Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
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Towards a restriction proteinase: construction of a self-activating enzymeThe dynamic structure of thrombin in solutionRedesigning allosteric activation in an enzyme.NMR reveals a dynamic allosteric pathway in thrombin.Proteases as therapeutics.Differential protease activity augments polyphagy in Helicoverpa armigera.
P2860
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
description
2010 nî lūn-bûn
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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@ast
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@en
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@nl
type
label
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@ast
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@en
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@nl
prefLabel
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@ast
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@en
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@nl
P2860
P1476
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold
@en
P2093
Enrico Di Cera
Michael J Page
P2860
P304
P356
10.1016/J.JMB.2010.04.024
P407
P577
2010-06-04T00:00:00Z