Caspase Activation and Recruitment Domain

Known as: Recruitment Domains, Caspase, Caspase Activation and Recruitment Domains, CARD Domain 
A homotypic protein interaction module of the death domain superfamily. It is composed of a bundle of six alpha-helices that is related in sequence… (More)
National Institutes of Health

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2 relations
aspects of radiation effectsphysiological aspects

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Highly Cited
2007
Highly Cited
2007
Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2.
RIG-I is an RNA helicase containing caspase activation and recruitment domains (CARDs). RNA binding and signaling by RIG-I are… (More)
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2007
2007
Crystal structure of the Nod1 caspase activation and recruitment domain.
Nod-like receptors (NLRs), Nod1 and Nod2 are cytosolic detectors of pathogen-associated molecular patterns (PAMPs). Nod1 is a… (More)
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Highly Cited
2004
Highly Cited
2004
The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
Intracellular double-stranded RNA (dsRNA) is a chief sign of replication for many viruses. Host mechanisms detect the dsRNA and… (More)
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Highly Cited
2004
Highly Cited
2004
Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation.
Myocardial ischemia/reperfusion (I/R) is associated with an extensive loss of myocardial cells. The apoptosis repressor with… (More)
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Highly Cited
2003
Highly Cited
2003
Apoptosis-associated speck-like protein containing a caspase recruitment domain is a regulator of procaspase-1 activation.
Apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC)/target of methylation-induced silencing… (More)
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Highly Cited
2001
Highly Cited
2001
Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB.
Apaf-1 and Nod1 are members of a protein family, each of which contains a caspase recruitment domain (CARD) linked to a… (More)
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Highly Cited
2001
Highly Cited
2001
CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B.
The caspase recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins into… (More)
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Highly Cited
2000
Highly Cited
2000
TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers.
Gene silencing associated with aberrant methylation of promoter region CpG islands is an acquired epigenetic alteration that… (More)
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Highly Cited
1999
Highly Cited
1999
Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)
Mucosa-associated lymphoid tissue (MALT) lymphomas most frequently involve the gastrointestinal tract and are the most common… (More)
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Highly Cited
1998
Highly Cited
1998
Solution Structure of the RAIDD CARD and Model for CARD/CARD Interaction in Caspase-2 and Caspase-9 Recruitment
Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs… (More)
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