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Volumn 110, Issue 6, 2013, Pages 1529-1549

Visualizing cellulase activity

Author keywords

(E)TEM; AFM; Cellulase; Cellulose degradation; Renewable energy; SEM

Indexed keywords

ADVANCED VISUALIZATIONS; AFM; BIOTECHNOLOGICAL PRODUCTION; CELLULASE; CELLULOSE DEGRADATION; COMMERCIAL EXPLOITATION; RENEWABLE ENERGIES; SUBSTRATE MORPHOLOGIES;

EID: 84876774277     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24884     Document Type: Review
Times cited : (47)

References (143)
  • 1
    • 60049098657 scopus 로고
    • Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung
    • Abbe E. 1873. Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung. Arch Mikrosk Anat 9: 413-420.
    • (1873) Arch Mikrosk Anat , vol.9 , pp. 413-420
    • Abbe, E.1
  • 2
    • 0024286212 scopus 로고
    • Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: Close resemblance to cellobiohydrolase I
    • Abuja PM, Pilz I, Claeyssens M, Tomme P. 1988a. Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: Close resemblance to cellobiohydrolase I. Biochem Biophys Res Commun 156: 180-185.
    • (1988) Biochem Biophys Res Commun , vol.156 , pp. 180-185
    • Abuja, P.M.1    Pilz, I.2    Claeyssens, M.3    Tomme, P.4
  • 4
    • 77649274709 scopus 로고    scopus 로고
    • Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: Crystal structure of interacting Clostridium thermocellum multimodular components
    • Adams JJ, Currie MA, Ali S, Bayer EA, Jia Z, Smith SP. 2010. Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: Crystal structure of interacting Clostridium thermocellum multimodular components. J Mol Biol 396: 833-839.
    • (2010) J Mol Biol , vol.396 , pp. 833-839
    • Adams, J.J.1    Currie, M.A.2    Ali, S.3    Bayer, E.A.4    Jia, Z.5    Smith, S.P.6
  • 5
    • 55549135339 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of native cellulose nanofibrils and other cellulose model films: Effect of surface structure
    • Ahola S, Turon X, Osterberg M, Laine J, Rojas OJ. 2008. Enzymatic hydrolysis of native cellulose nanofibrils and other cellulose model films: Effect of surface structure. Langmuir 24: 11592-11599.
    • (2008) Langmuir , vol.24 , pp. 11592-11599
    • Ahola, S.1    Turon, X.2    Osterberg, M.3    Laine, J.4    Rojas, O.J.5
  • 7
    • 77950356429 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis
    • Arantes V, Saddler JN. 2010. Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis. Biotechnol Biofuels 3: 4.
    • (2010) Biotechnol Biofuels , vol.3 , pp. 4
    • Arantes, V.1    Saddler, J.N.2
  • 10
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr BK, Hsieh YL, Ganem B, Wilson DB. 1996. Identification of two functionally different classes of exocellulases. Biochemistry 35: 586-592.
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.L.2    Ganem, B.3    Wilson, D.B.4
  • 11
    • 0022512490 scopus 로고
    • Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose
    • Bayer EA, Lamed R. 1986. Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose. J Bacteriol 167: 828-836.
    • (1986) J Bacteriol , vol.167 , pp. 828-836
    • Bayer, E.A.1    Lamed, R.2
  • 12
    • 79953781576 scopus 로고    scopus 로고
    • Molecular-level origins of biomass recalcitrance: Decrystallization free energies for four common cellulose polymorphs
    • Beckham GT, Matthews JF, Peters B, Bomble YJ, Himmel ME, Crowley MF. 2011. Molecular-level origins of biomass recalcitrance: Decrystallization free energies for four common cellulose polymorphs. J Phys Chem B 115: 4118-4127.
    • (2011) J Phys Chem B , vol.115 , pp. 4118-4127
    • Beckham, G.T.1    Matthews, J.F.2    Peters, B.3    Bomble, Y.J.4    Himmel, M.E.5    Crowley, M.F.6
  • 14
    • 0001516950 scopus 로고
    • Ultrastructural localization of hemicellulose in birch wood (Betula papyrifera) decayed by brown and white rot fungi
    • Blanchette RA, Abad AR. 1988. Ultrastructural localization of hemicellulose in birch wood (Betula papyrifera) decayed by brown and white rot fungi. Holzforschung 42: 393-398.
    • (1988) Holzforschung , vol.42 , pp. 393-398
    • Blanchette, R.A.1    Abad, A.R.2
  • 15
    • 0001298434 scopus 로고
    • Colloidal gold cytochemistry of endo-1,4-beta-glucanase, 1,4-beta-D-glucan cellobiohydrolase, and endo-1,4-beta-xylanase: Ultrastructure of sound and decayed birch wood
    • Blanchette RA, Abad AR, Cease KR, Lovrien RE, Leathers TD. 1989. Colloidal gold cytochemistry of endo-1, 4-beta-glucanase, 1, 4-beta-D-glucan cellobiohydrolase, and endo-1, 4-beta-xylanase: Ultrastructure of sound and decayed birch wood. Appl Environ Microbiol 55: 2293-2301.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 2293-2301
    • Blanchette, R.A.1    Abad, A.R.2    Cease, K.R.3    Lovrien, R.E.4    Leathers, T.D.5
  • 16
    • 0002797974 scopus 로고    scopus 로고
    • An ultrastructural study of the interaction of a fungal endoglucanase from Humicola insolens with cotton fibers
    • Boisset C, Chanzy H, Schülein M, Henrissat B. 1997. An ultrastructural study of the interaction of a fungal endoglucanase from Humicola insolens with cotton fibers. Cellulose 4: 7-20.
    • (1997) Cellulose , vol.4 , pp. 7-20
    • Boisset, C.1    Chanzy, H.2    Schülein, M.3    Henrissat, B.4
  • 17
    • 0033564316 scopus 로고    scopus 로고
    • Digestion of crystalline cellulose substrates by the Clostridium thermocellum cellulosome: Structural and morphological aspects
    • Boisset C, Chanzy H, Henrissat B, Lamed R, Shoham Y, Bayer EA. 1999. Digestion of crystalline cellulose substrates by the Clostridium thermocellum cellulosome: Structural and morphological aspects. Biochem J 340: 829-835.
    • (1999) Biochem J , vol.340 , pp. 829-835
    • Boisset, C.1    Chanzy, H.2    Henrissat, B.3    Lamed, R.4    Shoham, Y.5    Bayer, E.A.6
  • 18
    • 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
    • Boisset C, Fraschini C, Schülein M, Henrissat B, Chanzy H. 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. Appl Environ Microbiol 66: 1444-1452.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1444-1452
    • Boisset, C.1    Fraschini, C.2    Schülein, M.3    Henrissat, B.4    Chanzy, H.5
  • 19
    • 0034850875 scopus 로고    scopus 로고
    • Rotation of cellulose ribbons during degradation with fungal cellulase
    • Bowling AJ, Amano Y, Lindstrom R, Brown RMJ. 2001. Rotation of cellulose ribbons during degradation with fungal cellulase. Cellulose 8: 91-97.
    • (2001) Cellulose , vol.8 , pp. 91-97
    • Bowling, A.J.1    Amano, Y.2    Lindstrom, R.3    Brown, R.M.J.4
  • 22
    • 84856072252 scopus 로고    scopus 로고
    • Cellulases dig deep: In situ observation of the mesoscopic structural dynamics of enzymatic cellulose degradation
    • Bubner P, Dohr J, Plank H, Mayrhofer C, Nidetzky B. 2012. Cellulases dig deep: In situ observation of the mesoscopic structural dynamics of enzymatic cellulose degradation. J Biol Chem 287: 2759-2765.
    • (2012) J Biol Chem , vol.287 , pp. 2759-2765
    • Bubner, P.1    Dohr, J.2    Plank, H.3    Mayrhofer, C.4    Nidetzky, B.5
  • 23
    • 70349586142 scopus 로고    scopus 로고
    • Contact-mode high-resolution high-speed atomic force microscopy movies of the purple membrane
    • Casuso I, Kodera N, Le Grimellec C, Ando T, Scheuring S. 2009. Contact-mode high-resolution high-speed atomic force microscopy movies of the purple membrane. Biophys J 97: 1354-1361.
    • (2009) Biophys J , vol.97 , pp. 1354-1361
    • Casuso, I.1    Kodera, N.2    Le Grimellec, C.3    Ando, T.4    Scheuring, S.5
  • 24
    • 0001879663 scopus 로고
    • Electron microscopy study of the enzymic hydrolysis of Valonia cellulose
    • Chanzy H, Henrissat B. 1983. Electron microscopy study of the enzymic hydrolysis of Valonia cellulose. Carbohydr Polym 3: 161-173.
    • (1983) Carbohydr Polym , vol.3 , pp. 161-173
    • Chanzy, H.1    Henrissat, B.2
  • 25
    • 0000028633 scopus 로고
    • Undirectional degradation of Valonia cellulose microcrystals subjected to cellulase action
    • Chanzy H, Henrissat B. 1985. Undirectional degradation of Valonia cellulose microcrystals subjected to cellulase action. FEBS Lett 184: 285-288.
    • (1985) FEBS Lett , vol.184 , pp. 285-288
    • Chanzy, H.1    Henrissat, B.2
  • 26
    • 0000551058 scopus 로고
    • The action of 1,4-β-D-glucan cellobiohydrolase on Valonia cellulose microcrystals. An electron microscopy study
    • Chanzy H, Henrissat B, Vuong H, Schülein M. 1983. The action of 1, 4-β-D-glucan cellobiohydrolase on Valonia cellulose microcrystals. An electron microscopy study. FEBS Lett 153: 113-118.
    • (1983) FEBS Lett , vol.153 , pp. 113-118
    • Chanzy, H.1    Henrissat, B.2    Vuong, H.3    Schülein, M.4
  • 27
    • 0000899955 scopus 로고
    • Colloidal gold labelling of 1,4-ß-D-glucan cellobiohydrolase adsorbed on cellulose substrates
    • Chanzy H, Henrissat B, Vuong H. 1984. Colloidal gold labelling of 1, 4-ß-D-glucan cellobiohydrolase adsorbed on cellulose substrates. FEBS Lett 172: 193-197.
    • (1984) FEBS Lett , vol.172 , pp. 193-197
    • Chanzy, H.1    Henrissat, B.2    Vuong, H.3
  • 29
    • 0004108136 scopus 로고
    • Clegg DW, Collyer AA, editors. . . New York: Elsevier Science.
    • Clegg DW, Collyer AA, editors. 1991. Irradiation effects on polymers. New York: Elsevier Science.
    • (1991) Irradiation effects on polymers
  • 32
    • 33847073028 scopus 로고    scopus 로고
    • Swelling and dissolution of cellulose part 1: Free floating cotton and wood fibres in N-methylmorpholine-N-oxide-water mixtures
    • Cuissinat C, Navard P. 2006. Swelling and dissolution of cellulose part 1: Free floating cotton and wood fibres in N-methylmorpholine-N-oxide-water mixtures. Macromol Symp 244: 1-18.
    • (2006) Macromol Symp , vol.244 , pp. 1-18
    • Cuissinat, C.1    Navard, P.2
  • 35
    • 0026376539 scopus 로고
    • The Iα→Iβ transformation of highly crystalline cellulose by annealing in various mediums
    • Debzi EM, Chanzy H, Sugiyama J, Tekely P, Excoffier G. 1991. The Iα→Iβ transformation of highly crystalline cellulose by annealing in various mediums. Macromolecules 24: 6816-6822.
    • (1991) Macromolecules , vol.24 , pp. 6816-6822
    • Debzi, E.M.1    Chanzy, H.2    Sugiyama, J.3    Tekely, P.4    Excoffier, G.5
  • 36
    • 14044262855 scopus 로고    scopus 로고
    • Serial block-face scanning electron microscopy to reconstruct three-dimensional tissue nanostructure
    • Denk W, Horstmann H. 2004. Serial block-face scanning electron microscopy to reconstruct three-dimensional tissue nanostructure. PLoS Biol 2: e329.
    • (2004) PLoS Biol , vol.2
    • Denk, W.1    Horstmann, H.2
  • 37
    • 33244486953 scopus 로고    scopus 로고
    • The maize primary cell wall microfibril: A new model derived from direct visualization
    • Ding SY, Himmel ME. 2006. The maize primary cell wall microfibril: A new model derived from direct visualization. J Agric Food Chem 54: 597-606.
    • (2006) J Agric Food Chem , vol.54 , pp. 597-606
    • Ding, S.Y.1    Himmel, M.E.2
  • 38
    • 34047193841 scopus 로고    scopus 로고
    • 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. 2006. Versatile derivatives of carbohydrate-binding modules for imaging of complex carbohydrates approaching the molecular level of resolution. Biotechniques 41(435-436): 438-440.
    • (2006) Biotechniques , vol.41 , Issue.435-436 , pp. 438-440
    • 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
  • 40
    • 84869854102 scopus 로고    scopus 로고
    • How does plant cell wall nanoscale architecture correlate with enzymatic digestibility?
    • Ding SY, Liu YS, Zeng Y, Himmel ME, Baker JO, Bayer EA. 2012. How does plant cell wall nanoscale architecture correlate with enzymatic digestibility? Science 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
  • 44
    • 25444435724 scopus 로고    scopus 로고
    • Model cellulose films exposed to H. insolens glucoside hydrolase family 45 endo-cellulase-The effect of the carbohydrate-binding module
    • Eriksson J, Malmsten M, Tiberg F, Callisen TH, Damhus T, Johansen KS. 2005b. Model cellulose films exposed to H. insolens glucoside hydrolase family 45 endo-cellulase-The effect of the carbohydrate-binding module. J Colloid Interface Sci 285: 94-99.
    • (2005) J Colloid Interface Sci , vol.285 , pp. 94-99
    • Eriksson, J.1    Malmsten, M.2    Tiberg, F.3    Callisen, T.H.4    Damhus, T.5    Johansen, K.S.6
  • 45
    • 0002440729 scopus 로고
    • Localisation of degradative enzymes in white-rot decay of lignocellulose
    • Evans CS, Gallagher IM, Atkey PT, Wood DA. 1991. Localisation of degradative enzymes in white-rot decay of lignocellulose. Biodegradation 2: 93-106.
    • (1991) Biodegradation , vol.2 , pp. 93-106
    • Evans, C.S.1    Gallagher, I.M.2    Atkey, P.T.3    Wood, D.A.4
  • 46
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: Highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes CM, Gilbert HJ. 2010. Cellulosomes: Highly efficient nanomachines 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
  • 47
    • 84856839149 scopus 로고    scopus 로고
    • Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes
    • Fox JM, Levine SE, Clark DS, Blanch HW. 2012. Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes. Biochemistry 51: 442-452.
    • (2012) Biochemistry , vol.51 , pp. 442-452
    • Fox, J.M.1    Levine, S.E.2    Clark, D.S.3    Blanch, H.W.4
  • 48
    • 79960846411 scopus 로고    scopus 로고
    • Effect of gold nanoparticle morphology on adsorbed protein structure and function
    • Gagner JE, Lopez MD, Dordick JS, Siegel RW. 2011. Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials 32: 7241-7252.
    • (2011) Biomaterials , vol.32 , pp. 7241-7252
    • Gagner, J.E.1    Lopez, M.D.2    Dordick, J.S.3    Siegel, R.W.4
  • 49
    • 84871553240 scopus 로고    scopus 로고
    • Dissecting and reconstructing synergism: In situ visualization of cooperativity among cellulases
    • Ganner T, Bubner P, Eibinger M, Mayrhofer C, Plank H, Nidetzky B. 2012. Dissecting and reconstructing synergism: In situ visualization of cooperativity among cellulases. J Biol Chem 287: 43215-43222.
    • (2012) J Biol Chem , vol.287 , pp. 43215-43222
    • Ganner, T.1    Bubner, P.2    Eibinger, M.3    Mayrhofer, C.4    Plank, H.5    Nidetzky, B.6
  • 51
    • 0017717846 scopus 로고
    • Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: A new method, theory and application
    • Geoghegan WD, Ackerman GA. 1977. Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: A new method, theory and application. J Histochem Cytochem 25: 1187-1200.
    • (1977) J Histochem Cytochem , vol.25 , pp. 1187-1200
    • Geoghegan, W.D.1    Ackerman, G.A.2
  • 52
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes NR, Warren RA, Miller RC Jr, Kilburn DG. 1988. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J Biol Chem 263: 10401-10407.
    • (1988) J Biol Chem , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.A.2    Miller Jr., R.C.3    Kilburn, D.G.4
  • 53
    • 0027433120 scopus 로고
    • Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose
    • Gilkes NR, Kilburn DG, Miller RC Jr, Warren RA, Sugiyama J, Chanzy H, Henrissat B. 1993. Visualization of the adsorption of a bacterial endo-beta-1, 4-glucanase and its isolated cellulose-binding domain to crystalline cellulose. Int J Biol Macromol 15: 347-351.
    • (1993) Int J Biol Macromol , vol.15 , pp. 347-351
    • Gilkes, N.R.1    Kilburn, D.G.2    Miller Jr., R.C.3    Warren, R.A.4    Sugiyama, J.5    Chanzy, H.6    Henrissat, B.7
  • 54
  • 55
    • 79959492513 scopus 로고    scopus 로고
    • Agriculture: Beyond food versus fuel
    • Graham-Rowe D. 2011. Agriculture: Beyond food versus fuel. Nature 474(7352): S6-S8.
    • (2011) Nature , vol.474 , Issue.7352
    • Graham-Rowe, D.1
  • 56
    • 77953296073 scopus 로고    scopus 로고
    • Cellulose nanocrystals: Chemistry, self-assembly, and applications
    • Habibi Y, Lucia LA, Rojas OJ. 2010. Cellulose nanocrystals: Chemistry, self-assembly, and applications. Chem Rev 110: 3479-3500.
    • (2010) Chem Rev , vol.110 , pp. 3479-3500
    • Habibi, Y.1    Lucia, L.A.2    Rojas, O.J.3
  • 57
    • 77749315426 scopus 로고    scopus 로고
    • Cellulose crystallinity-A key predictor of the enzymatic hydrolysis rate
    • Hall M, Bansal P, Lee JH, Realff MJ, Bommarius AS. 2010. Cellulose crystallinity-A key predictor of the enzymatic hydrolysis rate. FEBS J 277: 1571-1582.
    • (2010) FEBS J , vol.277 , pp. 1571-1582
    • Hall, M.1    Bansal, P.2    Lee, J.H.3    Realff, M.J.4    Bommarius, A.S.5
  • 60
    • 0034155791 scopus 로고    scopus 로고
    • 13C-NMR study of cellulose structure in spruce wood and kraft pulp
    • 13C-NMR study of cellulose structure in spruce wood and kraft pulp. Cellulose 7: 35-55.
    • (2000) Cellulose , vol.7 , pp. 35-55
    • Hult, E.L.1    Larsson, P.T.2    Iversen, T.3
  • 61
    • 0037824657 scopus 로고    scopus 로고
    • Characterization of the supermolecular structure of cellulose in wood pulp fibres
    • Hult EL, Iversen T, Sugiyama J. 2003. Characterization of the supermolecular structure of cellulose in wood pulp fibres. Cellulose 10: 103-110.
    • (2003) Cellulose , vol.10 , pp. 103-110
    • Hult, E.L.1    Iversen, T.2    Sugiyama, J.3
  • 62
    • 0029337026 scopus 로고
    • Ultra-small gold particles and silver enhancement as a detection system in immunolabeling and in situ hybridization experiments
    • Humbel BM, Sibon OC, Stierhof YD, Schwarz H. 1995. Ultra-small gold particles and silver enhancement as a detection system in immunolabeling and in situ hybridization experiments. J Histochem Cytochem 43: 735-737.
    • (1995) J Histochem Cytochem , vol.43 , pp. 735-737
    • Humbel, B.M.1    Sibon, O.C.2    Stierhof, Y.D.3    Schwarz, H.4
  • 63
    • 33745194822 scopus 로고    scopus 로고
    • Surface density of cellobiohydrolase on crystalline celluloses. A critical parameter to evaluate enzymatic kinetics at a solid-liquid interface
    • Igarashi K, Wada M, Hori R, Samejima M. 2006. Surface density of cellobiohydrolase on crystalline celluloses. A critical parameter to evaluate enzymatic kinetics at a solid-liquid interface. FEBS J 273: 2869-2878.
    • (2006) FEBS J , vol.273 , pp. 2869-2878
    • Igarashi, K.1    Wada, M.2    Hori, R.3    Samejima, M.4
  • 64
    • 33947228342 scopus 로고    scopus 로고
    • Activation of crystalline cellulose to cellulose III(I) results in efficient hydrolysis by cellobiohydrolase
    • Igarashi K, Wada M, Samejima M. 2007. Activation of crystalline cellulose to cellulose III(I) results in efficient hydrolysis by cellobiohydrolase. FEBS J 274: 1785-1792.
    • (2007) FEBS J , vol.274 , pp. 1785-1792
    • Igarashi, K.1    Wada, M.2    Samejima, M.3
  • 65
    • 73649106924 scopus 로고    scopus 로고
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose
    • Igarashi K, Koivula A, Wada M, Kimura S, Penttilä M, Samejima M. 2009. High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose. J Biol Chem 284: 36186-36190.
    • (2009) J Biol Chem , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttilä, M.5    Samejima, M.6
  • 67
    • 0031666637 scopus 로고    scopus 로고
    • Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals
    • Imai T, Boisset C, Samejima M, Igarashi K, Sugiyama J. 1998. Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals. FEBS Lett 432: 113-116.
    • (1998) FEBS Lett , vol.432 , pp. 113-116
    • Imai, T.1    Boisset, C.2    Samejima, M.3    Igarashi, K.4    Sugiyama, J.5
  • 68
    • 0037369085 scopus 로고    scopus 로고
    • Geometric phase analysis of lattice images from algal cellulose microfibrils
    • Imai T, Putaux J-L, Sugiyama J. 2003. Geometric phase analysis of lattice images from algal cellulose microfibrils. Polymer 44: 1871-1879.
    • (2003) Polymer , vol.44 , pp. 1871-1879
    • Imai, T.1    Putaux, J.-L.2    Sugiyama, J.3
  • 70
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
    • Jalak J, Väljamäe P. 2010. Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis. Biotechnol Bioeng 106: 871-883.
    • (2010) Biotechnol Bioeng , vol.106 , pp. 871-883
    • Jalak, J.1    Väljamäe, P.2
  • 71
    • 84865224370 scopus 로고    scopus 로고
    • Endo-exo synergism in cellulose hydrolysis revisited
    • Jalak J, Kurashin M, Teugjas H, Väljamäe P. 2012. Endo-exo synergism in cellulose hydrolysis revisited. J Biol Chem 287: 28802-28815.
    • (2012) J Biol Chem , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurashin, M.2    Teugjas, H.3    Väljamäe, P.4
  • 72
    • 0642276039 scopus 로고    scopus 로고
    • Chemistry: Cellulose stacks up
    • Jarvis M. 2003. Chemistry: Cellulose stacks up. Nature 426: 611-612.
    • (2003) Nature , vol.426 , pp. 611-612
    • Jarvis, M.1
  • 73
    • 0030825785 scopus 로고    scopus 로고
    • Surface diffusion of cellulases and their isolated binding domains on cellulose
    • Jervis EJ, Haynes CA, Kilburn DG. 1997. Surface diffusion of cellulases and their isolated binding domains on cellulose. J Biol Chem 272: 24016-24023.
    • (1997) J Biol Chem , vol.272 , pp. 24016-24023
    • Jervis, E.J.1    Haynes, C.A.2    Kilburn, D.G.3
  • 74
    • 38849118325 scopus 로고    scopus 로고
    • The physical action of cellulases revealed by a quartz crystal microbalance study using ultra thin cellulose films and pure cellulases
    • Josefsson P, Henriksson G, Wågberg L. 2008. The physical action of cellulases revealed by a quartz crystal microbalance study using ultra thin cellulose films and pure cellulases. Biomacromolecules 9: 249-254.
    • (2008) Biomacromolecules , vol.9 , pp. 249-254
    • Josefsson, P.1    Henriksson, G.2    Wågberg, L.3
  • 75
    • 20444400628 scopus 로고    scopus 로고
    • Cellulose: Fascinating biopolymer and sustainable raw material
    • Klemm D, Heublein B, Fink HP, Bohn A. 2005. Cellulose: Fascinating biopolymer and sustainable raw material. Angew Chem Int Ed Engl 44: 3358-3393.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 3358-3393
    • Klemm, D.1    Heublein, B.2    Fink, H.P.3    Bohn, A.4
  • 78
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin V by high-speed atomic force microscopy
    • Kodera N, Yamamoto D, Ishikawa R, Ando T. 2010. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468: 72-76.
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 79
    • 0038447037 scopus 로고    scopus 로고
    • Cellulose model surfaces-simplified preparation by spin coating and characterization by X-ray photoelectron spectroscopy, infrared spectroscopy, and atomic force microscopy
    • Kontturi E, Thüne PC, Niemantsverdriet JWH. 2003. Cellulose model surfaces-simplified preparation by spin coating and characterization by X-ray photoelectron spectroscopy, infrared spectroscopy, and atomic force microscopy. Langmuir 19: 5735-5741.
    • (2003) Langmuir , vol.19 , pp. 5735-5741
    • Kontturi, E.1    Thüne, P.C.2    Niemantsverdriet, J.W.H.3
  • 81
    • 80955179036 scopus 로고    scopus 로고
    • Modified cellulose morphologies and its composites; SEM and TEM analysis
    • Krishnamachari P, Hashaikeh R, Tiner M. 2011. Modified cellulose morphologies and its composites; SEM and TEM analysis. Micron 42: 751-761.
    • (2011) Micron , vol.42 , pp. 751-761
    • Krishnamachari, P.1    Hashaikeh, R.2    Tiner, M.3
  • 82
    • 0030174789 scopus 로고    scopus 로고
    • Cellulase formation by species of Trichoderma sect. Longibrachiatum and of Hypocrea spp. with anamorphs referable to Trichoderma sect. Longibrachiatum
    • Kubicek CP, Bolzlbauer UM, Kovacs W, Mach RL, Kuhls K, Lieckfeldt E, Borner T, Samuels GJ. 1996. Cellulase formation by species of Trichoderma sect. Longibrachiatum and of Hypocrea spp. with anamorphs referable to Trichoderma sect. Longibrachiatum . Fungal Genet Biol 20: 105-114.
    • (1996) Fungal Genet Biol , vol.20 , pp. 105-114
    • Kubicek, C.P.1    Bolzlbauer, U.M.2    Kovacs, W.3    Mach, R.L.4    Kuhls, K.5    Lieckfeldt, E.6    Borner, T.7    Samuels, G.J.8
  • 83
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • Kurasin M, Väljamäe P. 2011. Processivity of cellobiohydrolases is limited by the substrate. J Biol Chem 286: 169-177.
    • (2011) J Biol Chem , vol.286 , pp. 169-177
    • Kurasin, M.1    Väljamäe, P.2
  • 84
    • 0343472018 scopus 로고    scopus 로고
    • A comparative structural characterization of two cellobiohydrolases from Trichoderma reesei: A high resolution electron microscopy study
    • Lee HJ, Brown MJ. 1997. A comparative structural characterization of two cellobiohydrolases from Trichoderma reesei: A high resolution electron microscopy study. J Biotechnol 57: 127-136.
    • (1997) J Biotechnol , vol.57 , pp. 127-136
    • Lee, H.J.1    Brown, M.J.2
  • 85
    • 0030294965 scopus 로고    scopus 로고
    • Substrate-enzyme interactions in cellulase systems
    • Lee I, Evans BR, Lane LM, Woodward J. 1996. Substrate-enzyme interactions in cellulase systems. Biores Technol 58: 163-169.
    • (1996) Biores Technol , vol.58 , pp. 163-169
    • Lee, I.1    Evans, B.R.2    Lane, L.M.3    Woodward, J.4
  • 86
    • 0033979485 scopus 로고    scopus 로고
    • The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy
    • Lee I, Evans BR, Woodward J. 2000. The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy. Ultramicroscopy 82: 213-221.
    • (2000) Ultramicroscopy , vol.82 , pp. 213-221
    • Lee, I.1    Evans, B.R.2    Woodward, J.3
  • 87
    • 63549131316 scopus 로고    scopus 로고
    • Ionic liquid-mediated selective extraction of lignin from wood leading to enhanced enzymatic cellulose hydrolysis
    • Lee SH, Doherty TV, Linhardt RJ, Dordick JS. 2009. Ionic liquid-mediated selective extraction of lignin from wood leading to enhanced enzymatic cellulose hydrolysis. Biotechnol Bioeng 102: 1368-1376.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1368-1376
    • Lee, S.H.1    Doherty, T.V.2    Linhardt, R.J.3    Dordick, J.S.4
  • 88
    • 77956043498 scopus 로고    scopus 로고
    • An expansin-like protein from Hahella chejuensis binds cellulose and enhances cellulase activity
    • Lee HJ, Lee S, Ko HJ, Kim KH, Choi IG. 2010. An expansin-like protein from Hahella chejuensis binds cellulose and enhances cellulase activity. Mol Cells 29: 379-385.
    • (2010) Mol Cells , vol.29 , pp. 379-385
    • Lee, H.J.1    Lee, S.2    Ko, H.J.3    Kim, K.H.4    Choi, I.G.5
  • 90
    • 80052925884 scopus 로고    scopus 로고
    • Review of super-resolution fluorescence microscopy for biology
    • 250A-272A
    • Leung BO, Chou KC. 2011. Review of super-resolution fluorescence microscopy for biology. Appl Spectrosc 65(250A-272A): 967-1086.
    • (2011) Appl Spectrosc , vol.65 , pp. 967-1086
    • Leung, B.O.1    Chou, K.C.2
  • 91
  • 93
    • 68349137937 scopus 로고    scopus 로고
    • Visualization of enzymatic hydrolysis of cellulose using AFM phase imaging
    • Liu H, Fu S, Zhu JY, Li H, Zhan H. 2009a. Visualization of enzymatic hydrolysis of cellulose using AFM phase imaging. Enzyme Microb Tech 45: 274-281.
    • (2009) Enzyme Microb Tech , vol.45 , pp. 274-281
    • Liu, H.1    Fu, S.2    Zhu, J.Y.3    Li, H.4    Zhan, H.5
  • 95
    • 77951698881 scopus 로고    scopus 로고
    • Single molecule study of cellulase hydrolysis of crystalline cellulose. Society of Photo-Optical Instrumentation Engineers (SPIE) Photonics West 2010. San Francisco, CA, USA.
    • Liu YS, Luo Y, Baker JO, Zeng Y, Himmel ME, Ding S-Y. 2010. Single molecule study of cellulase hydrolysis of crystalline cellulose. Society of Photo-Optical Instrumentation Engineers (SPIE) Photonics West 2010. San Francisco, CA, USA.
    • (2010)
    • Liu, Y.S.1    Luo, Y.2    Baker, J.O.3    Zeng, Y.4    Himmel, M.E.5    Ding, S.-Y.6
  • 96
    • 79953223700 scopus 로고    scopus 로고
    • Cellobiohydrolase hydrolyzes crystalline cellulose on hydrophobic faces
    • Liu YS, Baker JO, Zeng Y, Himmel ME, Haas T, Ding SY. 2011. Cellobiohydrolase hydrolyzes crystalline cellulose on hydrophobic faces. J Biol Chem 286: 11195-11201.
    • (2011) J Biol Chem , vol.286 , pp. 11195-11201
    • Liu, Y.S.1    Baker, J.O.2    Zeng, Y.3    Himmel, M.E.4    Haas, T.5    Ding, S.Y.6
  • 97
    • 84869890173 scopus 로고    scopus 로고
    • Observing and modeling BMCC degradation by commercial cellulase cocktails with fluorescently labeled Trichoderma reseii Cel7A through confocal microscopy
    • Luterbacher JS, Walker LP, Moran-Mirabal JM. 2013. Observing and modeling BMCC degradation by commercial cellulase cocktails with fluorescently labeled Trichoderma reseii Cel7A through confocal microscopy. Biotechnol Bioeng 110: 108-117.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 108-117
    • Luterbacher, J.S.1    Walker, L.P.2    Moran-Mirabal, J.M.3
  • 100
    • 0033199811 scopus 로고    scopus 로고
    • Substrate and enzyme characteristics that limit cellulose hydrolysis
    • Mansfield SD, Mooney C, Saddler JN. 1999. Substrate and enzyme characteristics that limit cellulose hydrolysis. Biotechnol Prog 15: 804-816.
    • (1999) Biotechnol Prog , vol.15 , pp. 804-816
    • Mansfield, S.D.1    Mooney, C.2    Saddler, J.N.3
  • 101
    • 56749087792 scopus 로고    scopus 로고
    • Immobilization of cellulose fibrils on solid substrates for cellulase-binding studies through quantitative fluorescence microscopy
    • Moran-Mirabal JM, Santhanam N, Corgie SC, Craighead HG, Walker LP. 2008. Immobilization of cellulose fibrils on solid substrates for cellulase-binding studies through quantitative fluorescence microscopy. Biotechnol Bioeng 101: 1129-1141.
    • (2008) Biotechnol Bioeng , vol.101 , pp. 1129-1141
    • Moran-Mirabal, J.M.1    Santhanam, N.2    Corgie, S.C.3    Craighead, H.G.4    Walker, L.P.5
  • 102
    • 79953115825 scopus 로고    scopus 로고
    • Reversibility and binding kinetics of Thermobifida fusca cellulases studied through fluorescence recovery after photobleaching microscopy
    • Moran-Mirabal JM, Bolewski JC, Walker LP. 2011. Reversibility and binding kinetics of Thermobifida fusca cellulases studied through fluorescence recovery after photobleaching microscopy. Biophys Chem 155: 20-28.
    • (2011) Biophys Chem , vol.155 , pp. 20-28
    • Moran-Mirabal, J.M.1    Bolewski, J.C.2    Walker, L.P.3
  • 103
    • 84869880474 scopus 로고    scopus 로고
    • Thermobifida fusca cellulases exhibit limited surface diffusion on bacterial micro-crystalline cellulose
    • Moran-Mirabal JM, Bolewski JC, Walker LP. 2013. Thermobifida fusca cellulases exhibit limited surface diffusion on bacterial micro-crystalline cellulose. Biotechnol Bioeng 110: 47-56.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 47-56
    • Moran-Mirabal, J.M.1    Bolewski, J.C.2    Walker, L.P.3
  • 104
    • 0028353231 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction
    • Nidetzky B, Steiner W, Hayn M, Claeyssens M. 1994. Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction. Biochem J 298: 705-710.
    • (1994) Biochem J , vol.298 , pp. 705-710
    • Nidetzky, B.1    Steiner, W.2    Hayn, M.3    Claeyssens, M.4
  • 105
    • 0026048693 scopus 로고
    • Visualization of Trichoderma reesei cellobiohydrolase I and endoglucanase I on aspen cellulose by using monoclonal antibody-colloidal gold conjugates
    • Nieves RA, Ellis RP, Todd RJ, Johnson TJ, Grohmann K, Himmel ME. 1991. Visualization of Trichoderma reesei cellobiohydrolase I and endoglucanase I on aspen cellulose by using monoclonal antibody-colloidal gold conjugates. Appl Environ Microbiol 57: 3163-3170.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 3163-3170
    • Nieves, R.A.1    Ellis, R.P.2    Todd, R.J.3    Johnson, T.J.4    Grohmann, K.5    Himmel, M.E.6
  • 108
    • 84862004181 scopus 로고    scopus 로고
    • Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose
    • Nimlos MR, Beckham GT, Matthews JF, Bu L, Himmel ME, Crowley MF. 2012. Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose. J Biol Chem 287: 20603-20612.
    • (2012) J Biol Chem , vol.287 , pp. 20603-20612
    • Nimlos, M.R.1    Beckham, G.T.2    Matthews, J.F.3    Bu, L.4    Himmel, M.E.5    Crowley, M.F.6
  • 110
    • 77952511855 scopus 로고    scopus 로고
    • Cellulose crystallinity index: Measurement techniques and their impact on interpreting cellulase performance
    • Park S, Baker JO, Himmel ME, Parilla PA, Johnson DK. 2010. Cellulose crystallinity index: Measurement techniques and their impact on interpreting cellulase performance. Biotechnol Biofuels 3: 10.
    • (2010) Biotechnol Biofuels , vol.3 , pp. 10
    • Park, S.1    Baker, J.O.2    Himmel, M.E.3    Parilla, P.A.4    Johnson, D.K.5
  • 112
    • 79959673483 scopus 로고    scopus 로고
    • Fully hydrated yeast cells imaged with electron microscopy
    • Peckys DB, Mazur P, Gould KL, de Jonge N. 2011. Fully hydrated yeast cells imaged with electron microscopy. Biophys J 100: 2522-2529.
    • (2011) Biophys J , vol.100 , pp. 2522-2529
    • Peckys, D.B.1    Mazur, P.2    Gould, K.L.3    de Jonge, N.4
  • 114
    • 33747131733 scopus 로고    scopus 로고
    • Large-scale production of cellulose-binding domains. Adsorption studies using CBD-FITC conjugates
    • Pinto R, Carvalho J, Mota M, Gama M. 2006. Large-scale production of cellulose-binding domains. Adsorption studies using CBD-FITC conjugates. Cellulose 13: 557-569.
    • (2006) Cellulose , vol.13 , pp. 557-569
    • Pinto, R.1    Carvalho, J.2    Mota, M.3    Gama, M.4
  • 116
    • 77950573367 scopus 로고    scopus 로고
    • Direct visualization of the enzymatic digestion of a single fiber of native cellulose in an aqueous environment by atomic force microscopy
    • Quirk A, Lipkowski J, Vandenende C, Cockburn D, Clarke AJ, Dutcher JR, Roscoe SG. 2010. Direct visualization of the enzymatic digestion of a single fiber of native cellulose in an aqueous environment by atomic force microscopy. Langmuir 26: 5007-5013.
    • (2010) Langmuir , vol.26 , pp. 5007-5013
    • Quirk, A.1    Lipkowski, J.2    Vandenende, C.3    Cockburn, D.4    Clarke, A.J.5    Dutcher, J.R.6    Roscoe, S.G.7
  • 118
    • 43149096709 scopus 로고    scopus 로고
    • High-precision structural analysis of subnuclear complexes in fixed and live cells via spatially modulated illumination (SMI) microscopy
    • Reymann J, Baddeley D, Gunkel M, Lemmer P, Stadter W, Jegou T, Rippe K, Cremer C, Birk U. 2008. High-precision structural analysis of subnuclear complexes in fixed and live cells via spatially modulated illumination (SMI) microscopy. Chromosome Res 16: 367-382.
    • (2008) Chromosome Res , vol.16 , pp. 367-382
    • Reymann, J.1    Baddeley, D.2    Gunkel, M.3    Lemmer, P.4    Stadter, W.5    Jegou, T.6    Rippe, K.7    Cremer, C.8    Birk, U.9
  • 119
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, Zhuang X. 2006. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Methods 3: 793-795.
    • (2006) Nat Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 120
    • 0036046037 scopus 로고    scopus 로고
    • Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials
    • Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, Nyyssonen E, Bhatia A, Ward M, Penttila M. 2002. Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem 269: 4202-4211.
    • (2002) Eur J Biochem , vol.269 , pp. 4202-4211
    • Saloheimo, M.1    Paloheimo, M.2    Hakola, S.3    Pere, J.4    Swanson, B.5    Nyyssonen, E.6    Bhatia, A.7    Ward, M.8    Penttila, M.9
  • 121
    • 79959500308 scopus 로고    scopus 로고
    • Visualization of bionanostructures using transmission electron microscopical techniques
    • Sander B, Golas MM. 2011. Visualization of bionanostructures using transmission electron microscopical techniques. Microsc Res Tech 74: 642-663.
    • (2011) Microsc Res Tech , vol.74 , pp. 642-663
    • Sander, B.1    Golas, M.M.2
  • 122
    • 77955576397 scopus 로고    scopus 로고
    • Molecular-scale investigations of cellulose microstructure during enzymatic hydrolysis
    • Santa-Maria M, Jeoh T. 2010. Molecular-scale investigations of cellulose microstructure during enzymatic hydrolysis. Biomacromolecules 11: 2000-2007.
    • (2010) Biomacromolecules , vol.11 , pp. 2000-2007
    • Santa-Maria, M.1    Jeoh, T.2
  • 125
    • 69249127947 scopus 로고    scopus 로고
    • Visualization of biomass solubilization and cellulose regeneration during ionic liquid pretreatment of switchgrass
    • Singh S, Simmons BA, Vogel C. 2009. Visualization of biomass solubilization and cellulose regeneration during ionic liquid pretreatment of switchgrass. Biotech Bioeng 104: 68-75.
    • (2009) Biotech Bioeng , vol.104 , pp. 68-75
    • Singh, S.1    Simmons, B.A.2    Vogel, C.3
  • 126
    • 34147111433 scopus 로고    scopus 로고
    • Grain and cellulosic ethanol: History, economics, and energy policy
    • Solomon BD, Barnes JR, Halvorsen KE. 2007. Grain and cellulosic ethanol: History, economics, and energy policy. Biomass Bioenergy 31: 416-425.
    • (2007) Biomass Bioenergy , vol.31 , pp. 416-425
    • Solomon, B.D.1    Barnes, J.R.2    Halvorsen, K.E.3
  • 128
    • 77955584535 scopus 로고    scopus 로고
    • Impact of drying on wood ultrastructure: Similarities in cell wall alteration between native wood and isolated wood-based fibers
    • Suchy M, Kontturi E, Vuorinen T. 2010. Impact of drying on wood ultrastructure: Similarities in cell wall alteration between native wood and isolated wood-based fibers. Biomacromolecules 11: 2161-2168.
    • (2010) Biomacromolecules , vol.11 , pp. 2161-2168
    • Suchy, M.1    Kontturi, E.2    Vuorinen, T.3
  • 129
    • 61549088811 scopus 로고    scopus 로고
    • Hydrolytic activity of free and immobilized cellulase
    • Tébéka IR, Silva AG, Petri DF. 2009. Hydrolytic activity of free and immobilized cellulase. Langmuir 25: 1582-1587.
    • (2009) Langmuir , vol.25 , pp. 1582-1587
    • Tébéka, I.R.1    Silva, A.G.2    Petri, D.F.3
  • 130
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis
    • Tomme P, Van Tilbeurgh H, Pettersson G, Van Damme J, Vandekerckhove J, Knowles J, Teeri T, Claeyssens M. 1988. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur J Biochem 170: 575-581.
    • (1988) Eur J Biochem , vol.170 , pp. 575-581
    • Tomme, P.1    Van Tilbeurgh, H.2    Pettersson, G.3    Van Damme, J.4    Vandekerckhove, J.5    Knowles, J.6    Teeri, T.7    Claeyssens, M.8
  • 131
    • 84865814021 scopus 로고    scopus 로고
    • Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy
    • Uchihashi T, Kodera N, Ando T. 2012. Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nat Protoc 7: 1193-1206.
    • (2012) Nat Protoc , vol.7 , pp. 1193-1206
    • Uchihashi, T.1    Kodera, N.2    Ando, T.3
  • 132
    • 0032522362 scopus 로고    scopus 로고
    • The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model
    • Väljamäe P, Sild V, Pettersson G, Johansson G. 1998. The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model. Eur J Biochem 253: 469-475.
    • (1998) Eur J Biochem , vol.253 , pp. 469-475
    • Väljamäe, P.1    Sild, V.2    Pettersson, G.3    Johansson, G.4
  • 134
    • 84862900169 scopus 로고    scopus 로고
    • Real-time observation of the swelling and hydrolysis of a single crystalline cellulose fiber catalyzed by cellulase 7B from Trichoderma reesei
    • Wang J, Quirk A, Lipkowski J, Dutcher JR, Hill C, Mark A, Clarke AJ. 2012a. Real-time observation of the swelling and hydrolysis of a single crystalline cellulose fiber catalyzed by cellulase 7B from Trichoderma reesei . Langmuir 28: 9664-9672.
    • (2012) Langmuir , vol.28 , pp. 9664-9672
    • Wang, J.1    Quirk, A.2    Lipkowski, J.3    Dutcher, J.R.4    Hill, C.5    Mark, A.6    Clarke, A.J.7
  • 135
    • 84863151462 scopus 로고    scopus 로고
    • Determination of cellulase colocalization on cellulose fiber with quantitative FRET measured by acceptor photobleaching and spectrally unmixing fluorescence microscopy
    • Wang L, Wang Y, Ragauskas AJ. 2012b. Determination of cellulase colocalization on cellulose fiber with quantitative FRET measured by acceptor photobleaching and spectrally unmixing fluorescence microscopy. Analyst 137: 1319-1324.
    • (2012) Analyst , vol.137 , pp. 1319-1324
    • Wang, L.1    Wang, Y.2    Ragauskas, A.J.3
  • 137
    • 19244378054 scopus 로고
    • Enzymatic hydrolysis of cellulose: Visual characterization of the process
    • White AR, Brown RM. 1981. Enzymatic hydrolysis of cellulose: Visual characterization of the process. Proc Natl Acad Sci USA 78: 1047-1051.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 1047-1051
    • White, A.R.1    Brown, R.M.2
  • 139
    • 84856246025 scopus 로고    scopus 로고
    • Processive and nonprocessive cellulases for biofuel production-Lessons from bacterial genomes and structural analysis
    • Wilson DB. 2012. Processive and nonprocessive cellulases for biofuel production-Lessons from bacterial genomes and structural analysis. Appl Microbiol Biotechnol 93: 497-502.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 497-502
    • Wilson, D.B.1
  • 140
    • 58149293278 scopus 로고    scopus 로고
    • Labeling the planar face of crystalline cellulose using quantum dots directed by type-I carbohydrate-binding modules
    • Xu Q, Tucker MP, Arenkiel P, Ai X, Rumbles G, Sugiyama J, Himmel ME, Ding S. 2009. Labeling the planar face of crystalline cellulose using quantum dots directed by type-I carbohydrate-binding modules. Cellulose 16: 19-26.
    • (2009) Cellulose , vol.16 , pp. 19-26
    • Xu, Q.1    Tucker, M.P.2    Arenkiel, P.3    Ai, X.4    Rumbles, G.5    Sugiyama, J.6    Himmel, M.E.7    Ding, S.8
  • 141
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • Zhang YH, Lynd LR. 2004. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems. Biotechnol Bioeng 88: 797-824.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 797-824
    • Zhang, Y.H.1    Lynd, L.R.2
  • 142
    • 0031799382 scopus 로고    scopus 로고
    • Reclassification of Thermomonospora and Microtetraspora
    • Zhang Z, Wang Y, Ruan J. 1998. Reclassification of Thermomonospora and Microtetraspora . Int J Syst Bacteriol 48: 411-422.
    • (1998) Int J Syst Bacteriol , vol.48 , pp. 411-422
    • Zhang, Z.1    Wang, Y.2    Ruan, J.3
  • 143
    • 78149249096 scopus 로고    scopus 로고
    • Cellulose hydrolysis in evolving substrate morphologies III: Time-scale analysis
    • Zhou W, Xu Y, Schüttler H-B. 2010. Cellulose hydrolysis in evolving substrate morphologies III: Time-scale analysis. Biotech Bioeng 107: 224-234.
    • (2010) Biotech Bioeng , vol.107 , pp. 224-234
    • Zhou, W.1    Xu, Y.2    Schüttler, H.-B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.