Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila. - Wikidata - wikimedia - TriplyDB

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

http://www.wikidata.org/entity/Q30193377

about

ShcA and Grb2 mediate polyoma middle T antigen-induced endothelial transformation and Gab1 tyrosine phosphorylation.ShcA tyrosine phosphorylation sites can replace ShcA binding in signalling by middle T-antigen Drosophila-raf acts to elaborate dorsoventral pattern in the ectoderm of developing embryos Quantifying intramolecular binding in multivalent interactions: a structure-based synergistic study on Grb2-Sos1 complex Targeted expression of the class II phosphoinositide 3-kinase in Drosophila melanogaster reveals lipid kinase-dependent effects on patterning and interactions with receptor signaling pathways.Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase Octopamine-mediated circuit mechanism underlying controlled appetite for palatable food in Drosophila Alternate serotype adenovector provides long-term therapeutic gene expression in the eye.DRK/DOS/SOS converge with Crk/Mbc/dCed-12 to activate Rac1 during glial engulfment of axonal debris.Ocular localization and transduction by adenoviral vectors are serotype-dependent and can be modified by inclusion of RGD fiber modifications Deregulation of the Egfr/Ras signaling pathway induces age-related brain degeneration in the Drosophila mutant vap.Synergistic activities of multiple phosphotyrosine residues mediate full signaling from the Drosophila Torso receptor tyrosine kinase.Genetic analysis reveals cell type-specific regulation of receptor tyrosine kinase c-Kit by the protein tyrosine phosphatase SHP1 A Drosophila shc gene product is implicated in signaling by the DER receptor tyrosine kinase.Scaffolding protein Grb2-associated binder 1 sustains epidermal growth factor-induced mitogenic and survival signaling by multiple positive feedback loops.A dual role for the adaptor protein DRK in Drosophila olfactory learning and memory.p120 Ras GTPase-activating protein associates with fibroblast growth factor receptors in Drosophila.

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Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

http://www.wikidata.org/entity/Q30193377

description

1995 nî lūn-bûn

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1995 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հունիսին հրատարակված գիտական հոդված

@hy

1995年の論文

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1995年論文

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1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

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name

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@ast

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@en

type

label

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@ast

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@en

prefLabel

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@ast

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.

@en

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J.1460-2075.1995.TB07248.X

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The EMBO Journal

P1476

Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila

@en

P2093

Dickson B

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Gish GD

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Hafen E

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Liu X

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Olivier JP

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Pawson T

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Raabe T

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P2860

The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras

Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions

Structure of the PI3K SH3 domain and analysis of the SH3 family

Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy

SH2 domains recognize specific phosphopeptide sequences

SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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