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Thrombin inhibition by serpins disrupts exosite II

Thrombin inhibition by serpins disrupts exosite II

http://www.wikidata.org/entity/Q34352365

about

Rational design of potent, small, synthetic allosteric inhibitors of thrombin Development of Orally Active Thrombin Inhibitors for the Treatment of Thrombotic Disorder Diseases Thrombin inhibition by the serpins The complete N-terminal extension of heparin cofactor II is required for maximal effectiveness as a thrombin exosite 1 ligand.Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function Ligand binding to anion-binding exosites regulates conformational properties of thrombin.Non-canonical proteolytic activation of human prothrombin by subtilisin from Bacillus subtilis may shift the procoagulant-anticoagulant equilibrium toward thrombosis.β2 -Glycoprotein I binds to thrombin and selectively inhibits the enzyme procoagulant functions.

P2860

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P2860

Thrombin inhibition by serpins disrupts exosite II

http://www.wikidata.org/entity/Q34352365

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

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

Thrombin inhibition by serpins disrupts exosite II

@ast

Thrombin inhibition by serpins disrupts exosite II

@en

Thrombin inhibition by serpins disrupts exosite II

@nl

type

label

Thrombin inhibition by serpins disrupts exosite II

@ast

Thrombin inhibition by serpins disrupts exosite II

@en

Thrombin inhibition by serpins disrupts exosite II

@nl

prefLabel

Thrombin inhibition by serpins disrupts exosite II

@ast

Thrombin inhibition by serpins disrupts exosite II

@en

Thrombin inhibition by serpins disrupts exosite II

@nl

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P356

JBC.M110.144964

P1433

Journal of Biological Chemistry

P1476

Thrombin inhibition by serpins disrupts exosite II

@en

P2093

Daniel J D Johnson

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

James A Huntington

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

Ty E Adams

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

Vincenzo De Filippis

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

P2860

Structure of a serpin-protease complex shows inhibition by deformation

Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase

The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment

The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer

Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin

Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin

Serpin structure, mechanism, and function

A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism.

Molecular recognition mechanisms of thrombin.

Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase.

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38621-38629

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scholarly article

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49

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285

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20889971

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2992294

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