A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation. - Wikidata - wikimedia - TriplyDB

A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.

A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.

http://www.wikidata.org/entity/Q33826228

about

Mechanism of enzymatic reaction and protein-protein interactions of PLD from a 3D structural model.RGS4 is required for dopaminergic control of striatal LTD and susceptibility to parkinsonian motor deficits PLC-γ directly binds activated c-Src, which is necessary for carbachol-mediated inhibition of NHE3 activity in Caco-2/BBe cells Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.The molecular basis of phospholipase D2-induced chemotaxis: elucidation of differential pathways in macrophages and fibroblasts.Phospholipase D signaling pathways and phosphatidic acid as therapeutic targets in cancer A river runs through it: how autophagy, senescence, and phagocytosis could be linked to phospholipase D by Wnt signaling Cell invasion of highly metastatic MTLn3 cancer cells is dependent on phospholipase D2 (PLD2) and Janus kinase 3 (JAK3).The exquisite regulation of PLD2 by a wealth of interacting proteins: S6K, Grb2, Sos, WASp and Rac2 (and a surprise discovery: PLD2 is a GEF).Phospholipase D: enzymology, functionality, and chemical modulation Phosphatidic Acid Increases Epidermal Growth Factor Receptor Expression by Stabilizing mRNA Decay and by Inhibiting Lysosomal and Proteasomal Degradation of the Internalized Receptor Biochemical and cellular implications of a dual lipase-GEF function of phospholipase D2 (PLD2).Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells A Repertoire of MicroRNAs Regulates Cancer Cell Starvation by Targeting Phospholipase D in a Feedback Loop That Operates Maximally in Cancer Cells A new signaling pathway (JAK-Fes-phospholipase D) that is enhanced in highly proliferative breast cancer cells A GEF-to-phospholipase molecular switch caused by phosphatidic acid, Rac and JAK tyrosine kinase that explains leukocyte cell migration Phosphatidic acid, phospholipase D and tumorigenesis.Phospholipase D (PLD) drives cell invasion, tumor growth and metastasis in a human breast cancer xenograph model.Phosphatidic acid and neurotransmission.Phospholipase D inhibitors reduce human prostate cancer cell proliferation and colony formation.

P2860

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P2860

A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.

http://www.wikidata.org/entity/Q33826228

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին 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

A comprehensive model that exp ...... phorylation-dephosphorylation.

@ast

A comprehensive model that exp ...... phorylation-dephosphorylation.

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type

label

A comprehensive model that exp ...... phorylation-dephosphorylation.

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A comprehensive model that exp ...... phorylation-dephosphorylation.

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prefLabel

A comprehensive model that exp ...... phorylation-dephosphorylation.

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A comprehensive model that exp ...... phorylation-dephosphorylation.

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Molecular and Cellular Biology

P1476

A comprehensive model that exp ...... phorylation-dephosphorylation.

@en

P2093

Hong-Juan Peng

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

Julian Gomez-Cambronero

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Karen M Henkels

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

Kathleen Frondorf

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P2860

The Grb2/PLD2 interaction is essential for lipase activity, intracellular localization and signaling in response to EGF

The elucidation of novel SH2 binding sites on PLD2

Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization

Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2

Phospholipase D: molecular and cell biology of a novel gene family

Transmodulation between phospholipase D and c-Src enhances cell proliferation

Differential tyrosine phosphorylation of phospholipase D isozymes by hydrogen peroxide and the epidermal growth factor in A431 epidermoid carcinoma cells

Determination of interaction sites on the small G protein RhoA for phospholipase D

PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation

Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha

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2251-2263

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scholarly article

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10.1128/MCB.01239-09

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9

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30

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2010-02-22T00:00:00Z

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41532223

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20176813

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phosphorylation

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2863589

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