Identification of CARDIAK, a RIP-like kinase that associates with caspase-1 (Q24324244)

GOA release 2020-03-11

inflammatory response

1 reference

GOA release 2020-03-11

7

J Tschopp

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author name string

M Thome

1

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K Hofmann

2

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K Burns

3

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F Martinon

4

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J L Bodmer

5

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C Mattmann

The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death

6

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language of work or name

English

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publication date

16 July 1998

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published in

Current Biology

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volume

8

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page(s)

885-8

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issue

15

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cites work

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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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RAIDD is a new 'death' adaptor molecule

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The CARD domain: a new apoptotic signalling motif

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A flexible motif search technique based on generalized profiles.

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The Dominant W 42 Spotting Phenotype Results from a Missense Mutation in the c- kit Receptor Kinase

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A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor

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

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

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Ligation of CD40 activates interleukin 1beta-converting enzyme (caspase-1) activity in vascular smooth muscle and endothelial cells and promotes elaboration of active interleukin 1beta

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Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex

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MyD88, an adapter protein involved in interleukin-1 signaling

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TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and Fas(Apo-1/CD95)

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The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1

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