Inhibitory properties of the P1 Tyr variant of antithrombin. - Wikidata - awgldk - TriplyDB

Inhibitory properties of the P1 Tyr variant of antithrombin.

Inhibitory properties of the P1 Tyr variant of antithrombin.

http://www.wikidata.org/entity/Q33749182

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Inhibitory properties of the P1 Tyr variant of antithrombin.

http://www.wikidata.org/entity/Q33749182

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2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մարտին 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

Inhibitory properties of the P1 Tyr variant of antithrombin.

@ast

Inhibitory properties of the P1 Tyr variant of antithrombin.

@en

type

label

Inhibitory properties of the P1 Tyr variant of antithrombin.

@ast

Inhibitory properties of the P1 Tyr variant of antithrombin.

@en

prefLabel

Inhibitory properties of the P1 Tyr variant of antithrombin.

@ast

Inhibitory properties of the P1 Tyr variant of antithrombin.

@en

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Inhibitory properties of the P1 Tyr variant of antithrombin.

@en

P2093

Alireza R Rezaie

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

Chandrashekhara Manithody

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

Likui Yang

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

Shabir H Qureshi

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

P2860

The anticoagulant activation of antithrombin by heparin

Crystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor X

The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions

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

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

The protein Z-dependent protease inhibitor is a serpin

Serpin structure, mechanism, and function

Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor: both active site and exosite interactions are required for inhibition.

Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins.

Isolation of a protein Z-dependent plasma protease inhibitor

P304

2680-2686

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scholarly article

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10.1021/BI100120A

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P407

P433

12

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P478

49

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P577

2010-03-01T00:00:00Z

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P5875

41577040

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P698

20184328

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P932

2844450

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