Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation. - Wikidata - awgldk - TriplyDB

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

http://www.wikidata.org/entity/Q34583708

about

RAS isoforms and mutations in cancer at a glance Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis Tyrosine phosphorylation of RAS by ABL allosterically enhances effector binding Intracellular and intercellular signaling networks in cancer initiation, development and precision anti-cancer therapy: RAS acts as contextual signaling hub.C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin creates a feed-forward C-terminal Src kinase activation loop that promotes cell motility.Oncogenic K-Ras upregulates ITGA6 expression via FOSL1 to induce anoikis resistance and synergizes with αV-Class integrins to promote EMT.Farnesyltransferase Inhibition Exacerbates Eosinophilic Inflammation and Airway Hyperreactivity in Mice with Experimental Asthma: The Complex Roles of Ras GTPase and Farnesylpyrophosphate in Type 2 Allergic Inflammation.Phosphorylation promotes binding affinity of Rap-Raf complex by allosteric modulation of switch loop dynamics

P2860

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P2860

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

http://www.wikidata.org/entity/Q34583708

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@ast

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@en

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@nl

type

label

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@ast

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@en

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@nl

prefLabel

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@ast

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@en

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.

@nl

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PNAS.1406559111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation

@en

P2093

Brian Raught

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

Gelareh Zadeh

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

Jeffrey E Lee

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

Jonathan D Cook

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

Kelly Burrell

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

Michael Ohh

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

Pardeep Heir

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

Severa Bunda

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

Tharan Srikumar

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

P2860

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions

The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

Guanosine triphosphatase stimulation of oncogenic Ras mutants

Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma

What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf

Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins

The GTPase superfamily: conserved structure and molecular mechanism

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

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phosphorylation

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