src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity. - Wikidata - awgldk - TriplyDB

src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.

src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.

http://www.wikidata.org/entity/Q30193694

about

Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor Functional independence and interdependence of the Src homology domains of phospholipase C-gamma1 in B-cell receptor signal transduction.Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.Intramolecular regulation of phospholipase C-gamma1 by its C-terminal Src homology 2 domain.Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides.Requirements for distinct steps of phospholipase Cgamma2 regulation, membrane-raft-dependent targeting and subsequent enzyme activation in B-cell signalling.Purinergic stimulation of rat cardiomyocytes induces tyrosine phosphorylation and membrane association of phospholipase C gamma: a major mechanism for InsP3 generation.

P2860

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P2860

src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.

http://www.wikidata.org/entity/Q30193694

description

1995 nî lūn-bûn

@nan

1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

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

@wuu

name

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@ast

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@en

type

label

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@ast

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@en

prefLabel

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@ast

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@en

P1433

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P1433

Biochemical Journal

P1476

src-homology 2 (SH2) domain li ...... amma 1 structure and activity.

@en

P2093

Edwards G

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

Gibbs JB

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

Koblan KS

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

Pompliano DL

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

Schaber MD

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

P2860

DNA sequencing with chain-terminating inhibitors

A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1

Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes

Elevated content of the tyrosine kinase substrate phospholipase C-gamma 1 in primary human breast carcinomas

Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

SH2 domains recognize specific phosphopeptide sequences

Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq.

Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases

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

P304

745-751

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P31

scholarly article

P356

10.1042/BJ3050745

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P407

P478

305 ( Pt 3)

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P577

1995-02-01T00:00:00Z

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P5875

15668547

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P698

7531435

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P932

1136322

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