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Human FADD Protein expressed in Escherichia coli (E. coli) - ABIN667076
Tourneur, Buzyn, Chiocchia: FADD adaptor in cancer. in Medical immunology (London, England) 2005
Show all 2 references for ABIN667076
Human FADD Protein expressed in Wheat germ - ABIN1353355
García-Fuster, Ramos-Miguel, Miralles, García-Sevilla et al.: Opioid receptor agonists enhance the phosphorylation state of Fas-associated death domain (FADD) protein in the rat brain: functional interactions with casein kinase Ialpha, Galpha(i) proteins, and ... in Neuropharmacology 2008
A20 targets caspase-8 and FADD to protect HTLV-I-infected cells.
TCGA analysis showed that ANO1 and FADD, located at 11q13, were co-expressed at transcript level and significantly associated with overall and disease-free survival
Data (including data obtained in transgenic mice) suggest FADD is key in genesis of neural tube defects in pups of diabetic mice; unfolded protein response/endoplasmic reticulum stress was prevented by over-expression of human dominant negative FADD.
multifaceted kinase, CK2, phosphorylates FADD and is involved in its sub-cellular localization.
domains of calmodulin (show CALM1 Proteins) mediate FADD and TRADD (show TRADD Proteins) interaction
The gene expression analysis showed statistically significant difference between cases and healthy controls for both FADD (p<0.02) and FAS (show FAS Proteins) (p<0.007) genes
Observed upregulation of cortical p-194 FADD and p-FADD/FADD ratio (higher pro-survival index) in major depression; could play a major role to counteract the known activation of the intrinsic (mitochondrial) apoptotic pathway in the brain
FADD death effector domain and c-FLIP (show CFLAR Proteins) death effector domain structures, the binding activity of FADD DED (show AATF Proteins) to the c-FLIP (show CFLAR Proteins) death effector domains, and the protein-protein interactions involving the regulation of both apoptosis and necrosis.
The genotype of the promoter SNP (rs10898853) of FADD was found to be significantly associated with papillary thyroid cancer in a South Korean case control study.
These results indicate that FADD, as a host pro-apoptotic protein, plays important roles in regulating HIV-1 replication and production in several ways, and apoptotic pathway inhibition is able to decrease HIV-1 replication and production
Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88 (show MYD88 Proteins)-dependent systemic inflammation.
A constitutively phosphoryl-mimicking mutation of Fas (show FAS Proteins)-associated death domain (FADD-D) enhances Notch-1 (show NOTCH1 Proteins) signaling and compromises Wnt (show WNT2 Proteins) signaling in both cultured myoblasts and regenerating muscles.
Beta amyloid-induced upregulation of death receptor 6 (show TNFRSF21 Proteins) accelerates the toxic effect of N-terminal fragment of amyloid precursor protein (show APP Proteins)
Phosphorylation of FADD by the kinase CK1alpha (show CSNK1A1 Proteins) promotes KRASG12D-induced lung cancer.
This study evaluated the role of FADD in pancreatic islets and insulin (show INS Proteins) secretion.
depletion of alphaNAC in multiple types of cancer cells induce typical apoptotic cell death. This anti-apoptotic function is mediated by the FADD/c-Jun N-terminal kinase pathway.
These data suggest that as a death receptor, FADD is also required for cell survival in beta-selection as a regulator of Notch1 (show NOTCH1 Proteins) expression.
using T-cell specific deletion mice, we observed that FADD deficiency in thymocytes led to increased apoptosis and reduced cell numbers, which may be attributed to the reduction of Glut1 (show SLC2A1 Proteins) expression and correspondingly decreased glucose uptake
RIPK1 (show RIPK1 Proteins), FADD, and caspase-8 (show CASP8 Proteins) are required for YopJ-induced cell death and caspase-1 (show CASP1 Proteins) activation
FADD induces apoptosis
mapping and sequencing of bovine FADD cDNA, and characterization of its expression in endothelial cells
The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development.
Fas-associating death domain-containing protein
, Fas-associating protein with death domain
, growth-inhibiting gene 3 protein
, mediator of receptor induced toxicity
, mediator of receptor-induced toxicity
, protein FADD
, FAS-associated death domain protein
, FAS-associating death domain-containing protein
, Fas (TNF receptor superfamily, member 6)
, Fas-associated via death domain