Results 11 to 20 of about 105,192 (298)
FAS (Fas cell surface death receptor) [PDF]
CD95 (also known as Fas) is a death receptor that belongs to the TNF-receptor superfamily. Expressed at the cell surface as a homotrimer, this receptor implements both apoptotic and non-apoptotic signalling pathways. While the apoptotic signalling pathway is involved in tumor surveillance, peripheral tolerance and immune homeostasis (Strasser et al ...
Sanséau, Doriane, Legembre, Patrick
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FAS-dependent cell death in α-synuclein transgenic oligodendrocyte models of multiple system atrophy. [PDF]
Multiple system atrophy is a parkinsonian neurodegenerative disorder. It is cytopathologically characterized by accumulation of the protein p25α in cell bodies of oligodendrocytes followed by accumulation of aggregated α-synuclein in so-called glial ...
Christine L Kragh +12 more
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Viral double-stranded RNA (dsRNA) is recognised by pathogen recognition receptors such as Toll-Like Receptor 3 (TLR3) and retinoic acid inducible gene-I (RIG-I), and results in cytokine and interferon production. Fas, a well characterised death receptor,
Caitriona Lyons +4 more
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Fas death receptor signalling: roles of Bid and XIAP [PDF]
Fas (also called CD95 or APO-1), a member of a subgroup of the tumour necrosis factor receptor superfamily that contain an intracellular death domain, can initiate apoptosis signalling and has a critical role in the regulation of the immune system. Fas-induced apoptosis requires recruitment and activation of the initiator caspase, caspase-8 (in humans ...
Kaufmann T, Strasser A, Jost P J
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The Role of FAS Receptor Methylation in Osteosarcoma Metastasis. [PDF]
Osteosarcoma is the most frequent primary malignant bone tumor with an annual incidence of about 400 cases in the United States. Osteosarcoma primarily metastasizes to the lungs, where FAS ligand (FASL) is constitutively expressed. The interaction of FASL and its cell surface receptor, FAS, triggers apoptosis in normal cells; however, this function is ...
Sun JM +18 more
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The role of the Fas receptor in adipocyte metabolism [PDF]
Fas (FasR, CD95, Apo-1) is a member of the tumour necrosis receptor superfamily and plays a crucial role in the induction of apoptosis. In addition, depending on the cell type, activation of Fas can also induce non-apoptotic signalling pathways, including inflammation and proliferation.
Rapold, Reto Andreas
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Identification of the Calmodulin-Binding Domains of Fas Death Receptor
The extrinsic apoptotic pathway is initiated by binding of a Fas ligand to the ectodomain of the surface death receptor Fas protein. Subsequently, the intracellular death domain of Fas (FasDD) and that of the Fas-associated protein (FADD) interact to form the core of the death-inducing signaling complex (DISC), a crucial step for activation of caspases
Bliss J Chang +6 more
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Cholangiocarcinomas express fas ligand and disable the fas receptor [PDF]
Cholangiocarcinoma is a highly-malignant adenocarcinoma originating from cholangiocytes. Current concepts support escape from immune surveillance using aberrant expression of Fas ligand (FasL) and dysregulation of receptor (FasR) signaling as a potential mechanism for tumor progression.
F G, Que +6 more
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Requirement of Cysteine-rich Repeats of the Fas Receptor for Binding by the Fas Ligand [PDF]
The Fas receptor is a member of a family of cell death receptors, including tumor necrosis factor receptor I (TNFR I), death receptor 3 and 4 (DR3 and DR4), and cytopathic avian receptor 1 (CAR1). The Fas receptor is composed of several discrete domains, including three cysteine-rich domains (CRDs), a transmembrane domain, and an intracellular domain ...
J R, Orlinick +3 more
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A comparison of the cytoplasmic domains of the Fas receptor and the p75 neurotrophin receptor [PDF]
The p75 neurotrophic receptor (p75) shares structural features with the Fas receptor (FasR). Both receptors contain extracellular cysteine-rich repeats, a single transmembrane domain, and intracellular death domains. However, it has not been clearly established whether their death domains are equivalent in their ability to mediate apoptosis.
H, Kong +3 more
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