LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis. - Wikidata - awgldk - TriplyDB

LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis.

LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis.

http://www.wikidata.org/entity/Q33939284

about

Copper-catalyzed azide-alkyne cycloaddition (click chemistry)-based detection of global pathogen-host AMPylation on self-assembled human protein microarrays.Protective Role of Rho Guanosine Diphosphate Dissociation Inhibitor, Ly-GDI, in Pulmonary Alveolitis.Screening and identification of five serum proteins as novel potential biomarkers for cured pulmonary tuberculosis Analysis of the Effects of the Bruton's tyrosine kinase (Btk) Inhibitor Ibrutinib on Monocyte Fcγ Receptor (FcγR) Function.Pharmacological targeting of phosphoinositide lipid kinases and phosphatases in the immune system: success, disappointment, and new opportunities.Rho GDP dissociation inhibitor-β in renal cell carcinoma.VEGF-C mediates RhoGDI2-induced gastric cancer cell metastasis and cisplatin resistance.

P2860

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P2860

LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis.

http://www.wikidata.org/entity/Q33939284

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@ast

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

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type

label

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@ast

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@en

prefLabel

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@ast

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@en

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JOURNAL.PONE.0021175

P1433

P1476

LyGDI, a novel SHIP-interactin ...... of FcγR-mediated phagocytosis.

@en

P2093

Anne-Sophie Wavreille

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

David Jarjoura

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

Jianhua Yu

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

Jonathan P Butchar

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

Michael A Caligiuri

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

Payal Mehta

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

Rachel L Marsh

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Richard W Burry

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

Steven E Justiniano

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

Susheela Tridandapani

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

P2860

SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading

Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes

Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization.

cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins

Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton

RhoGDI: multiple functions in the regulation of Rho family GTPase activities

The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin

Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product

A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells

The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in B cells under negative signaling

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e21175

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scholarly article

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10.1371/JOURNAL.PONE.0021175

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6

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