scholarly article | Q13442814 |
P2093 | author name string | Shujun Zhang | |
Yefei Wang | |||
Lishan Yao | |||
Xiangfei Song | |||
P2860 | cites work | Microbial cellulose utilization: fundamentals and biotechnology | Q24533239 |
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PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa Predictions | Q57129760 | ||
Comparison of simple potential functions for simulating liquid water | Q26778447 | ||
Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens | Q27641622 | ||
Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D | Q27642386 | ||
Hallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens Chitinases | Q27672373 | ||
The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies | Q27687984 | ||
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes | Q27745581 | ||
High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei | Q27748854 | ||
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation | Q27860944 | ||
GROMACS: fast, flexible, and free | Q27860998 | ||
Comparison of multiple Amber force fields and development of improved protein backbone parameters | Q27861040 | ||
Origin of initial burst in activity for Trichoderma reesei endo-glucanases hydrolyzing insoluble cellulose | Q28732856 | ||
Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations | Q29615143 | ||
Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation | Q30407674 | ||
Product binding varies dramatically between processive and nonprocessive cellulase enzymes | Q30418292 | ||
On the interpretation of biochemical data by molecular dynamics computer simulation | Q30974251 | ||
High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose | Q33512667 | ||
Protein thermostability calculations using alchemical free energy simulations | Q33581606 | ||
Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A. | Q33863559 | ||
A structural basis for processivity | Q34342069 | ||
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Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. | Q35722100 | ||
Automated docking to explore subsite binding by glycoside hydrolase family 6 cellobiohydrolases and endoglucanases. | Q38298833 | ||
Glycoside hydrolase processivity is directly related to oligosaccharide binding free energy | Q38310852 | ||
Site-directed mutation of noncatalytic residues of Thermobifida fusca exocellulase Cel6B. | Q38312014 | ||
Hypocrea jecorina (Trichoderma reesei) Cel7A as a molecular machine: A docking study. | Q38323950 | ||
Fungal cellulase systems. Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei | Q38343901 | ||
Free energy via molecular simulation: applications to chemical and biomolecular systems | Q38648060 | ||
The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose | Q40600573 | ||
Processivity of cellobiohydrolases is limited by the substrate. | Q41556498 | ||
Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B. | Q41823402 | ||
Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency | Q41906475 | ||
Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I. | Q42664158 | ||
Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes. | Q46116039 | ||
A mechanistic model of the enzymatic hydrolysis of cellulose | Q46199858 | ||
The challenge of enzyme cost in the production of lignocellulosic biofuels | Q46621810 | ||
Force calculations in automated docking: enzyme-substrate interactions in Fusarium oxysporum Cel7B. | Q46683365 | ||
Binding site dynamics and aromatic-carbohydrate interactions in processive and non-processive family 7 glycoside hydrolases | Q46840842 | ||
Trichoderma reesei cellobiohydrolases: why so efficient on crystalline cellulose? | Q47898388 | ||
P433 | issue | 9 | |
P921 | main subject | cellulose | Q80294 |
P304 | page(s) | 1873-1880 | |
P577 | publication date | 2016-03-15 | |
P1433 | published in | Biotechnology and Bioengineering | Q4915339 |
P1476 | title | Cellulose chain binding free energy drives the processive move of cellulases on the cellulose surface. | |
P478 | volume | 113 |
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