Results 271 to 280 of about 288,899 (312)
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Apoptotic and necrotic cell death induced by death domain receptors
Cellular and Molecular Life Sciences, 2001Apoptosis and necrosis are two distinct forms of cell death. Caspases are indispensable as initiators and effectors of apoptotic cell death and are involved in many of the morphological and biochemical features of apoptosis. Major changes in mitochondrial membrane integrity and release of proapoptotic factors, such as cytochrome c from the ...
G, Denecker +3 more
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A death-domain-containing receptor that mediates apoptosis
Nature, 1996The cell-killing effects of the cytokines TNF-alpha and FasL are mediated by the distinct cell-surface receptors TNFR1, TNFR2 and Fas (also known as CD95/APO-1), which are all members of a receptor superfamily that is important for regulating cell survival.
J, Kitson +8 more
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An Antagonist Decoy Receptor and a Death Domain-Containing Receptor for TRAIL
Science, 1997TRAIL, also called Apo2L, is a cytotoxic protein that induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain–containing receptor, DR4, is expressed on both cell types. An antagonist decoy receptor (designated as TRID for TRAIL receptor without an intracellular domain) that may explain the resistant ...
G, Pan +5 more
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Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains
Nature, 2013The tumour necrosis factor (TNF) family is crucial for immune homeostasis, cell death and inflammation. These cytokines are recognized by members of the TNF receptor (TNFR) family of death receptors, including TNFR1 and TNFR2, and FAS and TNF-related apoptosis-inducing ligand (TRAIL) receptors.
Shan, Li +11 more
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Role of NMDA receptor functional domains in excitatory cell death
Neuropharmacology, 2000The mechanisms by which the NMDA receptor (NMDAR) induces excitotoxicity were investigated using a novel assay. We quantitated the capacity of wild type and mutant receptors for cell killing in CHO cells and cultured cortical neurons by measuring the activity of a co-transfected firefly luciferase expression plasmid.
G A, Rameau +3 more
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International Journal of Biological Macromolecules, 2023
p75 neurotrophin receptor (p75NTR) contains a C-terminal globular protein module known as the death domain (DD), which plays a central role in apoptotic and inflammatory signaling through the formation of oligomeric protein complexes. A monomeric state of the p75NTR-DD also exists depending on its chemical environment in vitro.
Zhen, Li +9 more
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p75 neurotrophin receptor (p75NTR) contains a C-terminal globular protein module known as the death domain (DD), which plays a central role in apoptotic and inflammatory signaling through the formation of oligomeric protein complexes. A monomeric state of the p75NTR-DD also exists depending on its chemical environment in vitro.
Zhen, Li +9 more
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Solution structure of the tumor necrosis factor receptor-1 death domain
Journal of Molecular Biology, 2001Tumor necrosis factor receptor-1 death domain (TNFR-1 DD) is the intracellular functional domain responsible for the receptor signaling activities. The solution structure of the R347K mutant of TNFR-1 DD was solved by NMR spectroscopy. A total of 20 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of ...
S F, Sukits +5 more
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Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains
Science, 1999Tumor necrosis factor receptor type 1 (TNF-R1) contains a cytoplasmic death domain that is required for the signaling of TNF activities such as apoptosis and nuclear factor kappa B (NF-κB) activation. Normally, these signals are generated only after TNF-induced receptor aggregation.
Y, Jiang +3 more
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Biochemical and Biophysical Research Communications, 2002
Caspase-8 and -10 are thought to be involved in a signaling pathway leading to death receptor-mediated apoptosis. The prodomains of these caspases are known to form fibrous structures in the perinuclear region when overexpressed, though the meaning of the structures remains unclear.
Yoshiaki, Shikama +5 more
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Caspase-8 and -10 are thought to be involved in a signaling pathway leading to death receptor-mediated apoptosis. The prodomains of these caspases are known to form fibrous structures in the perinuclear region when overexpressed, though the meaning of the structures remains unclear.
Yoshiaki, Shikama +5 more
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Biochemical and Biophysical Research Communications, 2006
FLASH protein is a component of death-inducing signaling complex and might be involved in death receptor-mediated extrinsic apoptosis. Here we developed the peptide aptamer against death effecter domain recruiting domain (DRD) of FLASH protein and showed that the peptide bound to FLASH protein in vitro.
Gab Seok, Kim +6 more
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FLASH protein is a component of death-inducing signaling complex and might be involved in death receptor-mediated extrinsic apoptosis. Here we developed the peptide aptamer against death effecter domain recruiting domain (DRD) of FLASH protein and showed that the peptide bound to FLASH protein in vitro.
Gab Seok, Kim +6 more
openaire +2 more sources

