Fungal Cellulases

Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process

Philippidis, G. P., Smith, T. K., & Wyman, C. E. (1993) · Biotechnology and Bioengineering · doi:10.1002/bit.260410903 · Cited by 316

Crystal Structure and Binding Properties of the Serratia marcescens Chitin-binding Protein CBP21

Vaaje-Kolstad, G., Houston, D. R., Riemen, A. H. K., Eijsink, V. G. H., & van Aalten, D. M. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407175200 · Cited by 314

Process and technoeconomic analysis of leading pretreatment technologies for lignocellulosic ethanol production using switchgrass

Tao, L., Aden, A., Elander, R. T., Pallapolu, V. R., Lee, Y. Y., Garlock, R. J., Balan, V., Dale, B. E., Kim, Y., Mosier, N. S., et al. (2011) · Bioresource Technology · doi:10.1016/j.biortech.2011.07.051 · Cited by 314

Reactor design for minimizing product inhibition during enzymatic lignocellulose hydrolysis: I. Significance and mechanism of cellobiose and glucose inhibition on cellulolytic enzymes

Andrić, P., Meyer, A. S., Jensen, P. A., & Dam-Johansen, K. (2010) · Biotechnology Advances · doi:10.1016/j.biotechadv.2010.01.003 · Cited by 311

A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants

Henrissat, B., Teeri, T. T., & Warren, R. A. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00265-8 · Cited by 309

Effects of Crystallinity on Dilute Acid Hydrolysis of Cellulose by Cellulose Ball-Milling Study

Zhao, H., Kwak, J. H., Wang, Y., Franz, J. A., White, J. M., & Holladay, J. E. (2006) · Energy & Fuels · doi:10.1021/ef050319a · Cited by 309

The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins 1 1Edited by B. Honig

Elcock, A. H. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2159 · Cited by 308

Technoeconomic analysis of the dilute sulfuric acid and enzymatic hydrolysis process for the conversion of corn stover to ethanol

Aden, A., & Foust, T. (2009) · Cellulose · doi:10.1007/s10570-009-9327-8 · Cited by 306

EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme

Saloheimo, M., Lehtovaara, P., Penttilä, M., Teeri, T. T., Ståhlberg, J., Johansson, G., Pettersson, G., Claeyssens, M., Tomme, P., & Knowles, J. K. C. (1988) · Gene · doi:10.1016/0378-1119(88)90541-0 · Cited by 304

The Mechanism of Enzymatic Cellulose Degradation

BERGHEM, L. E. R., & Pettersson, L. G. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02952.x · Cited by 303

Cellulose IIII Crystal Structure and Hydrogen Bonding by Synchrotron X-ray and Neutron Fiber Diffraction

Wada, M., Chanzy, H., Nishiyama, Y., & Langan, P. (2004) · Macromolecules · doi:10.1021/ma0485585 · Cited by 303

Nomenclature for members of the expansin superfamily of genes and proteins

Kende, H., Bradford, K., Brummell, D., Cho, H.-T., Cosgrove, D., Fleming, A., Gehring, C., Lee, Y., Mcqueen-mason, S., Rose, J., et al. (2004) · Plant Molecular Biology · doi:10.1007/s11103-004-0158-6 · Cited by 300

Comparative sugar recovery and fermentation data following pretreatment of poplar wood by leading technologies

Wyman, C. E., Dale, B. E., Elander, R. T., Holtzapple, M., Ladisch, M. R., Lee, Y. Y., Mitchinson, C., & Saddler, J. N. (2009) · Biotechnology Progress · doi:10.1002/btpr.142 · Cited by 299

Metabolic engineering for advanced biofuels production from Escherichia coli

Atsumi, S., & Liao, J. C. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.08.008 · Cited by 297

Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site.

Törrönen, A., Harkki, A., & Rouvinen, J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06536.x · Cited by 292

Non–Hydrolytic Disruption of Cellulose Fibres by the Binding Domain of a Bacterial Cellulase

Din, N., Gilkes, N. R., Tekant, B., Miller, R. C., Warren, R. A. J., & Kilburn, D. G. (1991) · Bio/Technology · doi:10.1038/nbt1191-1096 · Cited by 289

Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases

Forsberg, Z., Mackenzie, A. K., Sørlie, M., Røhr, Å. K., Helland, R., Arvai, A. S., Vaaje-Kolstad, G., & Eijsink, V. G. H. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402771111 · Cited by 289

Induction of cellulolytic enzymes in Trichoderma reesei by sophorose

Sternberg, D., & Mandels, G. R. (1979) · Journal of Bacteriology · doi:10.1128/jb.139.3.761-769.1979 · Cited by 288

Expansins: ever-expanding numbers and functions

Lee, Y., Choi, D., & Kende, H. (2001) · Current Opinion in Plant Biology · doi:10.1016/s1369-5266(00)00211-9 · Cited by 288

Structural Basis for Substrate Targeting and Catalysis by Fungal Polysaccharide Monooxygenases

Li, X., Beeson, W. T., Phillips, C. M., Marletta, M. A., & Cate, J. H. D. (2012) · Structure · doi:10.1016/j.str.2012.04.002 · Cited by 287

Preparation of mutants of Trichoderma reesei with enhanced cellulase production

Montenecourt, B. S., & Eveleigh, D. E. (1977) · Applied and Environmental Microbiology · doi:10.1128/aem.34.6.777-782.1977 · Cited by 284

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) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034611 · Cited by 284

Identification of Two Functionally Different Classes of Exocellulases

Barr, B. K., Hsieh, Y.-L., Ganem, B., & Wilson, D. B. (1996) · Biochemistry · doi:10.1021/bi9520388 · Cited by 281

NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions

Aachmann, F. L., Sørlie, M., Skjåk-Bræk, G., Eijsink, V. G. H., & Vaaje-Kolstad, G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208822109 · Cited by 280

Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides

Horn, S. J., Sikorski, P., Cederkvist, J. B., Vaaje-Kolstad, G., Sørlie, M., Synstad, B., Vriend, G., Vårum, K. M., & Eijsink, V. G. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608909103 · Cited by 277

Revealing Nature’s Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA

Brunecky, R., Alahuhta, M., Xu, Q., Donohoe, B. S., Crowley, M. F., Kataeva, I. A., Yang, S.-J., Resch, M. G., Adams, M. W. W., Lunin, V. V., et al. (2013) · Science · doi:10.1126/science.1244273 · Cited by 276

Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate

Gruno, M., Väljamäe, P., Pettersson, G., & Johansson, G. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.10838 · Cited by 276

A family of starch-active polysaccharide monooxygenases

Vu, V. V., Beeson, W. T., Span, E. A., Farquhar, E. R., & Marletta, M. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408090111 · Cited by 275

Processivity of Cellobiohydrolases Is Limited by the Substrate

Kurašin, M., & Väljamäe, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.161059 · Cited by 274

Spontaneous Hydrolysis of Glycosides

Wolfenden, R., Lu, X., & Young, G. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9813055 · Cited by 274

Determination of the Number-Average Degree of Polymerization of Cellodextrins and Cellulose with Application to Enzymatic Hydrolysis

Zhang, Y.-H. P., & Lynd, L. R. (2005) · Biomacromolecules · doi:10.1021/bm049235j · Cited by 273

BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis

Omadjela, O., Narahari, A., Strumillo, J., Mélida, H., Mazur, O., Bulone, V., & Zimmer, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314063110 · Cited by 273

Role of Swollenin, an Expansin-Like Protein from Trichoderma, in Plant Root Colonization

Brotman, Y., Briff, E., Viterbo, A., & Chet, I. (2008) · Plant Physiology · doi:10.1104/pp.108.116293 · Cited by 267

A family of thermostable fungal cellulases created by structure-guided recombination

Heinzelman, P., Snow, C. D., Wu, I., Nguyen, C., Villalobos, A., Govindarajan, S., Minshull, J., & Arnold, F. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901417106 · Cited by 267

Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-Å resolution

van Aalten, D. M. F., Synstad, B., Brurberg, M. B., Hough, E., Riise, B. W., Eijsink, V. G. H., & Wierenga, R. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.5842 · Cited by 265

β‐Glucosidase, β‐galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8‐fold β/α architecture and with two conserved glutamates near the carboxy‐terminal ends of β‐strands four and seven

Jenkins, J., Lo Leggio, L., Harris, G., & Pickersgill, R. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00252-5 · Cited by 264

Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides.

Fischer, W. H., & Spiess, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3628 · Cited by 261

Theozymes and compuzymes: theoretical models for biological catalysis

Tantillo, D. J., Jiangang, C., & Houk, K. N. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80112-9 · Cited by 261

Cell Wall Loosening by Expansins

Cosgrove, D. J. (1998) · Plant Physiology · doi:10.1104/pp.118.2.333 · Cited by 260

Fungal Beta-Glucosidases: A Bottleneck in Industrial Use of Lignocellulosic Materials

Sørensen, A., Lübeck, M., Lübeck, P., & Ahring, B. (2013) · Biomolecules · doi:10.3390/biom3030612 · Cited by 259

The cellulase of Trichoderma viride: Purification, characterization and comparison of all detectable endoglucanases, exoglucanases and β‐glucosidases

BELDMAN, G., SEARLE‐VAN LEEUWEN, M. F., ROMBOUTS, F. M., & VORAGEN, F. G. J. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb08653.x · Cited by 255

Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: an overview, an experimental study and mathematical modelling

Gan, Q., Allen, S. J., & Taylor, G. (2003) · Process Biochemistry · doi:10.1016/s0032-9592(02)00220-0 · Cited by 254

Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize

Yennawar, N. H., Li, L.-C., Dudzinski, D. M., Tabuchi, A., & Cosgrove, D. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605979103 · Cited by 254

Reduced inhibition of enzymatic hydrolysis of steam-pretreated softwood

Tengborg, C., Galbe, M., & Zacchi, G. (2001) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(01)00342-8 · Cited by 254

The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 Å resolution, and a comparison with related enzymes 1 1Edited by K.Nagai

Kleywegt, G. J., Zou, J.-Y., Divne, C., Davies, G. J., Sinning, I., Ståhlberg, J., Reinikainen, T., Srisodsuk, M., Teeri, T. T., & Jones, T. A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1243 · Cited by 253

A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidase

Podell, D. N., & Abraham, G. N. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91646-7 · Cited by 252

Oxygen Activation by the Noncoupled Binuclear Copper Site in Peptidylglycine α-Hydroxylating Monooxygenase. Reaction Mechanism and Role of the Noncoupled Nature of the Active Site

Chen, P., & Solomon, E. I. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031564g · Cited by 251

Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content

Cannella, D., Hsieh, C.-W. C., Felby, C., & Jørgensen, H. (2012) · Biotechnology for Biofuels · doi:10.1186/1754-6834-5-26 · Cited by 250

Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II fromTrichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes

Medve, J., Karlsson, J., Lee, D., & Tjerneld, F. (1998) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19980905)59:5<621::aid-bit13>3.0.co;2-c · Cited by 249

Selective Screening Methods for the Isolation of High Yielding Cellulase Mutants of Trichoderma reesei

MONTENECOURT, B. S., & EVELEIGH, D. E. (1979) · Advances in Chemistry · doi:10.1021/ba-1979-0181.ch014 · Cited by 248

Comparative Transcriptome and Secretome Analysis of Wood Decay Fungi Postia placenta and Phanerochaete chrysosporium

Vanden Wymelenberg, A., Gaskell, J., Mozuch, M., Sabat, G., Ralph, J., Skyba, O., Mansfield, S. D., Blanchette, R. A., Martinez, D., Grigoriev, I., et al. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00058-10 · Cited by 247

Crystal Structure of Thermostable Family 5 Endocellulase E1 from Acidothermus cellulolyticus in Complex with Cellotetraose,

Sakon, J., Adney, W. S., Himmel, M. E., Thomas, S. R., & Karplus, P. A. (1996) · Biochemistry · doi:10.1021/bi9604439 · Cited by 245

Conformational Analyses of the Reaction Coordinate of Glycosidases

Davies, G. J., Planas, A., & Rovira, C. (2012) · Accounts of Chemical Research · doi:10.1021/ar2001765 · Cited by 244

Wide-Angle X-Ray Scattering and Solid-State Nuclear Magnetic Resonance Data Combined to Test Models for Cellulose Microfibrils in Mung Bean Cell Walls

Newman, R. H., Hill, S., & Harris, P. J. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.228262 · Cited by 243

A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang, Y. ‐. P., & Lynd, L. R. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20906 · Cited by 241

Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D

Strynadka, N. C. J., & James, M. N. G. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90021-w · Cited by 236

Sensitivity-enhanced solid-state NMR detection of expansin’s target in plant cell walls

Wang, T., Park, Y. B., Caporini, M. A., Rosay, M., Zhong, L., Cosgrove, D. J., & Hong, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316290110 · Cited by 234

Structure of the Fusarium oxysporum Endoglucanase I with a Nonhydrolyzable Substrate Analogue: Substrate Distortion Gives Rise to the Preferred Axial Orientation for the Leaving Group,

Sulzenbacher, G., Driguez, H., Henrissat, B., Schülein, M., & Davies, G. J. (1996) · Biochemistry · doi:10.1021/bi961946h · Cited by 233

Enzymatic properties of cellulases from Humicola insolens

Schülein, M. (1997) · Journal of Biotechnology · doi:10.1016/s0168-1656(97)00090-4 · Cited by 230

Endo-exo Synergism in Cellulose Hydrolysis Revisited

Jalak, J., Kurašin, M., Teugjas, H., & Väljamäe, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.381624 · Cited by 225

A Model Explaining Declining Rate in Hydrolysis of Lignocellulose Substrates with Cellobiohydrolase I (Cel7A) and Endoglucanase I (Cel7B) of Trichoderma reesei

Eriksson, T., Karlsson, J., & Tjerneld, F. (2002) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:101:1:41 · Cited by 224

The purification and properties of the C1 component of Trichoderma koningii cellulase

Wood, T. M., & McCrae, S. I. (1972) · Biochemical Journal · doi:10.1042/bj1281183 · Cited by 220

The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B from Hypocrea jecorina, at 1.6 Å Resolution

Karkehabadi, S., Hansson, H., Kim, S., Piens, K., Mitchinson, C., & Sandgren, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.016 · Cited by 216

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) · Applied and Environmental Microbiology · doi:10.1128/aem.66.4.1444-1452.2000 · Cited by 216

Molecular-Level Origins of Biomass Recalcitrance: Decrystallization Free Energies for Four Common Cellulose Polymorphs

Beckham, G. T., Matthews, J. F., Peters, B., Bomble, Y. J., Himmel, M. E., & Crowley, M. F. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp1106394 · Cited by 216

The Conformational Free Energy Landscape of β-d-Glucopyranose. Implications for Substrate Preactivation in β-Glucoside Hydrolases

Biarnés, X., Ardèvol, A., Planas, A., Rovira, C., Laio, A., & Parrinello, M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068411o · Cited by 215

Stereoselective hydrolysis catalyzed by related beta-1,4-glucanases and beta-1,4-xylanases.

Gebler, J., Gilkes, N. R., Claeyssens, M., Wilson, D. B., Béguin, P., Wakarchuk, W. W., Kilburn, D. G., Miller, R. C., Warren, R. A., & Withers, S. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42313-7 · Cited by 213

Genome analyses highlight the different biological roles of cellulases

Medie, F. M., Davies, G. J., Drancourt, M., & Henrissat, B. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2729 · Cited by 213

Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization

Kerff, F., Amoroso, A., Herman, R., Sauvage, E., Petrella, S., Filée, P., Charlier, P., Joris, B., Tabuchi, A., Nikolaidis, N., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809382105 · Cited by 210

Homology among (βα) 8 barrels: implications for the evolution of metabolic pathways 1 1Edited by G. Von Heijne

Copley, R. R., & Bork, P. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4152 · Cited by 207

Do new cellulolytic enzyme preparations affect the industrial strategies for high solids lignocellulosic ethanol production?

Cannella, D., & Jørgensen, H. (2014) · Biotechnology and Bioengineering · doi:10.1002/bit.25098 · Cited by 207

Über den Bau des krystallisierten Anteils der Cellulose

Meyer, K. H., & Mark, H. (1928) · Berichte der deutschen chemischen Gesellschaft (A and B Series) · doi:10.1002/cber.19280610402 · Cited by 206

Crystal structure of the catalytic domain of a thermophilic endocellulase

Spezio, M., Wilson, D. B., & Karplus, P. A. (1993) · Biochemistry · doi:10.1021/bi00089a006 · Cited by 206

FT-IR Microscopic Analysis of Changing Cellulose Crystalline Structure during Wood Cell Wall Formation

Kataoka, Y., & Kondo, T. (1998) · Macromolecules · doi:10.1021/ma970768c · Cited by 206

Tracking the roots of cellulase hyperproduction by the fungus Trichoderma reesei using massively parallel DNA sequencing

Le Crom, S., Schackwitz, W., Pennacchio, L., Magnuson, J. K., Culley, D. E., Collett, J. R., Martin, J., Druzhinina, I. S., Mathis, H., Monot, F., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905848106 · Cited by 206

Protein glycosylation pathways in filamentous fungi

Deshpande, N., Wilkins, M. R., Packer, N., & Nevalainen, H. (2008) · Glycobiology · doi:10.1093/glycob/cwn044 · Cited by 206

Two Cellobiohydrolase-Encoding Genes from Aspergillus niger Require d -Xylose and the Xylanolytic Transcriptional Activator XlnR for Their Expression

Gielkens, M. M. C., Dekkers, E., Visser, J., & de Graaff, L. H. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.10.4340-4345.1999 · Cited by 205

Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose.

Srisodsuk, M., Reinikainen, T., Penttilä, M., & Teeri, T. T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36847-4 · Cited by 202

New genes and new biological roles for expansins

Cosgrove, D. J. (2000) · Current Opinion in Plant Biology · doi:10.1016/s1369-5266(99)00039-4 · Cited by 201

New Method for Determining the Degree of Cellulose I Crystallinity by Means of FT Raman Spectroscopy

Schenzel, K., Fischer, S., & Brendler, E. (2005) · Cellulose · doi:10.1007/s10570-004-3885-6 · Cited by 201

Genetic Modification of Carbon Catabolite Repression in Trichoderma reesei for Improved Protein Production

Nakari-Setälä, T., Paloheimo, M., Kallio, J., Vehmaanperä, J., Penttilä, M., & Saloheimo, M. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.00282-09 · Cited by 201

Recent insights into copper-containing lytic polysaccharide mono-oxygenases

Hemsworth, G. R., Davies, G. J., & Walton, P. H. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.05.006 · Cited by 200

Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis

Irwin, D., Shin, D.-H., Zhang, S., Barr, B. K., Sakon, J., Karplus, P. A., & Wilson, D. B. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.7.1709-1714.1998 · Cited by 200

Isolation of the ace1 Gene Encoding a Cys2-His2 Transcription Factor Involved in Regulation of Activity of the Cellulase Promoter cbh1of Trichoderma reesei

Saloheimo, A., Aro, N., Ilmén, M., & Penttilä, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5817 · Cited by 199

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Kiiskinen, L.-L., Kruus, K., Bailey, M., Ylösmäki, E., Siika-aho, M., & Saloheimo, M. (2004) · Microbiology · doi:10.1099/mic.0.27147-0 · Cited by 199

The Copper Active Site of CBM33 Polysaccharide Oxygenases

Hemsworth, G. R., Taylor, E. J., Kim, R. Q., Gregory, R. C., Lewis, S. J., Turkenburg, J. P., Parkin, A., Davies, G. J., & Walton, P. H. (2013) · Journal of the American Chemical Society · doi:10.1021/ja402106e · Cited by 198

Extensions to the likelihood maximization approach for finding reaction coordinates

Peters, B., Beckham, G. T., & Trout, B. L. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2748396 · Cited by 198

The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose.

Linder, M., & Teeri, T. T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12251 · Cited by 197

Degrees of Difficulty of Water-Consuming Reactions in the Absence of Enzymes

Wolfenden, R. (2006) · Chemical Reviews · doi:10.1021/cr050311y · Cited by 197

Investigation of the function of mutated cellulose‐binding domains of Trichoderma reesei cellobiohydrolase I

Reinikainen, T., Ruohonen, L., Nevanen, T., Laaksonen, L., Kraulis, P., Jones, T. A., Knowles, J. K. C., & Teeri, T. T. (1992) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340140408 · Cited by 195

Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions

GOTO, M. (2007) · Bioscience, Biotechnology, and Biochemistry · doi:10.1271/bbb.70080 · Cited by 192

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Bey, M., Zhou, S., Poidevin, L., Henrissat, B., Coutinho, P. M., Berrin, J.-G., & Sigoillot, J.-C. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.02942-12 · Cited by 192

Properties of cellulolytic enzyme systems

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Molecular Cloning and Expression of the Novel Fungal -Glucosidase Genes from Humicola grisea and Trichoderma reesei

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Harnessing glycosylation to improve cellulase activity

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Microfibril diameter in celery collenchyma cellulose: X-ray scattering and NMR evidence

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Cloning, expression, and characterization of novel thermostable family 7 cellobiohydrolases

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Comparison of Cellulose Iβ Simulations with Three Carbohydrate Force Fields

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Lignin boosts the cellulase performance of a GH-61 enzyme from Sporotrichum thermophile

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Cellulase EGZ of Erwinia chrysanthemi : structural organization and importance of His98 and Glu133 residues for catalysis

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Characterization and engineering of a plastic-degrading aromatic polyesterase

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Applications of Microbial Enzymes in Food Industry

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Lignocellulose degradation mechanisms across the Tree of Life

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Lignocellulose degradation: An overview of fungi and fungal enzymes involved in lignocellulose degradation

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Expanding plastics recycling technologies: chemical aspects, technology status and challenges

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