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Volumn 5, Issue , 2012, Pages

Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber

Author keywords

Aspergillus fumigatus; Aspergillus niveus; Biofuels; Biomass decomposition; Cellobiohydrolase; Cellobiohydrolase D; Cellobiohydrolase I; Cellulases; Crystalline cellulose breakdown

Indexed keywords

ASPERGILLUS FUMIGATUS; ASPERGILLUS NIVEUS; CELLOBIOHYDROLASE I; CELLOBIOHYDROLASES; CELLULASES; CRYSTALLINE CELLULOSE;

EID: 84859479878     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-5-21     Document Type: Article
Times cited : (22)

References (74)
  • 3
    • 34249949390 scopus 로고    scopus 로고
    • The potential of cellulases and cellulosomes for cellulosic waste management
    • DOI 10.1016/j.copbio.2007.04.004, PII S0958166907000535, Energy biotechnology / Environmental biotechnology
    • The potential of cellulases and cellulosomes for cellulosic waste management. Bayer EA, Lamed R, Himmel ME, Curr Opin Biotechnol 2007 18 3 237 245 (Pubitemid 46880283)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.3 , pp. 237-245
    • Bayer, E.A.1    Lamed, R.2    Himmel, M.E.3
  • 6
    • 34047193841 scopus 로고    scopus 로고
    • Versatile derivatives of carbohydrate-binding modules for imaging of complex carbohydrates approaching the molecular level of resolution
    • 438, 440 passim
    • Versatile derivatives of carbohydrate-binding modules for imaging of complex carbohydrates approaching the molecular level of resolution. Ding SY, Xu Q, Ali MK, Baker JO, Bayer EA, Barak Y, Lamed R, Sugiyama J, Rumbles G, Himmel ME, Biotechniques 2006 41 4 435 436 438, 440 passim
    • (2006) Biotechniques , vol.41 , Issue.4 , pp. 435-436
    • Ding, S.Y.1    Xu, Q.2    Ali, M.K.3    Baker, J.O.4    Bayer, E.A.5    Barak, Y.6    Lamed, R.7    Sugiyama, J.8    Rumbles, G.9    Himmel, M.E.10
  • 7
    • 51649096979 scopus 로고    scopus 로고
    • Relative crystallinity of plant biomass: Studies on assembly, adaptation and acclimation
    • Relative crystallinity of plant biomass: studies on assembly, adaptation and acclimation. Harris D, DeBolt S, PLoS One 2008 3 8 2897
    • (2008) PLoS One , vol.3 , Issue.8 , pp. 52897
    • Harris, D.1    Debolt, S.2
  • 8
    • 77949519739 scopus 로고    scopus 로고
    • Fermentable sugars by chemical hydrolysis of biomass
    • Fermentable sugars by chemical hydrolysis of biomass. Binder JB, Raines RT, Proc Natl Acad Sci U S A 2010 107 10 4516 4521
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.10 , pp. 4516-4521
    • Binder, J.B.1    Raines, R.T.2
  • 10
    • 44449160515 scopus 로고    scopus 로고
    • Energy balance and emissions associated with biochar sequestration and pyrolysis bioenergy production
    • DOI 10.1021/es071361i
    • Energy balance and emissions associated with biochar sequestration and pyrolysis bioenergy production. Gaunt JL, Lehmann J, Environ Sci Technol 2008 42 11 4152 4158 (Pubitemid 351770076)
    • (2008) Environmental Science and Technology , vol.42 , Issue.11 , pp. 4152-4158
    • Gaunt, J.L.1    Lehmann, J.2
  • 11
    • 17144409963 scopus 로고    scopus 로고
    • Detoxification of corn stover and corn starch pyrolysis liquors by Pseudomonas putida and Streptomyces setonii suspended cells and plastic compost support biofilms
    • Detoxification of corn stover and corn starch pyrolysis liquors by Pseudomonas putida and Streptomyces setonii suspended cells and plastic compost support biofilms. Khiyami MA, Pometto Iii AL, Brown RC, J Agric Food Chem 2005 53 8 2978 2987 (Pubitemid 40525259)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.8 , pp. 2978-2987
    • Khiyami, M.A.1    Pometto III, A.L.2    Brown, R.C.3
  • 13
    • 0027523710 scopus 로고
    • Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei
    • DOI 10.1016/0014-5793(93)81202-B
    • Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei. Macarron R, van Beeumen J, Henrissat B, de la Mata I, Claeyssens M, FEBS Lett 1993 316 2 137 140 (Pubitemid 23025045)
    • (1993) FEBS Letters , vol.316 , Issue.2 , pp. 137-140
    • Macarron, R.1    Van Beeumen, J.2    Henrissat, B.3    De La Mata, I.4    Claeyssens, M.5
  • 14
    • 0242383940 scopus 로고    scopus 로고
    • Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4- and β-1,3;1,4-linked glucans
    • DOI 10.1016/S0141-8130(03)00080-1
    • Catalytic properties and mode of action of three endo-beta-glucanases from Talaromyces emersonii on soluble beta-1,4- and beta-1,3;1,4-linked glucans. McCarthy T, Hanniffy O, Savage AV, Tuohy MG, Int J Biol Macromol 2003 33 1-3 141 148 (Pubitemid 37346369)
    • (2003) International Journal of Biological Macromolecules , vol.33 , Issue.1-3 , pp. 141-148
    • McCarthy, T.1    Hanniffy, O.2    Savage, A.V.3    Tuohy, M.G.4
  • 17
    • 34249300873 scopus 로고    scopus 로고
    • The structural basis for the exo-mode of action in GH74 oligoxyloglucan reducing end-specific cellobiohydrolase
    • DOI 10.1016/j.jmb.2007.04.035, PII S0022283607004925
    • The structural basis for the exo-mode of action in GH74 oligoxyloglucan reducing end-specific cellobiohydrolase. Yaoi K, Kondo H, Hiyoshi A, Noro N, Sugimoto H, Tsuda S, Mitsuishi Y, Miyazaki K, J Mol Biol 2007 370 1 53 62 (Pubitemid 46817567)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.1 , pp. 53-62
    • Yaoi, K.1    Kondo, H.2    Hiyoshi, A.3    Noro, N.4    Sugimoto, H.5    Tsuda, S.6    Mitsuishi, Y.7    Miyazaki, K.8
  • 18
    • 0030426625 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the β-D-glucosidase gene from Bifidobacterium breve clb, and expression of β-D-glucosidase activity in Escherichia coli
    • Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli. Nunoura N, Ohdan K, Tanaka K, Tamaki H, Yano T, Inui M, Yukawa H, Yamamoto K, Kumagai H, Biosci Biotechnol Biochem 1996 60 12 2011 2018 (Pubitemid 27155794)
    • (1996) Bioscience, Biotechnology and Biochemistry , vol.60 , Issue.12 , pp. 2011-2018
    • Nunoura, N.1    Ohdan, K.2    Tanaka, K.3    Tamaki, H.4    Yano, T.5    Inui, M.6    Yukawa, H.7    Yamamoto, K.8    Kumagai, H.9
  • 19
    • 0030088099 scopus 로고    scopus 로고
    • Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose
    • Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose. Nunoura N, Ohdan K, Yano T, Yamamoto K, Kumagai H, Biosci Biotechnol Biochem 1996 60 2 188 193
    • (1996) Biosci Biotechnol Biochem , vol.60 , Issue.2 , pp. 188-193
    • Nunoura, N.1    Ohdan, K.2    Yano, T.3    Yamamoto, K.4    Kumagai, H.5
  • 21
    • 0034029116 scopus 로고    scopus 로고
    • Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A
    • DOI 10.1128/AEM.66.4.1444-1452.2000
    • Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A. Boisset C, Fraschini C, Schulein M, Henrissat B, Chanzy H, Appl Environ Microbiol 2000 66 4 1444 1452 (Pubitemid 30185615)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.4 , pp. 1444-1452
    • Boisset, C.1    Fraschini, C.2    Schulein, M.3    Henrissat, B.4    Chanzy, H.5
  • 22
    • 0036022022 scopus 로고    scopus 로고
    • Cooperative and competitive binding in synergistic mixtures of Thermobifida fusca cellulases Cel5A, Cel6B, and Cel9A
    • DOI 10.1021/bp0200402
    • Cooperative and competitive binding in synergistic mixtures of Thermobifida fusca cellulases Cel5A, Cel6B, and Cel9A. Jeoh T, Wilson DB, Walker LP, Biotechnol Prog 2002 18 4 760 769 (Pubitemid 34853387)
    • (2002) Biotechnology Progress , vol.18 , Issue.4 , pp. 760-769
    • Jeoh, T.1    Wilson, D.B.2    Walker, L.P.3
  • 23
    • 0024116875 scopus 로고
    • Mode of action and synergism of cellulases from Penicillium funiculosum
    • Mode of action and synergism of cellulases from Penicillium funiculosum. Mishra C, Rao M, Appl Biochem Biotechnol 1988 19 2 139 150
    • (1988) Appl Biochem Biotechnol , vol.19 , Issue.2 , pp. 139-150
    • Mishra, C.1    Rao, M.2
  • 24
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G, Proc Natl Acad Sci U S A 1995 92 15 7090 7094
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.15 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 26
    • 0035809069 scopus 로고    scopus 로고
    • Optimized mixtures of recombinant Humicola insolens cellulases for the biodegradation of crystalline cellulose
    • DOI 10.1002/1097-0290(20010205)72:3<339::AID-BIT11>3.0.CO;2-#
    • Optimized mixtures of recombinant Humicola insolens cellulases for the biodegradation of crystalline cellulose. Boisset C, Petrequin C, Chanzy H, Henrissat B, Schulein M, Biotechnol Bioeng 2001 72 3 339 345 (Pubitemid 32101440)
    • (2001) Biotechnology and Bioengineering , vol.72 , Issue.3 , pp. 339-345
    • Boisset, C.1    Petrequin, C.2    Chanzy, H.3    Henrissat, B.4    Schlein, M.5
  • 27
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Structures and mechanisms of glycosyl hydrolases. Davies G, Henrissat B, Structure 1995 3 9 853 859
    • (1995) Structure , vol.3 , Issue.9 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 28
    • 12844278017 scopus 로고    scopus 로고
    • Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates
    • DOI 10.1042/BJ20041144
    • Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as burst kinetics on fluorescent polymeric model substrates. Kipper K, Valjamae P, Johansson G, Biochem J 2005 385 Pt 2 527 535 (Pubitemid 40165086)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 527-535
    • Kipper, K.1    Valjamae, P.2    Johansson, G.3
  • 29
    • 0036211985 scopus 로고    scopus 로고
    • Determination of subunit composition of Clostridium cellulovorans cellulosomes that degrade plant cell walls
    • DOI 10.1128/AEM.68.4.1610-1615.2002
    • Determination of subunit composition of Clostridium cellulovorans cellulosomes that degrade plant cell walls. Murashima K, Kosugi A, Doi RH, Appl Environ Microbiol 2002 68 4 1610 1615 (Pubitemid 34279965)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.4 , pp. 1610-1615
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 30
    • 0032708967 scopus 로고    scopus 로고
    • Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis
    • Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis. Palonen H, Tenkanen M, Linder M, Appl Environ Microbiol 1999 65 12 5229 5233 (Pubitemid 129520602)
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.12 , pp. 5229-5233
    • Palonen, H.1    Tenkanen, M.2    Linder, M.3
  • 31
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA, Science 1990 249 4967 380 386
    • (1990) Science , vol.249 , Issue.4967 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.K.4    Jones, T.A.5
  • 32
    • 33746879626 scopus 로고    scopus 로고
    • A functionally based model for hydrolysis of cellulose by fungal cellulase
    • DOI 10.1002/bit.20906
    • A functionally based model for hydrolysis of cellulose by fungal cellulase. Zhang YH, Lynd LR, Biotechnol Bioeng 2006 94 5 888 898 (Pubitemid 44186896)
    • (2006) Biotechnology and Bioengineering , vol.94 , Issue.5 , pp. 888-898
    • Zhang, Y.-H.P.1    Lynd, L.R.2
  • 33
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA, Science 1994 265 5171 524 528 (Pubitemid 24264997)
    • (1994) Science , vol.265 , Issue.5171 , pp. 524-528
    • Divne, C.1    Stahlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.C.6    Teeri, T.T.7    Jones, T.A.8
  • 34
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei
    • DOI 10.1006/jmbi.1997.1437
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. Divne C, Stahlberg J, Teeri TT, Jones TA, J Mol Biol 1998 275 2 309 325 (Pubitemid 28030006)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.2 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 35
    • 0032532639 scopus 로고    scopus 로고
    • Crystal structure of the family 7 endoglucanase i (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate
    • Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate. MacKenzie LF, Sulzenbacher G, Divne C, Jones TA, Woldike HF, Schulein M, Withers SG, Davies GJ, Biochem J 1998 335 Pt 2 409 416
    • (1998) Biochem J , vol.335 , Issue.PART 2 , pp. 409-416
    • MacKenzie, L.F.1    Sulzenbacher, G.2    Divne, C.3    Jones, T.A.4    Woldike, H.F.5    Schulein, M.6    Withers, S.G.7    Davies, G.J.8
  • 37
    • 0033556286 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution
    • DOI 10.1042/0264-6021:3370297
    • Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution. Varrot A, Hastrup S, Schulein M, Davies GJ, Biochem J 1999 337 Pt 2 297 304 (Pubitemid 29052024)
    • (1999) Biochemical Journal , vol.337 , Issue.2 , pp. 297-304
    • Varrot, A.1    Hastrup, S.2    Schulein, M.3    Davies, G.J.4
  • 38
    • 0040964309 scopus 로고    scopus 로고
    • Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding
    • Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding. Varrot A, Schulein M, Davies GJ, Biochemistry 1999 38 28 8884 8891
    • (1999) Biochemistry , vol.38 , Issue.28 , pp. 8884-8891
    • Varrot, A.1    Schulein, M.2    Davies, G.J.3
  • 39
    • 0033199581 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei
    • DOI 10.1016/S0969-2126(99)80171-3
    • Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei. Zou J, Kleywegt GJ, Stahlberg J, Driguez H, Nerinckx W, Claeyssens M, Koivula A, Teeri TT, Jones TA, Structure 1999 7 9 1035 1045 (Pubitemid 29436501)
    • (1999) Structure , vol.7 , Issue.9 , pp. 1035-1045
    • Zou, J.-Y.1    Kleywegt, G.J.2    Stahlberg, J.3    Driguez, H.4    Nerinckx, W.5    Claeyssens, M.6    Koivula, A.7    Teeri, T.T.8    Jones, T.A.9
  • 40
    • 76249113333 scopus 로고    scopus 로고
    • Identification of amino acids responsible for processivity in a Family 1 carbohydrate-binding module from a fungal cellulase
    • Identification of amino acids responsible for processivity in a Family 1 carbohydrate-binding module from a fungal cellulase. Beckham GT, Matthews JF, Bomble YJ, Bu L, Adney WS, Himmel ME, Nimlos MR, Crowley MF, J Phys Chem B 2010 114 3 1447 1453
    • (2010) J Phys Chem B , vol.114 , Issue.3 , pp. 1447-1453
    • Beckham, G.T.1    Matthews, J.F.2    Bomble, Y.J.3    Bu, L.4    Adney, W.S.5    Himmel, M.E.6    Nimlos, M.R.7    Crowley, M.F.8
  • 41
    • 47349122440 scopus 로고    scopus 로고
    • A novel function for the cellulose binding module of cellobiohydrolase I
    • DOI 10.1007/s11427-008-0088-3
    • A novel function for the cellulose binding module of cellobiohydrolase I. Wang L, Zhang Y, Gao P, Sci China C Life Sci 2008 51 7 620 629 (Pubitemid 351999750)
    • (2008) Science in China, Series C: Life Sciences , vol.51 , Issue.7 , pp. 620-629
    • Wang, L.1    Zhang, Y.2    Gao, P.3
  • 42
    • 68149156908 scopus 로고    scopus 로고
    • The energy landscape for the interaction of the family 1 carbohydrate-binding module and the cellulose surface is altered by hydrolyzed glycosidic bonds
    • The energy landscape for the interaction of the family 1 carbohydrate-binding module and the cellulose surface is altered by hydrolyzed glycosidic bonds. Bu L, Beckham GT, Crowley MF, Chang CH, Matthews JF, Bomble YJ, Adney WS, Himmel ME, Nimlos MR, J Phys Chem B 2009 113 31 10994 11002
    • (2009) J Phys Chem B , vol.113 , Issue.31 , pp. 10994-11002
    • Bu, L.1    Beckham, G.T.2    Crowley, M.F.3    Chang, C.H.4    Matthews, J.F.5    Bomble, Y.J.6    Adney, W.S.7    Himmel, M.E.8    Nimlos, M.R.9
  • 43
    • 34948842973 scopus 로고    scopus 로고
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates
    • DOI 10.1099/mic.0.2006/000513-0
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates. Sato S, Liu F, Koc H, Tien M, Microbiology 2007 153 Pt 9 3023 3033 (Pubitemid 47517063)
    • (2007) Microbiology , vol.153 , Issue.9 , pp. 3023-3033
    • Sato, S.1    Liu, F.2    Koc, H.3    Tien, M.4
  • 47
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii
    • DOI 10.1111/j.1432-1033.2004.04409.x
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Grassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, Tuohy MG, Eur J Biochem 2004 271 22 4495 4506 (Pubitemid 39585212)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.22 , pp. 4495-4506
    • Grassick, A.1    Murray, P.G.2    Thompson, R.3    Collins, C.M.4    Byrnes, L.5    Birrane, G.6    Higgins, T.M.7    Tuohy, M.G.8
  • 48
    • 78650791313 scopus 로고    scopus 로고
    • Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Santos CR, Tonoli CC, Trindade DM, Betzel C, Takata H, Kuriki T, Kanai T, Imanaka T, Arni RK, Murakami MT, Proteins 2011 79 2 547 557
    • (2011) Proteins , vol.79 , Issue.2 , pp. 547-557
    • Santos, C.R.1    Tonoli, C.C.2    Trindade, D.M.3    Betzel, C.4    Takata, H.5    Kuriki, T.6    Kanai, T.7    Imanaka, T.8    Arni, R.K.9    Murakami, M.T.10
  • 49
    • 80052394586 scopus 로고    scopus 로고
    • The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain
    • The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain. Hall M, Rubin J, Behrens SH, Bommarius AS, J Biotechnol 2011 155 4 370 376
    • (2011) J Biotechnol , vol.155 , Issue.4 , pp. 370-376
    • Hall, M.1    Rubin, J.2    Behrens, S.H.3    Bommarius, A.S.4
  • 51
    • 79955971297 scopus 로고    scopus 로고
    • Probing carbohydrate product expulsion from a processive cellulase with multiple absolute binding free energy methods
    • Probing carbohydrate product expulsion from a processive cellulase with multiple absolute binding free energy methods. Bu L, Beckham GT, Shirts MR, Nimlos MR, Adney WS, Himmel ME, Crowley MF, J Biol Chem 2011 286 20 18161 18169
    • (2011) J Biol Chem , vol.286 , Issue.20 , pp. 18161-18169
    • Bu, L.1    Beckham, G.T.2    Shirts, M.R.3    Nimlos, M.R.4    Adney, W.S.5    Himmel, M.E.6    Crowley, M.F.7
  • 52
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • Processivity of cellobiohydrolases is limited by the substrate. Kurasin M, Valjamae P, J Biol Chem 2011 286 1 169 177
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 169-177
    • Kurasin, M.1    Valjamae, P.2
  • 53
    • 73649106924 scopus 로고    scopus 로고
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase i on crystalline cellulose
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose. Igarashi K, Koivula A, Wada M, Kimura S, Penttila M, Samejima M, J Biol Chem 2009 284 52 36186 36190
    • (2009) J Biol Chem , vol.284 , Issue.52 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttila, M.5    Samejima, M.6
  • 55
    • 84856839149 scopus 로고    scopus 로고
    • Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes
    • Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes. Fox JM, Levine SE, Clark DS, Blanch HW, Biochemistry 2012 51 1 442 452
    • (2012) Biochemistry , vol.51 , Issue.1 , pp. 442-452
    • Fox, J.M.1    Levine, S.E.2    Clark, D.S.3    Blanch, H.W.4
  • 56
    • 0343907838 scopus 로고    scopus 로고
    • Attack of carboxymethylcellulose at opposite ends by two cellobiohydrolases from Cellulomonas fimi
    • DOI 10.1016/S0168-1656(97)00091-6, PII S0168165697000916
    • Attack of carboxymethylcellulose at opposite ends by two cellobiohydrolases from Cellulomonas fimi. Gilkes NR, Kwan E, Kilburn DG, Miller RC, Warren RAJ, Journal of Biotechnology 1997 57 1-3 83 90 (Pubitemid 27397473)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 83-90
    • Gilkes, N.R.1    Kwan, E.2    Kilburn, D.G.3    Miller, R.C.4    Warren, R.A.J.5
  • 57
    • 33947663004 scopus 로고    scopus 로고
    • Detection and identification of rhamnogalacturonan lyase activity in intercellular spaces of expanding cotton cotyledons
    • DOI 10.1111/j.1365-313X.2007.03033.x
    • Detection and identification of rhamnogalacturonan lyase activity in intercellular spaces of expanding cotton cotyledons. Naran R, Pierce ML, Mort AJ, Plant J 2007 50 1 95 107 (Pubitemid 46493396)
    • (2007) Plant Journal , vol.50 , Issue.1 , pp. 95-107
    • Naran, R.1    Pierce, M.L.2    Mort, A.J.3
  • 58
    • 77952511855 scopus 로고    scopus 로고
    • Cellulose crystallinity index: Measurement techniques and their impact on interpreting cellulase performance
    • Cellulose crystallinity index: measurement techniques and their impact on interpreting cellulase performance. Park S, Baker JO, Himmel ME, Parilla PA, Johnson DK, Biotechnology for biofuels 2010 3 1 10
    • (2010) Biotechnology for Biofuels , vol.3 , Issue.1 , pp. 10
    • Park, S.1    Baker, J.O.2    Himmel, M.E.3    Parilla, P.A.4    Johnson, D.K.5
  • 59
    • 0026716945 scopus 로고
    • Coomassie blue protein dye-binding assays measure formation of an insoluble protein-dye complex
    • Coomassie blue protein dye-binding assays measure formation of an insoluble protein-dye complex. Marshall T, Williams KM, Anal Biochem 1992 204 1 107 109
    • (1992) Anal Biochem , vol.204 , Issue.1 , pp. 107-109
    • Marshall, T.1    Williams, K.M.2
  • 60
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Shapiro AL, Vinuela E, Maizel JV, Biochem Biophys Res Commun 1967 28 5 815 820
    • (1967) Biochem Biophys Res Commun , vol.28 , Issue.5 , pp. 815-820
    • Shapiro, A.L.1    Vinuela, E.2    Maizel, J.V.3
  • 62
    • 0026437237 scopus 로고
    • Sexual and parasexual genetics of Aspergillus species
    • Sexual and parasexual genetics of Aspergillus species. Clutterbuck AJ, Biotechnology 1992 23 3 18
    • (1992) Biotechnology , vol.23 , pp. 3-18
    • Clutterbuck, A.J.1
  • 64
    • 0021346063 scopus 로고
    • Transformation of Aspergillus nidulans by using a trpC plasmid
    • Transformation of Aspergillus nidulans by using a trpC plasmid. Yelton MM, Hamer JE, Timberlake WE, Proc Natl Acad Sci U S A 1984 81 5 1470 1474 (Pubitemid 14174524)
    • (1984) ISOTOPENPRAXIS , vol.20 , Issue.1 , pp. 1470-1474
    • Yelton, M.M.1    Hamer, J.E.2    Timberlake, W.E.3
  • 65
    • 0026801912 scopus 로고
    • Activity staining of endoglucanases in polyacrylamide gels
    • Activity staining of endoglucanases in polyacrylamide gels. Mathew R, Rao KK, Anal Biochem 1992 206 1 50 52
    • (1992) Anal Biochem , vol.206 , Issue.1 , pp. 50-52
    • Mathew, R.1    Rao, K.K.2
  • 66
    • 0023377515 scopus 로고
    • Activity staining of cellulases in polyacrylamide gels containing mixed linkage beta-glucans
    • Activity staining of cellulases in polyacrylamide gels containing mixed linkage beta-glucans. Schwarz WH, Bronnenmeier K, Grabnitz F, Staudenbauer WL, Anal Biochem 1987 164 1 72 77
    • (1987) Anal Biochem , vol.164 , Issue.1 , pp. 72-77
    • Schwarz, W.H.1    Bronnenmeier, K.2    Grabnitz, F.3    Staudenbauer, W.L.4
  • 67
    • 0021456988 scopus 로고
    • A method for the detection and differentiation of cellulase components in polyacrylamide gels
    • A method for the detection and differentiation of cellulase components in polyacrylamide gels. Bartley TD, Murphy-Holland K, Eveleigh DE, Anal Biochem 1984 140 1 157 161
    • (1984) Anal Biochem , vol.140 , Issue.1 , pp. 157-161
    • Bartley, T.D.1    Murphy-Holland, K.2    Eveleigh, D.E.3
  • 68
    • 0020771857 scopus 로고
    • Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas
    • Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas. Beguin P, Anal Biochem 1983 131 2 333 336
    • (1983) Anal Biochem , vol.131 , Issue.2 , pp. 333-336
    • Beguin, P.1
  • 69
    • 33747333106 scopus 로고
    • Use of dintirosalicilic acid reagent for determination of reducing sugar
    • Use of dintirosalicilic acid reagent for determination of reducing sugar. Miller GL, Analytical Chemistry 1959 31 426 428
    • (1959) Analytical Chemistry , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 70
    • 0032005113 scopus 로고    scopus 로고
    • Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei
    • DOI 10.1046/j.1432-1327.1998.2510885.x
    • Modes of action on cotton and bacterial cellulose of a homologous endoglucanase-exoglucanase pair from Trichoderma reesei. Srisodsuk M, Kleman-Leyer K, Keranen S, Kirk TK, Teeri TT, Eur J Biochem 1998 251 3 885 892 (Pubitemid 28108985)
    • (1998) European Journal of Biochemistry , vol.251 , Issue.3 , pp. 885-892
    • Srisodsuk, M.1    Kleman-Leyer, K.2    Keranen, S.3    Kirk, T.K.4    Teeri, T.T.5
  • 71
    • 0347383758 scopus 로고    scopus 로고
    • MODELLER: Generation and refinement of homology-based protein structure models
    • DOI 10.1016/S0076-6879(03)74020-8
    • Modeller: generation and refinement of homology-based protein structure models. Fiser A, Sali A, Methods Enzymol 2003 374 461 491 (Pubitemid 37531821)
    • (2003) Methods in Enzymology , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 74
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Bayesian statistical analysis of protein side-chain rotamer preferences. Dunbrack RL, Cohen FE, Protein Sci 1997 6 8 1661 1681 (Pubitemid 27333069)
    • (1997) Protein Science , vol.6 , Issue.8 , pp. 1661-1681
    • Dunbrack Jr., R.L.1    Cohen, F.E.2


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