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Proteomicsp-FADD-CD8+T cell axis determines hepatocellular carcinoma response to immune checkpoint inhibitors
The heterogenicity of hepatocellular carcinoma (HCC) remains a key obstacle in turning the majority of ‘immune-cold’ tumors ‘hot’ for effective immune checkpoint inhibitors (ICIs). Through analyzing the naturally-existed ‘hot’ HCC variants, we identified fas-associated death domain (FADD) as a key m...
ORGANISM(S): Homo sapiens (Human) 
2025-07-07 | PXD057519 | Pride
Hcc Fadd Hepg2 
ProteomicsA dual role for FADD in human T-cell lymphoblastic neo-plasms
In this study, we set out to get insight into the clinical implications of FADD expres-sion in T-cell lymphoblastic neoplasms, and to explore the landscape of deregulated cell signaling events in human T-cell lymphoblastic neoplasms, taking FADD expression as the defining variable.
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD037858 | Pride
Dia T-lbl Fadd 
ProteomicsFADD is a new protein secreted unconventionally following classical NLRP3 inflammasome activation
NLRP3 inflammasome assembles in response to stress or danger signals and leads to unconventional secretion of proinflammatory IL-1. FADD is an NLRP3 inflammasome component. Here we found that classical NLRP3 inflammasome activation in human monocytes/macrophages induced FADD secretion, which require...
ORGANISM(S): Homo sapiens (Human) 
2019-02-28 | PXD008168 | Pride
Human thp1 macrophages Fadd Nlrp3 inflammasome Rheumatoid arthritis Orbitrap fusion 
GenomicsCaspase-8 and FADD prevent spontaneous ZBP1 expression and necroptosis
Caspase-8 and FADD prevent spontaneous ZBP1 expression and necroptosis
PRJNA860938 | ENA
ProteomicsCryo-EM structural analysis of FADD: Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
Uncovering the molecular architecture of the core FADD:Caspase-8 complex and how this is altered by regulatory partners, such as the cell death inhibitor c-FLIP, is essential to understand co-ordination of cell fate. Here, using electron microscopy, we visualize for the first time fulllength proca...
ORGANISM(S): Homo sapiens (Human) 
2021-02-08 | PXD022408 | Pride
Caspase 8 Cell death. disc Fadd Em C-flip complex Structure 
GenomicsFADD Functions as an Oncogene in Chr11q13.3 Amplified Head and Neck Squamous Cell Carcinoma
FADD Functions as an Oncogene in Chr11q13.3 Amplified Head and Neck Squamous Cell Carcinoma
PRJNA1224430 | ENA
ProteomicsFADD is recruited to activated STING oligomers initiating caspase mediated NF-κB activation in Drosophila melanogaster
STING is an evolutionarily conserved key regulator of innate immunity. In mammals, STING activates two distinct signaling pathways, the IRF3 and the NF-κB pathways, which act in conjunction to drive antiviral immunity. While the molecular mechanism of STING-mediated IRF3 activation has been untangle...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2026-04-09 | PXD054811 | Pride
Co-ip ms Sting singaling Fadd Innate immunity Nf-κb Drosophila melanogaster 
TranscriptomicsCaspase-8 and FADD prevent spontaneous ZBP1 expression and necroptosis 
Caspase-8 and FADD play key roles in the regulation of cell death by necroptosis. The absence of either protein results in early embryonic lethality due to the activation of the kinase RIPK3 and its phosphorylation of the necroptosis executioner, MLKL. We genetically engineered and characterized a m...
ORGANISM(S): Mus musculus 
2022-09-19 | GSE208744 | GEO
ProteomicsNleB host targets - The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD)
The inhibition of host innate immunity pathways is essential for the survival of attaching and effacing (A/E) pathogens such as enteropathogenic Escherichia coli (EPEC) and Citrobacter rodentium during mammalian infections. To subvert these pathways, A/E pathogens utilize a type III secretion system...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Escherichia coli 
2017-09-11 | PXD006810 | Pride
Epec Nleb 
UnknownTumor-targeted delivery of a C-terminally truncated FADD (N-FADD) significantly suppresses the B16F10 melanoma via enhancing apoptosis.
Not available
S-EPMC5073321 | biostudies-literature
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