Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes. - Test2 - elhamkhani - TriplyDB

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

http://www.wikidata.org/entity/Q34135196

about

Phosphoinositides: tiny lipids with giant impact on cell regulation Structural and Functional Integration of the PLCγ Interaction Domains Critical for Regulatory Mechanisms and Signaling Deregulation Autoinhibition and Phosphorylation-Induced Activation of Phospholipase C-γ Isozymes The phospholipase C isozymes and their regulation Novel regulation of PLCζ activity via its XY-linker Competition between Grb2 and Plcγ1 for FGFR2 regulates basal phospholipase activity and invasion.Role of Src homology domain binding in signaling complexes assembled by the murid γ-herpesvirus M2 protein.The autoinhibitory C-terminal SH2 domain of phospholipase C-γ2 stabilizes B cell receptor signalosome assembly.Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways Direct activation of human phospholipase C by its well known inhibitor u73122.Dynamics of PLCγ and Src family kinase 1 interactions during nuclear envelope formation revealed by FRET-FLIM.Membrane-induced allosteric control of phospholipase C-β isozymes.BANK1 and BLK act through phospholipase C gamma 2 in B-cell signaling Phospholipase Cζ binding to PtdIns(4,5)P2 requires the XY-linker region Inhibiting the Recruitment of PLCγ1 to Kaposi's Sarcoma Herpesvirus K15 Protein Reduces the Invasiveness and Angiogenesis of Infected Endothelial Cells Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2 deletions.Scaffold Protein SLP-76 Primes PLCγ1 for Activation by ITK-Mediated Phosphorylation.A hypermorphic missense mutation in PLCG2, encoding phospholipase Cγ2, causes a dominantly inherited autoinflammatory disease with immunodeficiency.Essential Role of the EF-hand Domain in Targeting Sperm Phospholipase Cζ to Membrane Phosphatidylinositol 4,5-Bisphosphate (PIP2).Mechanism of activation and inactivation of Gq/phospholipase C-β signaling nodes Chimeras of sperm PLCζ reveal disparate protein domain functions in the generation of intracellular Ca2+ oscillations in mammalian eggs at fertilization.Starting a new life: sperm PLC-zeta mobilizes the Ca2+ signal that induces egg activation and embryo development: an essential phospholipase C with implications for male infertility.Sperm PLCζ: from structure to Ca2+ oscillations, egg activation and therapeutic potential.Novel signalling mechanism and clinical applications of sperm-specific PLCζ.A PLC-γ1 Feedback Pathway Regulates Lck Substrate Phosphorylation at the T-Cell Receptor and SLP-76 Complex.Mechanism of Rac1-induced amplification in gastric mucosal phospholipase Cγ2 activation in response to Helicobacter pylori: modulatory effect of ghrelin.PLCγ1 participates in protein transport and diacylglycerol production triggered by cargo arrival at the Golgi.Serine/Threonine Kinase 3-Phosphoinositide-Dependent Protein Kinase-1 (PDK1) as a Key Regulator of Cell Migration and Cancer Dissemination.Nitrate signaling and early responses in Arabidopsis roots.Membrane environment exerts an important influence on rac-mediated activation of phospholipase Cγ2.A membrane-associated, fluorogenic reporter for mammalian phospholipase C isozymes.GLP-1 inhibits VEGFA-mediated signaling in isolated human endothelial cells and VEGFA-induced dilation of rat mesenteric arteries.SFKs phosphorylate PLCG1 Galpha(q) and phospholipase C-beta: turn on, turn off, and do it fast.Role of amplification in phospholipase Cγ2 activation in modulation of gastric mucosal inflammatory responses to Helicobacter pylori: effect of ghrelin.Dynamic Allostery in PLCγ1 and Its Modulation by a Cancer Mutation Revealed by MD Simulation and NMR Functional characterization of phospholipase C-γ mutant protein causing both somatic ibrutinib resistance and a germline monogenic autoinflammatory disorder

P2860

Q27012953-E11687CA-56B5-4C28-82FF-920741A6DEFB Q27674480-22EF52FC-2401-43B9-8D56-F0653DF6DCAB Q27678692-366E8FB4-1721-469E-9B30-63C6BFE2FB70 Q28261474-81E4E9FF-8DA0-4867-9F64-7DED8BF9CD94 Q28579036-8E7437F3-24E2-4D5D-934F-AB8C5D817208 Q30009495-6C4ADEA7-E1D4-42D9-8676-971BA508E448 Q30009958-B627643D-1407-4B2C-8906-C0CF8CB8F174 Q30588609-B53C89C9-FF3C-4770-8237-0EF0621D696C Q33737298-A5567D72-F594-4526-9997-D312839BF42F Q34160786-5CBAA065-F9A4-45BB-B0F0-6953F5BAD3CC Q34358006-E8446421-2934-461A-9A65-FCF0B645DFBD Q34396738-27ACB4AE-372E-47C2-B585-6AA655889108 Q34652368-438A907F-7088-47C3-9BEE-E2454245C04F Q35112291-272468BF-8120-4D34-85F0-07FCB0A1685A Q35752316-EE8AD6ED-C6DD-4B1B-857C-D2A0177E9412 Q35817877-2624ACA1-40C8-4A2D-8FB3-151BFF209E0C Q35967631-A858882D-EB71-4DE5-B5D9-F780FF1C1AFE Q36358469-E8D4232F-9FCE-423A-947B-112A4C802302 Q36444106-612841EB-B3A1-4062-9B1A-5D83F364A5DB Q36765162-BAFDBD7D-8CAB-42A8-906E-72111C49EB82 Q37348834-9BFD7444-8197-40CF-96C7-661C5A6E79BA Q37956573-B40A10EA-69E9-48D5-98D1-8EFD47D50FCB Q38155316-427FD5FF-232B-4A67-877A-BE8CB5803C1C Q38502046-F26B1051-7158-4E96-BADB-1222CE10DCE8 Q38712356-3151975F-6983-41E9-A568-019D4EEFE617 Q38896727-493E42B2-2FA1-48C9-BBAE-86E5BFAA6CB4 Q38930543-A51C175E-F0F4-4824-9B12-6303E9584F33 Q39175989-3253A7FD-028E-494E-83FD-BA84D2F1007E Q39215474-5CA20836-D333-4534-9EC1-7986D4381C6D Q39606133-069307FD-31E2-414A-835C-BD2C64FCE285 Q47269585-63470DEE-7F16-4A21-879C-632FF55E5F86 Q48255700-BBB91347-960B-4D43-9C88-C1C3EB2BF885 Q50297929-0E4DC8DC-44ED-465B-A10E-05C28FE60BBD Q53439100-64C75825-7270-4227-ADE2-8AA9F682027B Q55070384-CBC198E9-95D0-4AC4-A327-6CBD2DDDD635 Q57752495-544DA00A-A570-4348-AA88-D0B5BC73FAA4 Q57821054-EDFB19D3-33AF-4C1C-96F2-538C8103DA00

P2860

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

http://www.wikidata.org/entity/Q34135196

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@ast

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@en

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@nl

type

label

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@ast

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@en

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@nl

prefLabel

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@ast

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@en

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@nl

P1433

Q34135196-7470D327-6152-475A-9D11-0A182636FC60

P1476

Q34135196-C4150C77-FA5E-440E-83EC-28BABC4B80EC

P2093

Q34135196-143FF285-68B6-455E-91C1-C64974304D40

Q34135196-A9BB8EB3-F980-469F-962C-451FB245CBBC

Q34135196-E5F751B7-2265-4CF0-A9EB-BA85B21FE881

P2860

Q34135196-05F47376-255F-4EFE-A4FA-B8B1791415D7

Q34135196-0EFC1AB0-6421-4345-8B89-9FD1B1D12D5D

Q34135196-179CA857-960E-4AF5-B74B-145A0ADF2B50

Q34135196-19882481-3A66-4540-AD4E-0F2FA66C1F16

Q34135196-199DD669-D410-4298-A7C2-77111B65F05A

Q34135196-1D22CA4E-B3B3-4C08-AA43-47D4CCDAD195

Q34135196-229A6C89-6821-46BE-819F-F3F1556A5BB2

Q34135196-3B58B0A3-BAAC-41D4-8467-5CC7A3DBE203

Q34135196-3E74968F-3E5B-44AC-8FBD-99AD95C469CE

Q34135196-3FA333E0-EC76-43E9-8552-12D21C3AED02

P304

Q34135196-B8186C51-47C7-4A69-B35A-DA1F3A831B1B

P31

Q34135196-1707FE61-8E32-4452-8A94-3E7FA55969BE

P356

Q34135196-BF17E177-C161-4E55-8062-F35CA54F7F65

P407

Q34135196-068DAE68-2612-48F8-A1E8-057C6C59B3D5

P433

Q34135196-9F348FB4-CCD3-4577-91DB-2F9AA6A05319

P478

Q34135196-4328DE70-797A-4587-8F47-DA3F60998341

P50

Q34135196-B6F9F902-FD67-4692-AB56-E8069511B0C7

P577

Q34135196-87479D09-765D-4575-A3B6-7189CC133860

P698

Q34135196-8F369ACC-1F89-4F2F-8E16-7E9480984363

P921

Q34135196-5D5BDE4A-1DD6-4CB4-BD07-BE57AFBCD882

P932

Q34135196-72EAA699-85FD-4D28-9F96-724D216B513B

P356

JBC.M110.166512

P1433

Journal of Biological Chemistry

P1476

Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.

@en

P2093

Aurelie Gresset

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

Stephanie N Hicks

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

T Kendall Harden

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

P2860

Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling

Activation of phospholipase Cgamma2 by tyrosine phosphorylation

Loops govern SH2 domain specificity by controlling access to binding pockets

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

Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide

Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site

Crystal structure of human protein-tyrosine phosphatase SHP-1

Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor

A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases

P304

35836-35847

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

P31

scholarly article

P356

10.1074/JBC.M110.166512

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

P407

P433

46

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

P478

285

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

P50

P577

2010-08-31T00:00:00Z

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

P698

20807769

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

P921

phosphorylation

P932

2975207

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