RIP and FADD: two "death domain"-containing proteins can induce apoptosis by convergent, but dissociable, pathways. - Wikidata - awgldk - TriplyDB

RIP and FADD: two "death domain"-containing proteins can induce apoptosis by convergent, but dissociable, pathways.

RIP and FADD: two "death domain"-containing proteins can induce apoptosis by convergent, but dissociable, pathways.

http://www.wikidata.org/entity/Q37303348

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Daxx silencing sensitizes cells to multiple apoptotic pathways CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein Human ALKBH7 is required for alkylation and oxidation-induced programmed necrosis The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation MicroRNA-155 prevents necrotic cell death in human cardiomyocyte progenitor cells via targeting RIP1 Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP Noncanocial cell death program independent of caspase activation cascade and necroptotic modules is elicited by loss of TGFβ-activated kinase 1.Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway The RIP-like kinase, RIP3, induces apoptosis and NF-kappaB nuclear translocation and localizes to mitochondria.Caspase-3 apoptotic signaling following injury to the central nervous system.Unique and overlapping substrate specificities of caspase-8 and caspase-10.Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway Defects in regulation of apoptosis in caspase-2-deficient mice.Reactive nitrogen species-induced cell death requires Fas-dependent activation of c-Jun N-terminal kinase The dual functions of receptor interacting protein 1 in fas-induced hepatocyte death during sepsis.Novel transcriptome assembly and comparative toxicity pathway analysis in mahi-mahi (Coryphaena hippurus) embryos and larvae exposed to Deepwater Horizon oil Focal adhesion kinase suppresses apoptosis by binding to the death domain of receptor-interacting protein.Chemical regulation of signaling pathways to programmed necrosis.Molluscum Contagiosum Virus MC159 Abrogates cIAP1-NEMO Interactions and Inhibits NEMO Polyubiquitination.Increased miR-155-5p and reduced miR-148a-3p contribute to the suppression of osteosarcoma cell death.Necrosome core machinery: MLKL.RIPK1- and RIPK3-induced cell death mode is determined by target availability.Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis.The receptor interacting protein 1 inhibits p53 induction through NF-kappaB activation and confers a worse prognosis in glioblastoma.RIPK1-dependent apoptosis bypasses pathogen blockade of innate signaling to promote immune defense.Role of receptor-interacting protein in tumor necrosis factor-alpha -dependent MEKK1 activation.RIP1 activates PI3K-Akt via a dual mechanism involving NF-kappaB-mediated inhibition of the mTOR-S6K-IRS1 negative feedback loop and down-regulation of PTEN.RIP1 comes back to life as a cell death regulator in TNFR1 signaling.Propapoptotic effects of NF-kappaB in LNCaP prostate cancer cells lead to serine protease activation.Targeting proliferating tumor cells via the transcriptional control of therapeutic genes.NF-kappaB protects macrophages from lipopolysaccharide-induced cell death: the role of caspase 8 and receptor-interacting protein.T47-D cells and type V collagen: a model for the study of apoptotic gene expression by breast cancer cells.Phenytoin-induced gingival overgrowth caused by death receptor pathway malfunction.Tumor necrosis factor-alpha and Fas activate complementary Fas-associated death domain-dependent pathways that enhance apoptosis induced by gamma-irradiation.Exploiting Cell Death Pathways for Inducible Cell Elimination to Modulate Graft-versus-Host-Disease.

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RIP and FADD: two "death domain"-containing proteins can induce apoptosis by convergent, but dissociable, pathways.

http://www.wikidata.org/entity/Q37303348

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on October 1996

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@en

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@nl

type

label

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@en

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@nl

prefLabel

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@en

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@nl

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P356

PNAS.93.20.10923

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

P1476

RIP and FADD: two "death domai ...... nt, but dissociable, pathways.

@en

P2093

Grimm S

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

Leder P

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Stanger BZ

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P2860

A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways

The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor

Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system

FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

P304

10923-10927

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scholarly article

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10.1073/PNAS.93.20.10923

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20

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93

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1996-10-01T00:00:00Z

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14350723

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P698

8855284

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P921

apoptotic process

P932

38259

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