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The megalencephaly, lissencephaly variant, and intellectual disability associated with loss of CRADD/caspase-2 (show CASP2 Proteins)-mediated apoptosis imply a role for CRADD/caspase-2 (show CASP2 Proteins) signaling in development of the human cerebral cortex.
The adaptor molecule RAIDD coordinates IKKepsilon (show IKBKE Proteins) and IRF7 (show IRF7 Proteins) interaction to ensure efficient expression of type I interferon (show IFNA Proteins).
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 Proteins) and FLVCR1 (show FLVCR1 Proteins), and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1 (show C7orf27 Proteins), SNIP1 (show SNIP1 Proteins), CRADD, and HARS (show HARS Proteins).
point mutations on RAIDD (R147E) and on PIDD (show PIDD Proteins) (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 Proteins) 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 Proteins) activation, data report the crystal structure of the RAIDD death domain at 2.0 A resolution.
PIDD (show PIDD Proteins) death domain (DD) and RAIDD DD assemble into an oligomeric complex. Within the PIDDosome, the interaction between PIDD (show PIDD Proteins) 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 Proteins) and Pidd1 do not require the scaffold protein (show HOMER1 Proteins) Raidd
Neuronal caspase-2 (show CASP2 Proteins)-dependent execution of neurons requires recptor-interacting protein RAIDD, not p53-inducible protein with a death domain (PIDD (show PIDD Proteins)).
We show that CRADD interacts with BCL10 (show BCL10 Proteins) through its caspase (show CASP3 Proteins) recruitment domain and suppresses interactions between BCL10 (show BCL10 Proteins) and CARMA1 (show CARD11 Proteins)
Overexpression of Raidd cDNA in 3T3L1 cells inhibited differentiation of the preadipocytes.
P53-induced protein with a death domain (show PIDD Proteins) -induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP (show RIPK1 Proteins))-associated ICH-1 (show CASP2 Proteins)/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