c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment. - Wikidata - awgldk - TriplyDB

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

http://www.wikidata.org/entity/Q40838878

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BAD is a pro-survival factor prior to activation of its pro-apoptotic function Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth Proteolytic cleavage of Livin (ML-IAP) in apoptotic melanoma cells potentially mediated by a non-canonical caspase Endogenous association of TRAF2, TRAF3, cIAP1, and Smac with lymphotoxin beta receptor reveals a novel mechanism of apoptosis Expression of BIRC7 protein and mRNA in non-Hodgkin's lymphoma Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9 Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo Comparative proteomic analysis of low stage and high stage endometrioid ovarian adenocarcinomas.Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance Splice variants of mIAP1 have an enhanced ability to inhibit apoptosis Enhancing DNA vaccine potency by coadministration of DNA encoding antiapoptotic proteins.tLivin displays flexibility by promoting alternative cell death mechanisms Alphaviruses and apoptosis.Modulation and function of caspase pathways in B lymphocytes.The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling Inhibitor of apoptosis proteins: new therapeutic targets in hematological cancer?RIP1 Cleavage in the Kinase Domain Regulates TRAIL-Induced NF-κB Activation and Lymphoma Survival.The RING domain of cIAP1 mediates the degradation of RING-bearing inhibitor of apoptosis proteins by distinct pathways.Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway.PERK-dependent regulation of IAP translation during ER stress.Neuronal apoptosis inhibitory protein is overexpressed in patients with unfavorable prognostic factors in breast cancer IAP-targeted therapies for cancer.Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2.Distinctive effects of the cellular inhibitor of apoptosis protein c-IAP2 through stabilization by XIAP in glioblastoma multiforme cells.The Paradox of p53: What, How, and Why?Degradation of cIAPs contributes to hepatocyte lipoapoptosis.Promotion of Caspase Activation by Caspase-9-mediated Feedback Amplification of Mitochondrial Damage.Activation of specific apoptotic caspases with an engineered small-molecule-activated protease.Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells.Alpha-fetoprotein positively regulates cytochrome c-mediated caspase activation and apoptosome complex formation.Renal tubular epithelial cell apoptosis is associated with caspase cleavage of the NHE1 Na+/H+ exchanger.Inhibiting apoptosis in mammalian cell culture using the caspase inhibitor XIAP and deletion mutants.Cellular inhibitor of apoptosis 1 (cIAP-1) degradation by caspase 8 during TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis.A novel function of cIAP1 as a mediator of CHIP-driven eIF4E regulation.Caspases and IAPs: a dance of death ensures cell survival.cIAP-1, but not XIAP, is cleaved by caspases during the apoptosis induced by TGF-beta in fetal rat hepatocytes.The translation of an antiapoptotic protein HIAP2 is regulated by an upstream open reading frame.Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways.Alterations in apoptosis regulatory factors during hypertrophy and heart failure.

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P2860

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

http://www.wikidata.org/entity/Q40838878

description

2000 nî lūn-bûn

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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2000年學術文章

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2000年學術文章

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name

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

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type

label

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

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prefLabel

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

@en

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Journal of Biological Chemistry

P1476

c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment.

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P2093

Clem RJ

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Duckett CS

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Hardwick JM

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He WW

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Richter BW

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Sheu TT

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Thornberry NA

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7602-7608

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scholarly article

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10.1074/JBC.M010259200

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10

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276

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11106668

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