbauer. 1986. Properties of a Clostridium thermocellum endoglucanse produced in Escherichia coli. Appl. Environ. Microbiol. 51:1293-1299.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 1293-1299
    • Schwarz, W.H.1    Grabnitz, F.2    Staudenbauer, W.L.3
  • 60
    • 18444415756 scopus 로고    scopus 로고
    • Bacillus subtilis antibiotics: structures, syntheses and specific functions
    • Stein, T. 2005. Bacillus subtilis antibiotics: structures, syntheses and specific functions. Mol. Microbiol. 56:845-857.
    • (2005) Mol. Microbiol. , vol.56 , pp. 845-857
    • Stein, T.1
  • 61
    • 0031926846 scopus 로고    scopus 로고
    • Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis
    • Stephenson, K., and C. R. Harwood. 1998. Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis. Appl. Environ. Microbiol. 64:2875-2881.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2875-2881
    • Stephenson, K.1    Harwood, C.R.2
  • 62
    • 0017823254 scopus 로고
    • Carboxymethylcellulase produced by facultative bacteria from the hind-gut of the termite Reticulitermes hesperus
    • Thayer, D. W. 1978. Carboxymethylcellulase produced by facultative bacteria from the hind-gut of the termite Reticulitermes hesperus. J. Gen. Microbiol. 106:13-18.
    • (1978) J. Gen. Microbiol. , vol.106 , pp. 13-18
    • Thayer, D.W.1
  • 63
    • 0031032671 scopus 로고    scopus 로고
    • Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis
    • Tobisch, S., P. Glaser, S. Kruger, and M. Hecker. 1997. Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis. J. Bacteriol. 179:496-506.
    • (1997) J. Bacteriol. , vol.179 , pp. 496-506
    • Tobisch, S.1    Glaser, P.2    Kruger, S.3    Hecker, M.4
  • 64
    • 0025940435 scopus 로고
    • Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components
    • Tokatlidis, K., S. Salamitou, P. Beguin, P. Dhurjati, and J. P. Aubert. 1991. Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components. FEBS Lett. 291:185-188.
    • (1991) FEBS Lett , vol.291 , pp. 185-188
    • Tokatlidis, K.1    Salamitou, S.2    Beguin, P.3    Dhurjati, P.4    Aubert, J.P.5
  • 65
    • 70349436024 scopus 로고    scopus 로고
    • Functional assembly of minicellulosomes on the Saccharomyces cerevisiae cell surface for cellulose hydrolysis and ethanol production
    • Tsai, S. L., J. Oh, S. Singh, R. Chen, and W. Chen. 2009. Functional assembly of minicellulosomes on the Saccharomyces cerevisiae cell surface for cellulose hydrolysis and ethanol production. Appl. Environ. Microbiol. 75:6087-6093.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6087-6093
    • Tsai, S.L.1    Oh, J.2    Singh, S.3    Chen, R.4    Chen, W.5
  • 66
    • 76649105430 scopus 로고    scopus 로고
    • Yeast surface display of trifunctional minicellulosomes for simultaneous saccharification and fermentation of cellulose to ethanol
    • Wen, F., J. Sun, and H. Zhao. 2010. Yeast surface display of trifunctional minicellulosomes for simultaneous saccharification and fermentation of cellulose to ethanol. Appl. Environ. Microbiol. 76:1251-1260.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1251-1260
    • Wen, F.1    Sun, J.2    Zhao, H.3
  • 67
    • 8844278305 scopus 로고    scopus 로고
    • Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism
    • Westers, L., H. Westers, and W. J. Quax. 2004. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim. Biophys. Acta 1694:299-310.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 68
    • 67649815010 scopus 로고    scopus 로고
    • Cellulases and biofuels
    • Wilson, D. B. 2009. Cellulases and biofuels. Curr. Opin. Biotechnol. 20:295-299.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 295-299
    • Wilson, D.B.1
  • 69
    • 0036307716 scopus 로고    scopus 로고
    • Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production
    • Wu, S. C., et al. 2002. Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production. Appl. Environ. Microbiol. 68:3261-3269.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3261-3269
    • Wu, S.C.1
  • 70
    • 77951630910 scopus 로고    scopus 로고
    • Thermostable enzymes as biocatalysts in the biofuel industry
    • Yeoman, C. J., et al. 2010. Thermostable enzymes as biocatalysts in the biofuel industry. Adv. Appl. Microbiol. 70:1-55.
    • (2010) Adv. Appl. Microbiol. , vol.70 , pp. 1-55
    • Yeoman, C.J.1
  • 71
    • 62949176947 scopus 로고    scopus 로고
    • Organosolv pretreatment of lignocellulosic biomass for enzymatic hydrolysis
    • Zhao, X., K. Cheng, and D. Liu. 2009. Organosolv pretreatment of lignocellulosic biomass for enzymatic hydrolysis. Appl. Microbiol. Biotechnol. 82: 815-827.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 815-827
    • Zhao, X.1    Cheng, K.2    Liu, D.3
  • 72
    • 23644460722 scopus 로고    scopus 로고
    • Functional subgenomics of Clostridium thermocellum cellulosomal genes: identification of the major catalytic components in the extracellular complex and detection of three new enzymes
    • Zverlov, V. V., J. Kellermann, and W. H. Schwarz. 2005. Functional subgenomics of Clostridium thermocellum cellulosomal genes: identification of the major catalytic components in the extracellular complex and detection of three new enzymes. Proteomics 5:3646-3653.
    • (2005) Proteomics , vol.5 , pp. 3646-3653
    • Zverlov, V.V.1    Kellermann, J.2    Schwarz, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.