Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP. - Test2 - elhamkhani - TriplyDB

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

http://www.wikidata.org/entity/Q37376986

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Protective roles of NF-kB for chromium (VI)-induced cytotoxicity is revealed by expression of IkB kinase-B mutant IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition.XIAP: cell death regulation meets copper homeostasis A novel role for XIAP in copper homeostasis through regulation of MURR1 VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activation XIAP deficiency: a unique primary immunodeficiency best classified as X-linked familial hemophagocytic lymphohistiocytosis and not as X-linked lymphoproliferative disease Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death FGD2, a CDC42-specific exchange factor expressed by antigen-presenting cells, localizes to early endosomes and active membrane ruffles The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites XIAP regulates cytosol-specific innate immunity to Listeria infection XIAP Induces NF-κB Activation via the BIR1/TAB1 Interaction and BIR1 Dimerization X-linked lymphoproliferative syndromes: brothers or distant cousins?ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis Neurotrophin receptor-interacting mage homologue is an inducible inhibitor of apoptosis protein-interacting protein that augments cell death Does antigen masking by ubiquitin chains protect from the development of autoimmune diseases?Jun kinase delays caspase-9 activation by interaction with the apoptosome IAP regulation of metastasis.Using flow cytometry to screen patients for X-linked lymphoproliferative disease due to SAP deficiency and XIAP deficiency African swine fever virus IAP-like protein induces the activation of nuclear factor kappa B The IAP proteins: caspase inhibitors and beyond.Survivin and IAP proteins in cell-death mechanisms Translational upregulation of the X-linked inhibitor of apoptosis.Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function.Proliferation of human HCC cells and chemically induced mouse liver cancers requires JNK1-dependent p21 downregulation.IAP-targeted therapies for cancer.XIAP mediates NOD signaling via interaction with RIP2 XIAP as a ubiquitin ligase in cellular signaling.A mutational analysis of the baculovirus inhibitor of apoptosis Op-IAP.X-linked inhibitor of apoptosis protein deficiency: more than an X-linked lymphoproliferative syndrome.XIAP upregulates expression of HIF target genes by targeting HIF1α for Lys63-linked polyubiquitination.Distinct role of calmodulin and calmodulin-dependent protein kinase-II in lipopolysaccharide and tumor necrosis factor-alpha-mediated suppression of apoptosis and antiapoptotic c-IAP2 gene expression in human monocytic cells.Uncoupling of the signaling and caspase-inhibitory properties of X-linked inhibitor of apoptosis.Inhibiting apoptosis in mammalian cell culture using the caspase inhibitor XIAP and deletion mutants.Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium.Inhibitor of apoptosis protein cIAP2 is essential for lipopolysaccharide-induced macrophage survival.Activation of JNK, p38 and ERK mitogen-activated protein kinases by chromium(VI) is mediated through oxidative stress but does not affect cytotoxicity.XIAP inhibition of caspase-3 preserves its association with the Apaf-1 apoptosome and prevents CD95- and Bax-induced apoptosis.

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P2860

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

http://www.wikidata.org/entity/Q37376986

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 1998

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@en

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@nl

type

label

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@en

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@nl

prefLabel

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@en

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@nl

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P356

PNAS.95.11.6015

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

@en

P2093

B W Richter

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

C B Thompson

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

C S Duckett

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

M G Sanna

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

R J Ulevitch

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

P2860

JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes

Daxx, a novel Fas-binding protein that activates JNK and apoptosis

X-linked IAP is a direct inhibitor of cell-death proteases

The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases

A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors

Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine

Stress-signalling kinase Sek1 protects thymocytes from apoptosis mediated by CD95 and CD3

P304

6015-6020

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scholarly article

P356

10.1073/PNAS.95.11.6015

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P407

P433

11

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P478

95

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1998-05-01T00:00:00Z

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P5875

13683101

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P698

9600909

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P921

apoptotic process

P932

27577

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