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The unique binding mode of cellulosomal CBM4 from Clostridium thermocellum cellobiohydrolase AStructure of a fibronectin type III-like module fromClostridium thermocellumCel48A from Thermobifida fusca: structure and site directed mutagenesis of key residuesRevealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelABioprospecting metagenomics of decaying wood: mining for new glycoside hydrolasesRedistribution of xylan in maize cell walls during dilute acid pretreatment.Towards an Understanding of Enhanced Biomass Digestibility by In Planta Expression of a Family 5 Glycoside Hydrolase.Cellulase linkers are optimized based on domain type and function: insights from sequence analysis, biophysical measurements, and molecular simulation.Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: implications for the genetic engineering of bioenergy cropsExpression of the Acidothermus cellulolyticus E1 endoglucanase in Caldicellulosiruptor bescii enhances its ability to deconstruct crystalline cellulose.Crystal structure and biochemical characterization of Chlamydomonas FDX2 reveal two residues that, when mutated, partially confer FDX2 the redox potential and catalytic properties of FDX1Investigation of the binding geometry of a peripheral membrane protein.Improving activity of minicellulosomes by integration of intra- and intermolecular synergies.Strategies to reduce end-product inhibition in family 48 glycoside hydrolases.The Multi Domain Caldicellulosiruptor bescii CelA Cellulase Excels at the Hydrolysis of Crystalline CelluloseImpact of alg3 gene deletion on growth, development, pigment production, protein secretion, and functions of recombinant Trichoderma reesei cellobiohydrolases in Aspergillus niger.Handling gene and protein names in the age of bioinformatics: the special challenge of secreted multimodular bacterial enzymes such as the cbhA/cbh9A gene of Clostridium thermocellum.Charge engineering of cellulases improves ionic liquid tolerance and reduces lignin inhibitionResponse to Comment on "Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA"
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description
researcher, ORCID id # 0000-0002-8352-4234
@en
wetenschapper
@nl
name
Roman Brunecky
@ast
Roman Brunecky
@en
Roman Brunecky
@es
Roman Brunecky
@nl
type
label
Roman Brunecky
@ast
Roman Brunecky
@en
Roman Brunecky
@es
Roman Brunecky
@nl
prefLabel
Roman Brunecky
@ast
Roman Brunecky
@en
Roman Brunecky
@es
Roman Brunecky
@nl
P106
P31
P496
0000-0002-8352-4234