Results 251 to 260 of about 4,743,951 (299)
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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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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
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Death domain receptors and their role in cell demise.
Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, 1998Apoptotic signals are transduced by five death domain-containing receptors--TNFR1, Fas, DR3, DR4, and DR5--by binding to their ligands. The intracellular portion of all these receptors contains a region, approximately 80 amino acids long, referred to as the "death domain" (DD).
A, Singh, J, Ni, B B, Aggarwal
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The role of neurotransmission and the Chopper domain in p75 neurotrophin receptor death signaling
2004The role of p75 neurotrophin receptor (p75NTR) in mediating cell death is now well characterized, however, it is only recently that details of the death signaling pathway have become clearer. This review focuses on the importance of the juxtamembrane Chopper domain region of p75NTR in this process.
Coulson, E. +5 more
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Journal of Molecular Biology, 2017
Dysregulation of tumor necrosis factor (TNF) receptor signaling is a key feature of various inflammatory disorders. Current treatments for TNF-related diseases function either by sequestering ligand or blocking ligand-receptor interactions, which can cause dangerous side effects by inhibiting the receptors that are not involved in the disease condition.
Nagamani, Vunnam +4 more
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Dysregulation of tumor necrosis factor (TNF) receptor signaling is a key feature of various inflammatory disorders. Current treatments for TNF-related diseases function either by sequestering ligand or blocking ligand-receptor interactions, which can cause dangerous side effects by inhibiting the receptors that are not involved in the disease condition.
Nagamani, Vunnam +4 more
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Protein & Peptide Letters, 2012
The extracellular domains of death ligands and those of death receptors are closely related to many serious human diseases through the initiation of apoptosis. Recombinant production of the extracellular domains has been investigated due to demand for a large amount of purified samples, which are a prerequisite for their biochemical characterization ...
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The extracellular domains of death ligands and those of death receptors are closely related to many serious human diseases through the initiation of apoptosis. Recombinant production of the extracellular domains has been investigated due to demand for a large amount of purified samples, which are a prerequisite for their biochemical characterization ...
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[The primary study on a novel protein binding to the death domain of the death receptor 4].
Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae, 2004To clone and identify novel proteins binding to the death domain of the death receptor 4 (DR4).The yeast two-hybrid system was used for this study. Automatic sequencing was carried out for DNA sequencing. The sequence homology and the functional domains were analyzed by BLAST and the ScanProsite Tool softwares, respectively. Co-immunoprecipitate method
Xiao-ling, Li +3 more
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