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Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD (show PIDD Antibodies) and caspase-2 (show CASP2 Antibodies) to initiate apoptosis
The megalencephaly, lissencephaly variant, and intellectual disability associated with loss of CRADD/caspase-2 (show CASP2 Antibodies)-mediated apoptosis imply a role for CRADD/caspase-2 (show CASP2 Antibodies) signaling in development of the human cerebral cortex.
The adaptor molecule RAIDD coordinates IKKepsilon (show IKBKE Antibodies) and IRF7 (show IRF7 Antibodies) interaction to ensure efficient expression of type I interferon (show IFNA Antibodies).
define a novel function for CRADD in endothelial cells as an inducible suppressor of BCL10, a key mediator of responses to proinflammatory agonists
Study identified sequence variants in the known disease-causing genes SLC6A3 (show SLC6A3 Antibodies) and FLVCR1 (show FLVCR1 Antibodies), and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6 (show TUBGCP6 Antibodies), BRAT1 (show C7orf27 Antibodies), SNIP1 (show SNIP1 Antibodies), CRADD, and HARS (show HARS Antibodies).
point mutations on RAIDD (R147E) and on PIDD (show PIDD Antibodies) (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed
The expressions of PIDD (show PIDD Antibodies) and RAIDD are upregulated during tumour progression in renal cell carcinomas.
As a first step towards elucidating the molecular mechanisms of caspase-2 (show CASP2 Antibodies) activation, data report the crystal structure of the RAIDD death domain at 2.0 A resolution.
PIDD (show PIDD Antibodies) death domain (DD) and RAIDD DD assemble into an oligomeric complex. Within the PIDDosome, the interaction between PIDD (show PIDD Antibodies) and RAIDD is mediated by a homotypic interaction between their death domains.
impaired expression of RAIDD in drug induced apoptosis may play a role in the multidrug resistance of osteosarcoma cells
The tumor-modulatory effects of Caspase-2 (show CASP2 Antibodies) and Pidd1 do not require the scaffold protein (show HOMER1 Antibodies) Raidd
Neuronal caspase-2 (show CASP2 Antibodies)-dependent execution of neurons requires recptor-interacting protein RAIDD, not p53-inducible protein with a death domain (PIDD (show PIDD Antibodies)).
We show that CRADD interacts with BCL10 (show BCL10 Antibodies) through its caspase (show CASP3 Antibodies) recruitment domain and suppresses interactions between BCL10 (show BCL10 Antibodies) and CARMA1 (show CARD11 Antibodies)
Overexpression of Raidd cDNA in 3T3L1 cells inhibited differentiation of the preadipocytes.
P53-induced protein with a death domain (show PIDD Antibodies) -induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP (show RIPK1 Antibodies))-associated ICH-1 (show CASP2 Antibodies)/CED-3 homologous protein with a death domain (RAIDD).
The protein encoded by this gene is a death domain (CARD/DD)-containing protein and has been shown to induce cell apoptosis. Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes tumor necrosis factor receptor 1 (TNFR1A), RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.
death domain-containing protein CRADD
, CASP2 and RIPK1 domain containing adaptor with death domain
, Death domain-containing protein CRADD
, death domain-containing protein cradd
, CASP2 and RIPK1 domain containing adaptor with death, gene 2
, RIP-associated ICH1/CED3-homologous protein with death domain
, RIP-associated protein with a death domain
, caspase and RIP adaptor with death domain
, death adaptor molecule RAIDD
, CASP2 and RIPK1 domain-containing adaptor with death domain
, caspase and RIP adapter with death domain