Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

about

Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

Item

http://www.wikidata.org/entity/Q43629456

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

2001年學術文章

@zh

2001年學術文章

@zh-hant

name

Structural basis for the activity of pp60

@nl

Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

@en

type

Item

label

Structural basis for the activity of pp60

@nl

Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

@en

prefLabel

Structural basis for the activity of pp60

@nl

Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

@en

P1476

Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.

@en

P2093

McMurray JS

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

Pettitt BM

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

Prabhu NV

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

Siddiqui SA

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

P2860

Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor

Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

Three-dimensional structure of the tyrosine kinase c-Src

Crystal structure of the Src family tyrosine kinase Hck

The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units

Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

P304

167-179

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

P31

scholarly article

P356

10.1002/1097-0282(200109)59:3<167::AID-BIP1016>3.0.CO;2-L

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

P433

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

P478

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

P577

2001-09-01T00:00:00Z

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

P698

11391566

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