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10.1146/annurev-chembioeng-061010-114205
10.1146/annurev-chembioeng-061010-114205
Outlook for cellulase improvement: screening and selection strategies
10.1016/j.biotechadv.2006.03.003 · 2006
10.1016/s0167-7799(97)01032-9
10.1016/s0167-7799(97)01032-9
10.1002/bit.20282
10.1002/bit.20282
Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
10.1021/bi00444a016 · 1989
10.1126/science.2377893
10.1126/science.2377893
10.1126/science.8036495
10.1126/science.8036495
High-resolution crystal structures reveal how a cellulose chain is bound in the 50Å long tunnel of cellobiohydrolase I from Trichoderma reesei
10.1006/jmbi.1997.1437 · 1998
The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose
10.1073/pnas.93.22.12251 · 1996
The binding specificity and affinity determinants of family 1 and family 3 cellulose binding modules
10.1073/pnas.212651999 · 2003
10.1074/jbc.m110.216556
10.1074/jbc.m110.216556
10.1074/jbc.m112.381624
10.1074/jbc.m112.381624
10.1074/jbc.m110.161059
10.1074/jbc.m110.161059
10.1074/jbc.m111.334946
10.1074/jbc.m111.334946
10.1021/ja012659q
10.1021/ja012659q
10.1093/nar/gkn663
10.1093/nar/gkn663
Modified glycosylation of cellobiohydrolase I from a high cellulase-producing mutant strain of Trichoderma reesei
10.1046/j.1432-1327.1998.2560119.x · 1998
The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven
10.1042/bj20041473 · 2005
Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretional changes of the O- and N-glycosylation pattern of Cel7A
10.1093/glycob/cwh080 · 2004
Factors influencing glycosylation of Trichoderma reesei cellulases. II: N-glycosylation of Cel7A core protein isolated from different strains
10.1093/glycob/cwh081 · 2004
10.1093/glycob/cwf089
10.1093/glycob/cwf089
Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding
10.1021/bi9903998 · 1999
10.1016/s0969-2126(03)00124-2
10.1016/s0969-2126(03)00124-2
10.1111/j.1742-4658.2005.04625.x
10.1111/j.1742-4658.2005.04625.x
10.1074/jbc.270.9.4383
10.1074/jbc.270.9.4383
The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution
10.1016/0014-5793(95)00961-8 · 1995
10.1002/pro.5560040604
10.1002/pro.5560040604
10.1074/jbc.m109.034611
10.1074/jbc.m109.034611
10.1074/jbc.m112.358184
10.1074/jbc.m112.358184
10.1021/jp908810a
10.1021/jp908810a
10.1016/j.bpj.2010.10.032
10.1016/j.bpj.2010.10.032
10.1016/s0014-5793(98)00596-1
10.1016/s0014-5793(98)00596-1
10.1074/jbc.m111.297713
10.1074/jbc.m111.297713
Structure of the catalytic core module of the Chaetomium thermophilum family GH6 cellobiohydrolase Cel6A
2012
10.1016/s0022-2836(03)00881-7
10.1016/s0022-2836(03)00881-7
10.1074/jbc.m112.365510
10.1074/jbc.m112.365510
10.1021/jp1106394
10.1021/jp1106394
10.1074/jbc.m110.212076
10.1074/jbc.m110.212076
10.1002/bit.10838
10.1002/bit.10838
Applications of computational science for understanding enzymatic deconstruction of cellulose
10.1016/j.copbio.2010.11.005 · 2011
10.1002/bit.22388
10.1002/bit.22388 · doi-reference
10.1016/s0969-2126(99)80171-3
10.1016/s0969-2126(99)80171-3 · doi-reference
The kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model
10.1046/j.1432-1327.1998.2530469.x · doi-reference
10.1126/science.1208386
10.1126/science.1208386 · doi-reference
10.1002/bit.22779
10.1002/bit.22779 · doi-reference
A model explaining declining rate in hydrolysis of lignocelluloses substrates with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) of Trichoderma reesei
10.1385/abab:101:1:41 · doi-reference
Cellulose hydrolysis in evolving substrate morphologies III: time-scale analysis
10.1002/bit.22814 · doi-reference
10.1002/bit.22389
10.1002/bit.22389 · doi-reference
A mechanistic model of the enzymatic hydrolysis of cellulose
10.1002/bit.22789 · doi-reference
Modeling cellulose kinetics on lignocellulosic materials
10.1016/j.biotechadv.2009.06.005 · doi-reference