Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps - sprookjes - yvandenbroek - TriplyDB

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

http://www.wikidata.org/entity/Q27339563

about

Smooth deuterated cellulose films for the visualisation of adsorbed bio-macromolecules Endozoicomonas genomes reveal functional adaptation and plasticity in bacterial strains symbiotically associated with diverse marine hosts.A novel bi-directional promoter system allows tunable recombinant protein production in Pichia pastoris Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose.Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states.Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.Collective Force Regulation in Anti-parallel Microtubule Gliding by Dimeric Kif15 Kinesin Motors.New Genomic Approaches to Enhance Biomass Degradation by the Industrial Fungus Processive chitinase is Brownian monorail operated by fast catalysis after peeling rail from crystalline chitin

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P2860

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

http://www.wikidata.org/entity/Q27339563

description

2015 nî lūn-bûn

@nan

2015 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@ast

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@en

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@nl

type

label

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@ast

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@en

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@nl

prefLabel

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@ast

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@en

Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@nl

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Nature Communications

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Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

@en

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Matthew J Lang

http://www.w3.org/2001/XMLSchema#string

Sarangapani Sreelatha

http://www.w3.org/2001/XMLSchema#string

Shishir P S Chundawat

http://www.w3.org/2001/XMLSchema#string

Sonia K Brady

http://www.w3.org/2001/XMLSchema#string

Yinnian Feng

http://www.w3.org/2001/XMLSchema#string

P2860

Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis

Direct observation of base-pair stepping by RNA polymerase

Myosin VI is a processive motor with a large step size

Single-molecule analysis of dynein processivity and stepping behavior

Cellulose: fascinating biopolymer and sustainable raw material

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

A comparison of step-detection methods: how well can you do?

Binding and movement of individual Cel7A cellobiohydrolases on crystalline cellulose surfaces revealed by single-molecule fluorescence imaging

Picocalorimetry of transcription by RNA polymerase.

High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose

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P304

10149

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scholarly article

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2743389

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10.1038/NCOMMS10149

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P478

6

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P577

2015-12-10T00:00:00Z

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286543655

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1017295789

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26657780

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P932

4682103

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