Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain - Wikidata - awgldk - TriplyDB

Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain

Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain

http://www.wikidata.org/entity/Q30009972

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A lack of peptide binding and decreased thermostability suggests that the CASKIN2 scaffolding protein SH3 domain may be vestigial.

P2860

Q30008864-F6ABEA73-8AA2-48B6-BD0A-F1112AAF2244

P2860

Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain

http://www.wikidata.org/entity/Q30009972

description

2012 nî lūn-bûn

@nan

2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@ast

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@en

type

label

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@ast

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@en

prefLabel

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@ast

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

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1478-811X-10-36

P1433

Cell Communication and Signaling

P1476

Complex formation of EphB1/Nck ...... nges of the Caskin1 SH3 domain

@en

P2093

Anna Fekete

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

Annamária Balázs

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

Gábor Bőgel

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

László Buday

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

Roopesh Udupa

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

Szabolcs Pesti

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

P2860

PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands

Characterization of interactions of Nck with Sos and dynamin

Identification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1

CASK participates in alternative tripartite complexes in which Mint 1 competes for binding with caskin 1, a novel CASK-binding protein

EphB1 associates with Grb7 and regulates cell migration

Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor

Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase

High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1

Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation

SH3 domains come of age

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1478-811x-10-36

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36

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

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scholarly article

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3561486

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10.1186/1478-811X-10-36

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1

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10

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2012-11-27T00:00:00Z

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1035617661

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P698

23181695

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

P921

phosphorylation

P932

3549760

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