RIP3, a novel apoptosis-inducing kinase (Q22009930)

protein modification process

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

X Sun

Sun

1 reference

7 February 2023

J Lee

Lee

1 reference

7 February 2023

T Navas

Navas

1 reference

7 February 2023

D T Baldwin

D T

Baldwin

1 reference

7 February 2023

T A Stewart

T A

Stewart

1 reference

7 February 2023

V M Dixit

V M

Dixit

1 reference

Journal of Biological Chemistry

7 February 2023

language of work or name

English

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publication date

11 June 1999

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published in

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volume

274

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issue

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page(s)

16871-5

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

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

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

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

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An induced proximity model for caspase-8 activation.

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FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis

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Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1

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RAIDD is a new 'death' adaptor molecule

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Defects in regulation of apoptosis in caspase-2-deficient mice

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

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TRAF2-mediated activation of NF-kappa B by TNF receptor 2 and CD40

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Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice

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

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The death domain kinase RIP mediates the TNF-induced NF-kappaB signal

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

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RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase

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Identification of CARDIAK, a RIP-like kinase that associates with caspase-1

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RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis

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The CARD domain: a new apoptotic signalling motif

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Neutralization of the AIDS retrovirus by antibodies to a recombinant envelope glycoprotein

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44 Use of degenerate oligonucleotide probes to identify clones that encode protein kinases

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TRAF6 is a signal transducer for interleukin-1

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TRAF2 is essential for JNK but not NF-kappaB activation and regulates lymphocyte proliferation and survival

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