about
The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complexPTEN function: how normal cells control it and tumour cells lose itInhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3Phosphoinositides: tiny lipids with giant impact on cell regulationThe Multifaceted Roles of PI3Kγ in Hypertension, Vascular Biology, and InflammationInpp5f is a polyphosphoinositide phosphatase that regulates cardiac hypertrophic responsivenessThe SH2-domain-containing inositol 5-phosphatase (SHIP) limits the motility of neutrophils and their recruitment to wounds in zebrafishLyn, PKC-delta, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretionDifferential roles for the inositol phosphatase SHIP in the regulation of macrophages and lymphocytes.Role of SHIP-1 in the adaptive immune responses to aeroallergen in the airwayPhosphoinositide phosphatases in cell biology and disease.Optimal aggregation of FcεRI with a structurally defined trivalent ligand overrides negative regulation driven by phosphatases.Alteration of phosphatidylinositol 3-kinase cascade in the multilobulated nuclear formation of adult T cell leukemia/lymphoma (ATLL)Coordinate suppression of B cell lymphoma by PTEN and SHIP phosphatases.Functional requirements for inhibitory signal transmission by the immunomodulatory receptor CD300a.Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival.Accumulation of splice variants and transcripts in response to PI3K inhibition in T cells.Deficiency of lipid phosphatase SHIP enables long-term reconstitution of hematopoietic inductive bone marrow microenvironment.SH2-containing inositol 5'-phosphatase inhibits transformation of Abelson murine leukemia virus.The structure of phosphoinositide phosphatases: Insights into substrate specificity and catalysis.Glycodelin-A protein interacts with Siglec-6 protein to suppress trophoblast invasiveness by down-regulating extracellular signal-regulated kinase (ERK)/c-Jun signaling pathway.Therapeutic potential of SH2 domain-containing inositol-5'-phosphatase 1 (SHIP1) and SHIP2 inhibition in cancermiR-155 regulates IFN-γ production in natural killer cells.T cell-specific deletion of the inositol phosphatase SHIP reveals its role in regulating Th1/Th2 and cytotoxic responses.Nik-related kinase regulates trophoblast proliferation and placental development by modulating AKT phosphorylation.A regulatory role for Src homology 2 domain-containing inositol 5'-phosphatase (SHIP) in phagocytosis mediated by Fc gamma receptors and complement receptor 3 (alpha(M)beta(2); CD11b/CD18)Phospholipids: "greasing the wheels" of humoral immunityAging of the brain, neurotrophin signaling, and Alzheimer's disease: is IGF1-R the common culprit?The inositol phosphatase SHIP controls Salmonella enterica serovar Typhimurium infection in vivoOverexpression of miR-155 causes expansion, arrest in terminal differentiation and functional activation of mouse natural killer cellsSurvival of monocytes and macrophages and their role in health and disease.High expression of inositol polyphosphate phosphatase-like 1 associates with unfavorable survival in hepatocellular carcinomaAberrant antibody affinity selection in SHIP-deficient B cells.Inhibitor and activator: dual functions for SHIP in immunity and cancer.Inhibitory receptors on lymphocytes: insights from infectionsPotential role of histamine releasing factor (HRF) as a therapeutic target for treating asthma and allergy.Biochemistry and structure of phosphoinositide phosphatases.Role of phosphoinositide 3-kinase in the pathogenesis of acute pancreatitis.BMP4/Smad5 dependent stress erythropoiesis is required for the expansion of erythroid progenitors during fetal development.The tumor suppressor SHIP1 colocalizes in nucleolar cavities with p53 and components of PML nuclear bodies.
P2860
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P2860
description
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im März 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/03/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/03/01)
@nl
наукова стаття, опублікована в березні 2000
@uk
مقالة علمية (نشرت في مارس 2000)
@ar
name
Structure, function, and biology of SHIP proteins
@ast
Structure, function, and biology of SHIP proteins
@en
Structure, function, and biology of SHIP proteins
@nl
type
label
Structure, function, and biology of SHIP proteins
@ast
Structure, function, and biology of SHIP proteins
@en
Structure, function, and biology of SHIP proteins
@nl
prefLabel
Structure, function, and biology of SHIP proteins
@ast
Structure, function, and biology of SHIP proteins
@en
Structure, function, and biology of SHIP proteins
@nl
P2093
P1433
P1476
Structure, function, and biology of SHIP proteins
@en
P2093
D. M. Lucas
J. F. Fuller
L. R. Rohrschneider
P304
P577
2000-03-01T00:00:00Z