Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

about

Influences of argatroban on five fibrinogen assays.

P2860

Q48000795-14CC2EEA-B54D-4A9B-A1D5-778C179DA8BA

P2860

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

Item

http://www.wikidata.org/entity/Q36053189

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh

2016年學術文章

@zh-hant

name

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@ast

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@en

type

Item

label

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@ast

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@en

prefLabel

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@ast

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@en

P1476

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

@en

P2093

Alan R Stafford

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

Beverly A Leslie

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

Calvin H Yeh

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

James C Fredenburgh

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

Jeffrey I Weitz

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

P2860

Structure-based design of novel potent nonpeptide thrombin inhibitors

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

Structural identification of the pathway of long-range communication in an allosteric enzyme

Molecular basis of thrombomodulin activation of slow thrombin

Rigidification of the autolysis loop enhances Na+ binding to thrombin

Binding of -thrombin to surface-anchored platelet glycoprotein Ib sulfotyrosines through a two-site mechanism involving exosite I

Rational Design and Characterization of D-Phe-Pro-D-Arg-Derived Direct Thrombin Inhibitors

GpIbα Interacts Exclusively with Exosite II of Thrombin

Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors

Allosteric changes in solvent accessibility observed in thrombin upon active site occupation.

P304

e0157471

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0157471

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

P407

English

P433

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

P478

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

P577

2016-06-15T00:00:00Z

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

P698

27305147

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

P932

4909201

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

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

about

P2860

P2860

Dabigatran and Argatroban Diametrically Modulate Thrombin Exosite Function

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932