about
The role of receptor internalization in CD95 signaling.FADD protein release mirrors the development and aggressiveness of human non-small cell lung cancerFADD adaptor in cancerAntiapoptotic Effects of EGb 761Activation of inflammasomes requires intracellular redistribution of the apoptotic speck-like protein containing a caspase recruitment domainEffect of cocaine on Fas-associated protein with death domain in the rat brain: individual differences in a model of differential vulnerability to drug abusePreferential Fas-mediated apoptotic execution at G1 phase: the resistance of mitotic cells to the cell deathInteraction of double-stranded RNA-dependent protein kinase (PKR) with the death receptor signaling pathway in amyloid beta (Abeta)-treated cells and in APPSLPS1 knock-in miceExpression of serine 194-phosphorylated Fas-associated death domain protein correlates with proliferation in B-cell non-Hodgkin lymphomas.Phosphorylated FADD induces NF-kappaB, perturbs cell cycle, and is associated with poor outcome in lung adenocarcinomasNucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3.Phosphorylation of FADD by the kinase CK1α promotes KRASG12D-induced lung cancer.FADD regulates thymocyte development at the β-selection checkpoint by modulating Notch signaling.The Drosophila IMD pathway in the activation of the humoral immune response.The DUSP26 phosphatase activator adenylate kinase 2 regulates FADD phosphorylation and cell growth.Fas-associated death domain protein and adenosine partnership: fad in RA.RIP1 links inflammatory and growth factor signaling pathways by regulating expression of the EGFR.The carboxyl-terminal segment of the adaptor protein ALX directs its nuclear export during T cell activation.Tumor necrosis factor alpha-induced apoptosis requires p73 and c-ABL activation downstream of RB degradationPin1-FADD interactions regulate Fas-mediated apoptosis in activated eosinophils.The large conductance calcium-activated potassium channel affects extrinsic and intrinsic mechanisms of apoptosisApoptotic potential of Fas-associated death domain on regulation of cell death regulatory protein cFLIP and death receptor mediated apoptosis in HEK 293T cells.Adenosine receptors control a new pathway of Fas-associated death domain protein expression regulation by secretion.Constitutive phosphorylation mutation in Fas-associated death domain (FADD) results in early cell cycle defects.Effects of opiate drugs on Fas-associated protein with death domain (FADD) and effector caspases in the rat brain: regulation by the ERK1/2 MAP kinase pathway.A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway.
P2860
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P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Molecular evidence for the nuclear localization of FADD
@ast
Molecular evidence for the nuclear localization of FADD
@en
Molecular evidence for the nuclear localization of FADD
@nl
type
label
Molecular evidence for the nuclear localization of FADD
@ast
Molecular evidence for the nuclear localization of FADD
@en
Molecular evidence for the nuclear localization of FADD
@nl
prefLabel
Molecular evidence for the nuclear localization of FADD
@ast
Molecular evidence for the nuclear localization of FADD
@en
Molecular evidence for the nuclear localization of FADD
@nl
P2860
P356
P1476
Molecular evidence for the nuclear localization of FADD
@en
P2093
Gómez-Angelats M
P2860
P2888
P304
P356
10.1038/SJ.CDD.4401237
P407
P577
2003-07-01T00:00:00Z