Enzyme-specific activation versus leaving group ability.

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Limiting the Number of Potential Binding Modes by Introducing Symmetry into Ligands: Structure-Based Design of Inhibitors for Trypsin-Like Serine Proteases.A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase.

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Enzyme-specific activation versus leaving group ability.

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http://www.wikidata.org/entity/Q43242803

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2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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name

Enzyme-specific activation versus leaving group ability.

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Enzyme-specific activation versus leaving group ability.

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type

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Enzyme-specific activation versus leaving group ability.

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Enzyme-specific activation versus leaving group ability.

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prefLabel

Enzyme-specific activation versus leaving group ability.

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Enzyme-specific activation versus leaving group ability.

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Enzyme-specific activation versus leaving group ability.

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P2093

Barbara Zarzycka

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

Berry Bögels

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

Floris L van Delft

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

Floris P J T Rutjes

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

Gijs Schaftenaar

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

Peter J L M Quaedflieg

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

Roseri J A C de Beer

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

Sander B Nabuurs

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

P2860

Density-functional thermochemistry. III. The role of exact exchange

X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate

Structure of a serine protease poised to resynthesize a peptide bond

On the size of the active site in proteases. I. Papain

Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field

Proteases in organic synthesis.

Substrate mimetics in protease catalysis: characteristics, kinetics, and synthetic utility.

A flexible approach to induced fit docking.

The catalytic triad of serine peptidases.

Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions.

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1785-1790

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scholarly article

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10.1002/CBIC.201200227

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P478

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

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2012-07-23T00:00:00Z

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229437768

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22821810

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Enzyme-specific activation versus leaving group ability.

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P2860

P2860

Enzyme-specific activation versus leaving group ability.

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