(Q28300622)

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RAIDD is a new 'death' adaptor molecule

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RAIDD is a new 'death' adaptor molecule (English)

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main subject

CASP2 and RIPK1 domain containing adaptor with death domain

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stated in

GOA release 2020-03-11

apoptotic signaling pathway

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GOA release 2020-03-11

author name string

H Duan

series ordinal

1

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V M Dixit

series ordinal

2

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language of work or name

English

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publication date

2 January 1997

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published in

Nature

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volume

385

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issue

6611

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page(s)

86-9

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https://api.crossref.org/works/10.1038%2F385086A0

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ICE family proteases: mediators of all apoptotic cell death?

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Crossref

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

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Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death

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The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

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Genetic control of programmed cell death in the nematode C. elegans.

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7 January 2021

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Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities

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Contenders in FasL/TNF death signaling

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The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression

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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 general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

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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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7 January 2021

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Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product

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(Q28300622)

RAIDD is a new 'death' adaptor molecule

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