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The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia.
at normal levels of expression during bacterial infection, NleB1/NleB(CR) antagonizes death receptor-induced apoptosis of infected cells by modifying FADD in an irreversible manner.
Caspase-8 can serve in two distinct roles in response to TRAIL receptor engagement, as a scaffold for assembly of a Caspase-8-FADD-RIPK1 "FADDosome" complex, leading to NFkappaB-dependent inflammation, or as a protease that promotes apoptosis.
Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 (show CASP8 ELISA Kits) and the distinct mechanisms of regulation by cFLIP (show CFLAR ELISA Kits) and MC159 through comingling and capping, respectively.
This study reveals an essential role of SUMOylated FADD in Drp1 (show CRMP1 ELISA Kits)- and caspase-10 (show CASP10 ELISA Kits)-dependent necrosis.
In myelodysplastic syndrome, FADD expression is regulated by SPAG6 (show SPAG6 ELISA Kits) which influences its interaction with TRAIL death receptors.
High levels of FADD and caspase-8 (show CASP8 ELISA Kits), but not caspase-3 (show CASP3 ELISA Kits), were associated with increased incidence of coronary events in subjects from the general population.
Both Fas associated via death domain gene copy number amplification and high protein expression were significantly associated with lymph node metastasis and had the shortest disease-free survival and overall survival.
FADD, as well as NEMO (show IKBKG ELISA Kits), is a substrate for LUBAC ubiquitin ligase (E3) complex, composed of the HOIP (show RNF31 ELISA Kits), HOIL-1L (show RBCK1 ELISA Kits), and SHARPIN (show SHARPIN ELISA Kits) subunits.
autoinflammation-associated H443P nlrc4 (show NLRC4 ELISA Kits) mutant is altered in interaction with SUG1 (show PSMC5 ELISA Kits) and ubiquitinated proteins, triggering constitutive caspase-8 (show CASP8 ELISA Kits)-mediated cell death dependent on FADD but independent of Ser (show SIGLEC1 ELISA Kits)(533) phosphorylation.
The authors conclude that FADD is a master regulator of glucose and fat metabolism.
Mice deficient in RIPK3 (show RIPK3 ELISA Kits) or doubly deficient in MLKL and FADD, but not MLKL alone, are more susceptible to influenza A virus than their wild-type counterparts, revealing an important role for RIPK3 (show RIPK3 ELISA Kits)-mediated apoptosis in antiviral immunity.
Wild-type cells can execute apoptosis via both, the mitochondrial and the receptor-mediated pathway whereas FADD-deficient cells can only activate the intrinsic pathway. There is a difference in UVC radiation response between two cell lines indicating the role of FADD in the selection of cell death modality.
knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS (show ROS1 ELISA Kits) accompanied by JNK1 (show MAPK8 ELISA Kits) activation to substantiate apoptosis.
A20 targets caspase-8 and FADD to protect HTLV-I-infected cells.
Deletion of FADD in macrophages and granulocytes results in RIP3 (show MPRIP ELISA Kits)- and MyD88 (show MYD88 ELISA Kits)-dependent systemic inflammation.
A constitutively phosphoryl-mimicking mutation of Fas (show FAS ELISA Kits)-associated death domain (FADD-D) enhances Notch-1 (show NOTCH1 ELISA Kits) signaling and compromises Wnt (show WNT2 ELISA Kits) signaling in both cultured myoblasts and regenerating muscles.
Beta amyloid-induced upregulation of death receptor 6 (show TNFRSF21 ELISA Kits) accelerates the toxic effect of N-terminal fragment of amyloid precursor protein (show APP ELISA Kits)
Phosphorylation of FADD by the kinase CK1alpha (show CSNK1A1 ELISA Kits) promotes KRASG12D-induced lung cancer.
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
, Fas (TNFRSF6)-associated via death domain
, Fas associated via death domain S homeolog