about
Microbial enzymes: tools for biotechnological processesHeterologous expression of plant cell wall degrading enzymes for effective production of cellulosic biofuelsPrecise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic WavesInsights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass componentsStructural Basis for Substrate Targeting and Catalysis by Fungal Polysaccharide MonooxygenasesCellulolytic enzyme expression and simultaneous conversion of lignocellulosic sugars into ethanol and xylitol by a new Candida tropicalis strainEffect of highly branched hyphal morphology on the enhanced production of cellulase in Trichoderma reesei DES-15Production of a high-efficiency cellulase complex via β-glucosidase engineering in Penicillium oxalicumCellulose degradation: a therapeutic strategy in the improved treatment of Acanthamoeba infectionsIsolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic libraryCellulose degradation by Sulfolobus solfataricus requires a cell-anchored endo-β-1-4-glucanaseImproved thermostability of Clostridium thermocellum endoglucanase Cel8A by using consensus-guided mutagenesisA versatile toolkit for high throughput functional genomics with Trichoderma reeseiA cellular automaton model of crystalline cellulose hydrolysis by cellulasesEffects of NIPAm polymer additives on the enzymatic hydrolysis of Avicel and pretreated Miscanthus.Single-molecule imaging analysis of elementary reaction steps of Trichoderma reesei cellobiohydrolase I (Cel7A) hydrolyzing crystalline cellulose Iα and IIIIEngineering microbial surfaces to degrade lignocellulosic biomass.High throughput screening of fungal endoglucanase activity in Escherichia coliReal-time detection of the morphological change in cellulose by a nanomechanical sensorExpression and characterization of a novel metagenome-derived cellulase Exo2b and its application to improve cellulase activity in Trichoderma reesei.Hypocrea jecorina CEL6A protein engineering.Inhibition of cellulase-catalyzed lignocellulosic hydrolysis by iron and oxidative metal ions and complexes.Biased clique shuffling reveals stabilizing mutations in cellulase Cel7A.The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered proteinSupplementing with non-glycoside hydrolase proteins enhances enzymatic deconstruction of plant biomassChallenges and advances in the heterologous expression of cellulolytic enzymes: a reviewTargets of light signalling in Trichoderma reesei.Assembly of minicellulosomes on the surface of Bacillus subtilis.Comparative performance of precommercial cellulases hydrolyzing pretreated corn stoverStructure and stability of metagenome-derived glycoside hydrolase family 12 cellulase (LC-CelA) a homolog of Cel12A from Rhodothermus marinus.Cellulases from thermophilic fungi: recent insights and biotechnological potential.Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module.The impact of chromatin remodelling on cellulase expression in Trichoderma reesei.A homologous production system for Trichoderma reesei secreted proteins in a cellulase-free backgroundA Novel GH7 Endo-β-1,4-Glucanase from Neosartorya fischeri P1 with Good Thermostability, Broad Substrate Specificity and Potential Application in the Brewing IndustryDevelopment of cellobiose-degrading ability in Yarrowia lipolytica strain by overexpression of endogenous genesBinding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose.Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallographyChimeric cellulase matrix for investigating intramolecular synergism between non-hydrolytic disruptive functions of carbohydrate-binding modules and catalytic hydrolysis.Subsite-specific contributions of different aromatic residues in the active site architecture of glycoside hydrolase family 12.
P2860
Q26827731-9B16BB49-279B-4898-8E20-A75618991E80Q27003232-B8D653EE-CEE4-4B8A-A0A0-73B8287D470FQ27330322-1C4D76FB-977B-4AA3-A35E-0EBD79743B75Q27672444-64015719-3184-4E9E-A883-EB1DD60F6B88Q27679023-7F059DE7-4111-4AA3-B6CE-B6D2506C669EQ28595881-3969CBF5-2D6F-430C-8700-647855C481B8Q28597905-6D015C24-E691-455F-BC1A-F99114CD1AEEQ28601619-42C48780-E5E1-4993-9113-CF75813AA4FEQ28651985-EDE05BD9-7945-402F-B38F-5AFF1339ACA5Q28660964-BE1E2363-21B6-4011-8506-67ABB8B2574EQ28728187-507C4A0A-77D7-4BD3-9927-AAFD5249A61EQ28730087-8F6AB06A-7E60-4396-B5EC-BACE36F9AEC2Q28732773-993555D8-96CE-47DC-BF02-82FF16D23A2CQ28742837-269909B2-F93F-48BC-A3C1-A280538E06B6Q30799720-54C71272-5BE1-4DB6-8369-E694A66A0099Q33619443-9403CA1A-D3DF-47F5-BA6F-933446BF2BA0Q33728270-372F4970-4AFB-47FB-BB4D-BF9247B37830Q34000774-BE1FC471-C6C2-4782-841C-F4388198864BQ34018502-6952019D-874B-4C53-8D08-652C2588337CQ34136503-52966F8A-2F4D-4F27-AA2E-E81CE974B5B3Q34154286-EAF79AC8-E34D-4EB1-882D-673788096F86Q34334762-4FA6FA85-DFDD-4BD5-BBB0-7296E2E11FF6Q34377603-37B0AC6F-5E31-4690-B9D9-8E6B700514D3Q34388738-F176D61D-BDA3-4E18-8581-981745FA7219Q34405654-953498B8-BA30-4C60-A0B2-87351059A0BCQ34416748-9F0C632C-360A-4731-9F9A-A0F5017295A8Q35000233-21E514D9-DD63-48A9-94F5-BCBAB61A228BQ35138894-E626B833-5F78-4DFE-A286-E38D7F49759AQ35439686-402A6CFB-9A34-4114-A774-70D391816AB1Q35451274-E61C0379-3E9E-418A-88D6-9E4C74CABAC0Q35579359-92050328-AC72-4872-B078-F218FEAD83E8Q35728158-562ABF84-E1F5-4FFC-8C64-D99847F8D8F3Q35739100-55DA174C-BD77-49F3-9FDA-2CE78DA39C12Q35745643-3FDED685-F3DA-47B2-83B0-1260F4055B63Q35770728-C9A7CE89-2ABC-4F84-AC58-5C63F8F71D53Q35914842-7CB990C1-A040-42CA-92C1-DBDEA995CAABQ36016970-4E651150-117A-48FD-8849-3B610A9E8DC8Q36155089-C8F6B212-E4A6-46AC-A812-D1728D97A801Q36216074-24D1FAE3-288F-4FA8-A4F8-891482ACA3F5Q36376289-72096641-06A2-4D5C-AAFD-09B0975F93F4
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 06 June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Cellulases and biofuels.
@en
Cellulases and biofuels.
@nl
type
label
Cellulases and biofuels.
@en
Cellulases and biofuels.
@nl
prefLabel
Cellulases and biofuels.
@en
Cellulases and biofuels.
@nl
P1476
Cellulases and biofuels.
@en
P2093
David B Wilson
P304
P356
10.1016/J.COPBIO.2009.05.007
P577
2009-06-06T00:00:00Z