The PYRIN domain: a member of the death domain-fold superfamily (Q24644648)

1

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N C Gordon

2

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E W Humke

3

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K M O'Rourke

4

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M A Starovasnik

5

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J P Yin

6

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V M Dixit

Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins

7

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language of work or name

English

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publication date

September 2001

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published in

Protein Science

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volume

10

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issue

9

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page(s)

1911-8

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cites work

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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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7 April 2017

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Three-dimensional structure of a complex between the death domains of Pelle and Tube

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Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment

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7 April 2017

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7 April 2017

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The PYRIN domain: a novel motif found in apoptosis and inflammation proteins

7 April 2017

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The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation

7 April 2017

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Activation of a caspase-9-mediated apoptotic pathway by subcellular redistribution of the novel caspase recruitment domain protein TMS1

7 April 2017

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TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers

7 April 2017

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Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB

7 April 2017

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7 April 2017

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PubMed

https://pubmed.ncbi.nlm.nih.gov/11514682

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Protein folds from pair interactions: a blind test in fold recognition

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/11514682

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1110/PS.13801

1 reference

1 reference

1 reference

PubMed publication ID

11514682

1 reference