Differential contributions of Glu96, Asp102 and Asp111 to coagulation factor V/Va metal ion binding and subunit stability.

about

Functional characterization of a novel missense mutation identified in a Turkish patient affected by severe coagulation factor V deficiency.

P2860

Q45871981-8F528EFA-568D-435B-AB3B-02ADA4F53680

P2860

Differential contributions of Glu96, Asp102 and Asp111 to coagulation factor V/Va metal ion binding and subunit stability.

Item

http://www.wikidata.org/entity/Q45971310

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

Differential contributions of ...... binding and subunit stability.

@en

Differential contributions of ...... binding and subunit stability.

@nl

type

Item

label

Differential contributions of ...... binding and subunit stability.

@en

Differential contributions of ...... binding and subunit stability.

@nl

prefLabel

Differential contributions of ...... binding and subunit stability.

@en

Differential contributions of ...... binding and subunit stability.

@nl

P1476

Differential contributions of ...... binding and subunit stability.

@en

P2093

Edward L G Pryzdial

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

Jeffrey Hewitt

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

Jina Song

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

Kimberley Talbot

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

Ross T A MacGillivray

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

P2860

Crystal structures of the membrane-binding C2 domain of human coagulation factor V

Factor V: a combination of Dr Jekyll and Mr Hyde

The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.

Coagulation factor Va Glu-96-Asp-111: a chelator-sensitive site involved in function and subunit association.

Structural investigation of the A domains of human blood coagulation factor V by molecular modeling.

Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity.

Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity.

Functional properties of recombinant factor V mutated in a potential calcium-binding site.

A domain mutations in 65 haemophilia A families and molecular modelling of dysfunctional factor VIII proteins.

Factor VIII (FVIII) gene mutations in 120 patients with hemophilia A: detection of 26 novel mutations and correlation with FVIII inhibitor development.

P304

257-264

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

P31

scholarly article

P356

10.1042/BJ20090405

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

P407

English

P433

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

P478

422

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

P577

2009-08-13T00:00:00Z

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

P5875

26288570

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

P698

19522703

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

Differential contributions of Glu96, Asp102 and Asp111 to coagulation factor V/Va metal ion binding and subunit stability.

about

P2860

P2860

Differential contributions of Glu96, Asp102 and Asp111 to coagulation factor V/Va metal ion binding and subunit stability.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698