about
The Grb2/PLD2 interaction is essential for lipase activity, intracellular localization and signaling in response to EGFA novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanismMechanism of enzymatic reaction and protein-protein interactions of PLD from a 3D structural model.Phospholipase D2 acts as an essential adaptor protein in the activation of Syk in antigen-stimulated mast cellsShort-hairpin RNA-mediated stable silencing of Grb2 impairs cell growth and DNA synthesisTwo sites of action for PLD2 inhibitors: The enzyme catalytic center and an allosteric, phosphoinositide biding pocket.A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.Mammalian target of rapamycin (mTOR) and S6 kinase down-regulate phospholipase D2 basal expression and function.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 cancerThe mechanism of cell membrane ruffling relies on a phospholipase D2 (PLD2), Grb2 and Rac2 associationThe 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 modulationPhospholipase D2 (PLD2) is a guanine nucleotide exchange factor (GEF) for the GTPase Rac2.Phospholipase D2 (PLD2) shortens the time required for myeloid leukemic cell differentiation: mechanism of actionPhosphatidic Acid Increases Epidermal Growth Factor Receptor Expression by Stabilizing mRNA Decay and by Inhibiting Lysosomal and Proteasomal Degradation of the Internalized ReceptorMutation of Y179 on phospholipase D2 (PLD2) upregulates DNA synthesis in a PI3K-and Akt-dependent manner.Serum deprivation confers the MDA-MB-231 breast cancer line with an EGFR/JAK3/PLD2 system that maximizes cancer cell invasionA new signaling pathway (JAK-Fes-phospholipase D) that is enhanced in highly proliferative breast cancer cellsPhosphatidic acid signaling regulation of Ras superfamily of small guanosine triphosphatases.PLD2 has both enzymatic and cell proliferation-inducing capabilities, that are differentially regulated by phosphorylation and dephosphorylation.Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease.Role of phospholipase d in g-protein coupled receptor functionPhagocyte cell migration is mediated by phospholipases PLD1 and PLD2.PA promoted to manager
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The elucidation of novel SH2 binding sites on PLD2
@ast
The elucidation of novel SH2 binding sites on PLD2
@en
The elucidation of novel SH2 binding sites on PLD2
@en-gb
The elucidation of novel SH2 binding sites on PLD2
@nl
type
label
The elucidation of novel SH2 binding sites on PLD2
@ast
The elucidation of novel SH2 binding sites on PLD2
@en
The elucidation of novel SH2 binding sites on PLD2
@en-gb
The elucidation of novel SH2 binding sites on PLD2
@nl
prefLabel
The elucidation of novel SH2 binding sites on PLD2
@ast
The elucidation of novel SH2 binding sites on PLD2
@en
The elucidation of novel SH2 binding sites on PLD2
@en-gb
The elucidation of novel SH2 binding sites on PLD2
@nl
P2093
P2860
P356
P1433
P1476
The elucidation of novel SH2 binding sites on PLD2
@en
P2093
P2860
P2888
P304
P356
10.1038/SJ.ONC.1209340
P407
P577
2006-05-18T00:00:00Z
P5875
P6179
1030992348