메뉴 건너뛰기




Volumn 6, Issue 1, 2013, Pages

A synthetic biology approach for evaluating the functional contribution of designer cellulosome components to deconstruction of cellulosic substrates

Author keywords

Biofuels; Cellulases; Cellulosic biomass; Cellulosomes; Clostridium thermocellum; Multi enzyme complex

Indexed keywords

CELLULASES; CELLULOSIC BIOMASS; CELLULOSOMES; CLOSTRIDIUM THERMOCELLUM; MULTI-ENZYME COMPLEX;

EID: 84890295928     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-182     Document Type: Article
Times cited : (70)

References (74)
  • 1
    • 0021016163 scopus 로고
    • Characterization of a cellulose-binding, cellulase-containing complex in clostridium thermocellum
    • Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. Lamed R, Setter E, Bayer EA, J Bacteriol 1983 156 828 836 (Pubitemid 14202591)
    • (1983) Journal of Bacteriology , vol.156 , Issue.2 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 2
    • 0020958567 scopus 로고
    • The cellulosome: A discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities
    • The cellulosome-a discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities. Lamed R, Setter E, Kenig R, Bayer EA, Biotechnol Bioeng Symp 1983 13 163 181 (Pubitemid 14102885)
    • (1983) Biotechnology Bioengineering Symposium , vol.VOL. 13 , Issue.13 , pp. 163-181
    • Lamed, R.1    Setter, E.2    Kenig, R.3    Bayer, E.A.4
  • 4
    • 0039519782 scopus 로고    scopus 로고
    • The cellulolytic system of clostridium cellulolyticum
    • DOI 10.1016/S0168-1656(97)00085-0, PII S0168165697000850
    • The cellulolytic system of Clostridium cellulolyticum. Belaich JP, Tardif C, Belaich A, Gaudin C, J Biotechnol 1997 57 3 14 (Pubitemid 27397466)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 3-14
    • Belaich, J.-P.1    Tardif, C.2    Belaich, A.3    Gaudin, C.4
  • 5
    • 1142298547 scopus 로고    scopus 로고
    • Architecture of the Bacteroides cellulosolvens Cellulosome: Description of a Cell Surface-Anchoring Scaffoldin and a Family 48 Cellulase
    • DOI 10.1128/JB.186.4.968-977.2004
    • Architecture of the Bacteroides cellulosolvens cellulosome: description of a cell surface-anchoring scaffoldin and a family 48 cellulase. Xu Q, Bayer EA, Goldman M, Kenig R, Shoham Y, Lamed R, J Bacteriol 2004 186 968 977 (Pubitemid 38209456)
    • (2004) Journal of Bacteriology , vol.186 , Issue.4 , pp. 968-977
    • Xu, Q.1    Bayer, E.A.2    Goldman, M.3    Kenig, R.4    Shoham, Y.5    Lamed, R.6
  • 6
    • 0032754343 scopus 로고    scopus 로고
    • A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family 9 glycosyl hydrolase
    • A novel cellulosomal scaffoldin from Acetivibrio cellulolyticus that contains a family 9 glycosyl hydrolase. Ding SY, Bayer EA, Steiner D, Shoham Y, Lamed R, J Bacteriol 1999 181 6720 6729 (Pubitemid 29517987)
    • (1999) Journal of Bacteriology , vol.181 , Issue.21 , pp. 6720-6729
    • Ding, S.-Y.1    Bayer, E.A.2    Steiner, D.3    Shoham, Y.4    Lamed, R.5
  • 7
    • 0033901462 scopus 로고    scopus 로고
    • A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins
    • DOI 10.1128/JB.182.17.4915-4925.2000
    • A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins. Ding SY, Bayer EA, Steiner D, Shoham Y, Lamed R, J Bacteriol 2000 182 4915 4925 (Pubitemid 30641817)
    • (2000) Journal of Bacteriology , vol.182 , Issue.17 , pp. 4915-4925
    • Ding, S.-Y.1    Bayer, E.A.2    Steiner, D.3    Shoham, Y.4    Lamed, R.5
  • 8
    • 0038443570 scopus 로고    scopus 로고
    • The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein
    • DOI 10.1128/JB.185.15.4548-4557.2003
    • The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein. Xu Q, Gao W, Ding SY, Kenig R, Shoham Y, Bayer EA, Lamed R, J Bacteriol 2003 185 4548 4557 (Pubitemid 36890502)
    • (2003) Journal of Bacteriology , vol.185 , Issue.15 , pp. 4548-4557
    • Xu, Q.1    Gao, W.2    Ding, S.-Y.3    Kenig, R.4    Shoham, Y.5    Bayer, E.A.6    Lamed, R.7
  • 9
    • 0034132054 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus
    • Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus. Ohara H, Karita S, Kimura T, Sakka K, Ohmiya K, Biosci Biotechnol Biochem 2000 64 254 260
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 254-260
    • Ohara, H.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 11
    • 1942539976 scopus 로고    scopus 로고
    • ScaC, an Adaptor Protein Carrying a Novel Cohesin That Expands the Dockerin-Binding Repertoire of the Ruminococcus flavefaciens 17 Cellulosome
    • DOI 10.1128/JB.186.9.2576-2585.2004
    • ScaC, an adaptor protein carrying a novel cohesin that expands the dockerin-binding repertoire of the Ruminococcus flavefaciens 17 cellulosome. Rincon MT, Martin JC, Aurilia V, McCrae SI, Rucklidge GJ, Reid MD, Bayer EA, Lamed R, Flint HJ, J Bacteriol 2004 186 2576 2585 (Pubitemid 38525910)
    • (2004) Journal of Bacteriology , vol.186 , Issue.9 , pp. 2576-2585
    • Rincon, M.T.1    Martin, J.C.2    Aurilia, V.3    McCrae, S.I.4    Rucklidge, G.J.5    Reid, M.D.6    Bayer, E.A.7    Lamed, R.8    Flint, H.J.9
  • 14
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • DOI 10.1146/annurev.micro.57.030502.091022
    • The cellulosomes: Multi-enzyme machines for degradation of plant cell wall polysaccharides. Bayer EA, Belaich J-P, Shoham Y, Lamed R, Annu Rev Microbiol 2004 58 521 554 (Pubitemid 39551996)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.-P.2    Shoham, Y.3    Lamed, R.4
  • 17
    • 0029040820 scopus 로고
    • Expression, purification and characterization of the cellulose-binding domain of the scaffoldin subunit from the cellulosome of Clostridium thermocellum
    • Expression, purification and characterization of the cellulose-binding domain of the scaffoldin subunit from the cellulosome of Clostridium thermocellum. Morag E, Lapidot A, Govorko D, Lamed R, Wilchek M, Bayer EA, Shoham Y, Appl Environ Microbiol 1995 61 1980 1986
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1980-1986
    • Morag, E.1    Lapidot, A.2    Govorko, D.3    Lamed, R.4    Wilchek, M.5    Bayer, E.A.6    Shoham, Y.7
  • 18
    • 0343247806 scopus 로고    scopus 로고
    • The roles and function of cellulose-binding domains
    • DOI 10.1016/S0168-1656(97)00087-4, PII S0168165697000874
    • The roles and function of cellulose-binding domains. Linder M, Teeri TT, J Biotechnol 1997 57 15 28 (Pubitemid 27397467)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 15-28
    • Linder, M.1    Teeri, T.T.2
  • 19
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • DOI 10.1042/BJ20040892
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Boraston AB, Bolam DN, Gilbert HJ, Davies GJ, Biochem J 2004 382 769 781 (Pubitemid 39312891)
    • (2004) Biochemical Journal , vol.382 , Issue.3 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 20
    • 0027984011 scopus 로고
    • The cellulosome - A treasure-trove for biotechnology
    • The cellulosome-a treasure-trove for biotechnology. Bayer EA, Morag E, Lamed R, Trends Biotechnol 1994 12 378 386
    • (1994) Trends Biotechnol , vol.12 , pp. 378-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 21
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • DOI 10.1016/S0966-842X(99)01533-4, PII S0966842X99015334
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Shoham Y, Lamed R, Bayer EA, Trends Microbiol 1999 7 275 281 (Pubitemid 29304563)
    • (1999) Trends in Microbiology , vol.7 , Issue.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 22
    • 0019974576 scopus 로고
    • Saccharification of complex cellulosic substrates by the cellulase system from Clostridium thermocellum
    • Saccharification of complex cellulosic substrates by the cellulase system from Clostridium thermocellum. Johnson EA, Sakojoh M, Halliwell G, Madia A, Demain AL, Appl Environ Microbiol 1982 43 1125 1132 (Pubitemid 12067117)
    • (1982) Applied and Environmental Microbiology , vol.43 , Issue.5 , pp. 1125-1132
    • Johnson, E.A.1    Sakajoh, M.2    Halliwell, G.3
  • 23
    • 0027502582 scopus 로고
    • Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface
    • Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface. Fujino T, Beguin P, Aubert JP, J Bacteriol 1993 175 1891 1899 (Pubitemid 23097496)
    • (1993) Journal of Bacteriology , vol.175 , Issue.7 , pp. 1891-1899
    • Fujino, T.1    Beguin, P.2    Aubert, J.-P.3
  • 24
    • 0032053815 scopus 로고    scopus 로고
    • Cellulase and hemicellulase genes of Clostridium thermocellum from five independent collections contain few overlaps and are widely scattered across the chromosome
    • DOI 10.1016/S0378-1097(98)00076-7, PII S0378109798000767
    • Cellulase and hemicellulase genes of Clostridium thermocellum from five independent collections contain few overlaps and are widely scattered across the chromosome. Guglielmi G, Beguin P, FEMS Microbiol Lett 1998 161 209 215 (Pubitemid 28161337)
    • (1998) FEMS Microbiology Letters , vol.161 , Issue.1 , pp. 209-215
    • Guglielmi, G.1    Beguin, P.2
  • 26
    • 0033814145 scopus 로고    scopus 로고
    • A large gene cluster for the Clostridium cellulovorans cellulosome
    • A large gene cluster for the Clostridium cellulovorans cellulosome. Tamaru Y, Karita S, Ibrahim A, Chan H, Doi RH, J Bacteriol 2000 182 5906 5910
    • (2000) J Bacteriol , vol.182 , pp. 5906-5910
    • Tamaru, Y.1    Karita, S.2    Ibrahim, A.3    Chan, H.4    Doi, R.H.5
  • 27
    • 0037137211 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum
    • DOI 10.1016/S0378-1097(02)00991-6, PII S0378109702009916
    • Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum. Sabathe F, Belaich A, Soucaille P, FEMS Microbiol Lett 2002 217 15 22 (Pubitemid 35356538)
    • (2002) FEMS Microbiology Letters , vol.217 , Issue.1 , pp. 15-22
    • Sabathe, F.1    Belaich, A.2    Soucaille, P.3
  • 28
    • 78049404208 scopus 로고    scopus 로고
    • Analysis of a Clostridium josui cellulase gene cluster containing the man5A gene and characterization of recombinant Man5A
    • Analysis of a Clostridium josui cellulase gene cluster containing the man5A gene and characterization of recombinant Man5A. Sakka M, Goto M, Fujino T, Fujino E, Karita S, Kimura T, Sakka K, Biosci Biotechnol Biochem 2010 74 2077 2082
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 2077-2082
    • Sakka, M.1    Goto, M.2    Fujino, T.3    Fujino, E.4    Karita, S.5    Kimura, T.6    Sakka, K.7
  • 29
    • 0034711446 scopus 로고    scopus 로고
    • Solution Structure of the Module X2 1 of Unknown Function of the Cellulosomal Scaffolding Protein CipC of Clostridium cellulolyticum
    • Solution Structure of the Module X2 1 of Unknown Function of the Cellulosomal Scaffolding Protein CipC of Clostridium cellulolyticum. Mosbah A, Belaich A, Bornet O, Belaich JP, Henrissat B, Darbon H, J Mol Biol 2000 304 201 217
    • (2000) J Mol Biol , vol.304 , pp. 201-217
    • Mosbah, A.1    Belaich, A.2    Bornet, O.3    Belaich, J.P.4    Henrissat, B.5    Darbon, H.6
  • 30
    • 84861168059 scopus 로고    scopus 로고
    • Designer cellulosomes for enhanced hydrolysis of cellulosic substrates
    • Designer cellulosomes for enhanced hydrolysis of cellulosic substrates. Vazana Y, Morais S, Barak Y, Lamed R, Bayer EA, Methods Enzymol 2012 510 429 452
    • (2012) Methods Enzymol , vol.510 , pp. 429-452
    • Vazana, Y.1    Morais, S.2    Barak, Y.3    Lamed, R.4    Bayer, E.A.5
  • 31
    • 0028936572 scopus 로고
    • Expression, purification and subunit-binding properties of cohesins 2 and 3 of the Clostridium thermocellum cellulosome
    • Expression, purification and subunit-binding properties of cohesins 2 and 3 of the Clostridium thermocellum cellulosome. Yaron S, Morag E, Bayer EA, Lamed R, Shoham Y, FEBS Lett 1995 360 121 124
    • (1995) FEBS Lett , vol.360 , pp. 121-124
    • Yaron, S.1    Morag, E.2    Bayer, E.A.3    Lamed, R.4    Shoham, Y.5
  • 32
    • 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
    • DOI 10.1002/(SICI)1097-0134(199712)29:4<517::AID-PROT11>3.0.CO;2-P
    • Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain. Pagès S, Belaich A, Belaich J-P, Morag E, Lamed R, Shoham Y, Bayer EA, Proteins 1997 29 517 527 (Pubitemid 27520204)
    • (1997) Proteins: Structure, Function and Genetics , vol.29 , Issue.4 , pp. 517-527
    • Pages, S.1    Belaich, A.2    Belaich, J.-P.3    Morag, E.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 33
    • 0030029469 scopus 로고    scopus 로고
    • Interactions of the CelS binding ligand with various receptor domains of the Clostridium thermocellum cellulosomal scaffolding protein, CipA
    • Interactions of the CelS binding ligand with various receptor domains of the Clostridium thermocellum cellulosomal scaffolding protein, CipA. Lytle B, Myers C, Kruus K, Wu JH, J Bacteriol 1996 178 1200 1203 (Pubitemid 26048041)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1200-1203
    • Lytle, B.1    Myers, C.2    Kruus, K.3    Wu, J.H.D.4
  • 34
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes
    • Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes. Fierobe H-P, Mechaly A, Tardif C, Belaich A, Lamed R, Shoham Y, Belaich J-P, Bayer EA, J Biol Chem 2001 276 21257 21261
    • (2001) J Biol Chem , vol.276 , pp. 21257-21261
    • Fierobe, H.-P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.-P.7    Bayer, E.A.8
  • 36
    • 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
    • DOI 10.1074/jbc.M414449200
    • Action of designer cellulosomes on homogeneous versus complex substrates: Controlled incorporation of three distinct enzymes into a defined tri-functional scaffoldin. Fierobe H-P, Mingardon F, Mechaly A, Belaich A, Rincon MT, Lamed R, Tardif C, Belaich J-P, Bayer EA, J Biol Chem 2005 280 16325 16334 (Pubitemid 40616761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16325-16334
    • Fierobe, H.-P.1    Mingardon, F.2    Mechaly, A.3    Belaich, A.4    Rincon, M.T.5    Pages, S.6    Lamed, R.7    Tardif, C.8    Belaich, J.-P.9    Bayer, E.A.10
  • 37
    • 47249125226 scopus 로고    scopus 로고
    • Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: Comparative impact on cellulose-degrading activity
    • Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: comparative impact on cellulose-degrading activity. Caspi J, Irwin D, Lamed R, Li Y, Fierobe HP, Wilson DB, Bayer EA, J Biotechnol 2008 135 351 357
    • (2008) J Biotechnol , vol.135 , pp. 351-357
    • Caspi, J.1    Irwin, D.2    Lamed, R.3    Li, Y.4    Fierobe, H.P.5    Wilson, D.B.6    Bayer, E.A.7
  • 38
    • 34250878420 scopus 로고    scopus 로고
    • Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes
    • DOI 10.1128/AEM.00398-07
    • Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes. Mingardon F, Chantal A, López-Contreras AM, Dray C, Bayer EA, Fierobe H-P, Appl Environ Microbiol 2007 73 3822 3832 (Pubitemid 46983228)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.12 , pp. 3822-3832
    • Mingardon, F.1    Chanal, A.2    Lopez-Contreras, A.M.3    Dray, C.4    Bayer, E.A.5    Fierobe, H.-P.6
  • 39
    • 77953636504 scopus 로고    scopus 로고
    • Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes
    • Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes. Morais S, Barak Y, Caspi J, Hadar Y, Lamed R, Shoham Y, Wilson DB, Bayer EA, Appl Environ Microbiol 2010 76 3787 3796
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3787-3796
    • Morais, S.1    Barak, Y.2    Caspi, J.3    Hadar, Y.4    Lamed, R.5    Shoham, Y.6    Wilson, D.B.7    Bayer, E.A.8
  • 42
    • 77957344915 scopus 로고    scopus 로고
    • Enhanced cellulose degradation by nano-complexed enzymes: Synergism between a scaffold-linked exoglucanase and a free endoglucanase
    • Enhanced cellulose degradation by nano-complexed enzymes: Synergism between a scaffold-linked exoglucanase and a free endoglucanase. Morais S, Heyman A, Barak Y, Caspi J, Wilson DB, Lamed R, Shoseyov O, Bayer EA, J Biotechnol 2010 147 205 211
    • (2010) J Biotechnol , vol.147 , pp. 205-211
    • Morais, S.1    Heyman, A.2    Barak, Y.3    Caspi, J.4    Wilson, D.B.5    Lamed, R.6    Shoseyov, O.7    Bayer, E.A.8
  • 46
    • 77956184308 scopus 로고    scopus 로고
    • Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression
    • Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression. Unger T, Jacobovitch Y, Dantes A, Bernheim R, Peleg Y, J Struct Biol 2010 172 34 44
    • (2010) J Struct Biol , vol.172 , pp. 34-44
    • Unger, T.1    Jacobovitch, Y.2    Dantes, A.3    Bernheim, R.4    Peleg, Y.5
  • 47
    • 0025879666 scopus 로고
    • Isolation and properties of a major cellobiohydrolase from the cellulosome of Clostridium thermocellum
    • Isolation and properties of a major cellobiohydrolase from the cellulosome of Clostridium thermocellum. Morag E, Halevy I, Bayer EA, Lamed R, J Bacteriol 1991 173 4155 4162
    • (1991) J Bacteriol , vol.173 , pp. 4155-4162
    • Morag, E.1    Halevy, I.2    Bayer, E.A.3    Lamed, R.4
  • 48
    • 0032857727 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: Evidence for gene duplication and recombination
    • Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination. Kataeva I, Li XL, Chen H, Choi SK, Ljungdahl LG, J Bacteriol 1999 181 5288 5295 (Pubitemid 29416348)
    • (1999) Journal of Bacteriology , vol.181 , Issue.17 , pp. 5288-5295
    • Kataeva, I.1    Li, X.-L.2    Chen, H.3    Choi, S.-K.4    Ljungdahl, L.G.5
  • 49
    • 0038643330 scopus 로고    scopus 로고
    • Regulation of the cellulosomal celS (cel48A) gene of Clostridium thermocellum is growth rate dependent
    • DOI 10.1128/JB.185.10.3042-3048.2003
    • Regulation of the cellulosomal CelS (cel48A) gene of Clostridium thermocellum is growth rate dependent. Dror TW, Morag E, Rolider A, Bayer EA, Lamed R, Shoham Y, J Bacteriol 2003 185 3042 3048 (Pubitemid 36539100)
    • (2003) Journal of Bacteriology , vol.185 , Issue.10 , pp. 3042-3048
    • Dror, T.W.1    Morag, E.2    Rolider, A.3    Bayer, E.A.4    Lamed, R.5    Shoham, Y.6
  • 50
    • 34948817185 scopus 로고    scopus 로고
    • Global view of the Clostridium thermocellum cellulosome revealed by quantitative proteomic analysis
    • DOI 10.1128/JB.00882-07
    • Global view of the Clostridium thermocellum cellulosome revealed by quantitative proteomic analysis. Gold ND, Martin VJ, J Bacteriol 2007 189 6787 6795 (Pubitemid 47525422)
    • (2007) Journal of Bacteriology , vol.189 , Issue.19 , pp. 6787-6795
    • Gold, N.D.1    Martin, V.J.J.2
  • 51
    • 67649214495 scopus 로고    scopus 로고
    • Impact of pretreated Switchgrass and biomass carbohydrates on Clostridium thermocellum ATCC 27405 cellulosome composition: A quantitative proteomic analysis
    • Impact of pretreated Switchgrass and biomass carbohydrates on Clostridium thermocellum ATCC 27405 cellulosome composition: a quantitative proteomic analysis. Raman B, Pan C, Hurst GB, Rodriguez M Jr, McKeown CK, Lankford PK, Samatova NF, Mielenz JR, PLoS ONE 2009 4 5271
    • (2009) PLoS ONE , vol.4 , pp. 55271
    • Raman, B.1    Pan, C.2    Hurst, G.B.3    Rodriguez Jr., M.4    McKeown, C.K.5    Lankford, P.K.6    Samatova, N.F.7    Mielenz, J.R.8
  • 52
    • 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
    • DOI 10.1002/pmic.200401199
    • Functional subgenomics of Clostridium thermocellum cellulosomal genes: Identification of the major catalytic components in the extracellular complex and detection of three new enzymes. Zverlov VV, Kellermann J, Schwarz WH, Proteomics 2005 5 3646 3653 (Pubitemid 41393298)
    • (2005) Proteomics , vol.5 , Issue.14 , pp. 3646-3653
    • Zverlov, V.V.1    Kellermann, J.2    Schwarz, W.H.3
  • 53
    • 0022001859 scopus 로고
    • Sequence of a cellulase gene of the thermophilic bacterium Clostridium thermocellum
    • Sequence of a cellulase gene of the thermophilic bacterium Clostridium thermocellum. Béguin P, Cornet P, Aubert JP, J Bacteriol 1985 162 102 105 (Pubitemid 15095839)
    • (1985) Journal of Bacteriology , vol.162 , Issue.1 , pp. 102-105
    • Beguin, P.1    Cornet, P.2    Aubert, J.-P.3
  • 54
  • 55
    • 40749098639 scopus 로고    scopus 로고
    • Endocellulolytic activity of the Clostridium thermocellum Cel9C (formerly CbhA) catalytic domain
    • DOI 10.1089/ind.2008.099
    • Endocellulolytic activity of the Clostridium thermocellum Cel9C (formerly CbhA) catalytic domain. McGrath CE, Wilson DB, Ind Biotechnol 2008 4 99 104 (Pubitemid 351390733)
    • (2008) Industrial Biotechnology , vol.4 , Issue.1 , pp. 99-104
    • McGrath, C.E.1    Wilson, D.B.2
  • 56
    • 0035117464 scopus 로고    scopus 로고
    • Properties and mutation analysis of the CelK cellulose-binding domain from the Clostridium thermocellum cellulosome
    • DOI 10.1128/JB.183.5.1552-1559.2001
    • Properties and mutation analysis of the CelK cellulose-binding domain from the Clostridium thermocellum cellulosome. Kataeva IA, Seidel RD, Li XL, Ljungdahl LG, J Bacteriol 2001 183 1552 1559 (Pubitemid 32172297)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1552-1559
    • Kataeva, I.A.1    Seidel III, R.D.2    Li, X.-L.3    Ljungdahl, L.G.4
  • 58
    • 0031592929 scopus 로고    scopus 로고
    • The crystal structure of a type I cohesin domain at 1.7 A resolution
    • DOI 10.1006/jmbi.1997.1326
    • The crystal structure of a type I cohesin domain at 1.7 A resolution. Tavares GA, Beguin P, Alzari PM, J Mol Biol 1997 273 701 713 (Pubitemid 27488811)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.3 , pp. 701-713
    • Tavares, G.A.1    Beguin, P.2    Alzari, P.M.3
  • 59
    • 77958497861 scopus 로고    scopus 로고
    • Thermobifida fusca exoglucanase Cel6B is incompatible with the cellulosomal mode in contrast to endoglucanase Cel6A
    • Thermobifida fusca exoglucanase Cel6B is incompatible with the cellulosomal mode in contrast to endoglucanase Cel6A. Caspi J, Barak Y, Haimovitz R, Gilary H, Irwin D, Lamed R, Wilson DB, Bayer EA, Syst Synth Biol 2010 4 193 201
    • (2010) Syst Synth Biol , vol.4 , pp. 193-201
    • Caspi, J.1    Barak, Y.2    Haimovitz, R.3    Gilary, H.4    Irwin, D.5    Lamed, R.6    Wilson, D.B.7    Bayer, E.A.8
  • 62
    • 0001728210 scopus 로고
    • Macromolecular Organization of the Cellulolytic Enzyme Complex of Clostridium thermocellum as Revealed by Electron Microscopy
    • Macromolecular Organization of the Cellulolytic Enzyme Complex of Clostridium thermocellum as Revealed by Electron Microscopy. Mayer F, Coughlan MP, Mori Y, Ljungdahl LG, Appl Environ Microbiol 1987 53 2785 2792
    • (1987) Appl Environ Microbiol , vol.53 , pp. 2785-2792
    • Mayer, F.1    Coughlan, M.P.2    Mori, Y.3    Ljungdahl, L.G.4
  • 64
    • 77953082436 scopus 로고    scopus 로고
    • Modular arrangement of a cellulosomal scaffoldin subunit revealed from the crystal structure of a cohesin dyad
    • Modular arrangement of a cellulosomal scaffoldin subunit revealed from the crystal structure of a cohesin dyad. Noach I, Levy-Assaraf M, Lamed R, Shimon LJ, Frolow F, Bayer EA, J Mol Biol 2010 399 294 305
    • (2010) J Mol Biol , vol.399 , pp. 294-305
    • Noach, I.1    Levy-Assaraf, M.2    Lamed, R.3    Shimon, L.J.4    Frolow, F.5    Bayer, E.A.6
  • 65
    • 67651115623 scopus 로고    scopus 로고
    • Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus
    • Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus. Noach I, Frolow F, Alber O, Lamed R, Shimon LJ, Bayer EA, J Mol Biol 2009 391 86 97
    • (2009) J Mol Biol , vol.391 , pp. 86-97
    • Noach, I.1    Frolow, F.2    Alber, O.3    Lamed, R.4    Shimon, L.J.5    Bayer, E.A.6
  • 66
    • 11244296147 scopus 로고    scopus 로고
    • Structural insights into the mechanism of formation of cellulosomes probed by small angle x-ray scattering
    • DOI 10.1074/jbc.M408979200
    • Structural insights into the mechanism of formation of cellulosomes probed by small angle X-ray scattering. Hammel M, Fierobe HP, Czjzek M, Finet S, Receveur-Brechot V, J Biol Chem 2004 279 55985 55994 (Pubitemid 40066606)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55985-55994
    • Hammel, M.1    Fierobe, H.-P.2    Czjzek, M.3    Finet, S.4    Receveur-Brechot, V.5
  • 67
    • 84861180864 scopus 로고    scopus 로고
    • Small-angle X-ray scattering and crystallography: A winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes
    • Small-angle X-ray scattering and crystallography: a winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes. Czjzek M, Fierobe HP, Receveur-Brechot V, Methods Enzymol 2012 510 183 210
    • (2012) Methods Enzymol , vol.510 , pp. 183-210
    • Czjzek, M.1    Fierobe, H.P.2    Receveur-Brechot, V.3
  • 70
    • 78650417465 scopus 로고    scopus 로고
    • Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesins linkers
    • Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesins linkers. Molinier AL, Nouailler M, Valette O, Tardif C, Receveur-Brechot V, Fierobe HP, J Mol Biol 2011 405 143 157
    • (2011) J Mol Biol , vol.405 , pp. 143-157
    • Molinier, A.L.1    Nouailler, M.2    Valette, O.3    Tardif, C.4    Receveur-Brechot, V.5    Fierobe, H.P.6
  • 71
    • 84869854102 scopus 로고    scopus 로고
    • How does plant cell wall nanoscale architecture correlate with enzymatic digestibility?
    • How does plant cell wall nanoscale architecture correlate with enzymatic digestibility? Ding SY, Liu YS, Zeng Y, Himmel ME, Baker JO, Bayer EA, Science 2012 338 1055 1060
    • (2012) Science , vol.338 , pp. 1055-1060
    • Ding, S.Y.1    Liu, Y.S.2    Zeng, Y.3    Himmel, M.E.4    Baker, J.O.5    Bayer, E.A.6
  • 73
    • 27744458385 scopus 로고    scopus 로고
    • Matching fusion protein systems for affinity analysis of two interacting families of proteins: The cohesin-dockerin interaction
    • DOI 10.1002/jmr.749
    • Matching fusion-protein systems for affinity analysis of two interacting families of proteins: The cohesin-dockerin interaction. Barak Y, Handelsman T, Nakar D, Mechaly A, Lamed R, Shoham Y, Bayer EA, J Mol Recogit 2005 18 491 501 (Pubitemid 41626122)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.6 , pp. 491-501
    • Barak, Y.1    Handelsman, T.2    Nakar, D.3    Mechaly, A.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.