Results 281 to 290 of about 288,899 (312)

Soluble Extracellular Domain of Death Receptor 5 Inhibits TRAIL-Induced Apoptosis by Disrupting Receptor–Receptor Interactions

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, Chih Hung, Lo, Benjamin D, Grant, David D, Thomas, Jonathan N, Sachs   +4 more
openaire   +2 more sources

The role of neurotransmission and the Chopper domain in p75 neurotrophin receptor death signaling

2004
The 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., Reid, K. M., Shipham, K. M., Morley, S. N., Kilpatrick, T. J., Bartlett, P. F.   +5 more
openaire   +4 more sources

Heterologous Production of Death Ligands’ and Death Receptors’ Extracellular Domains: Structural Features and Efficient Systems

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 ...
openaire   +2 more sources

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, 1998
Apoptotic 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
openaire   +1 more source

PLAIDD,a Type II Death Domain Protein that Interacts with p75 Neurotrophin Receptor

NeuroMolecular Medicine, 2002
We describe the cloning and characterization of a rat single transmembrane protein that is homologous to the common neurotrophin receptor p75NTR in its death domain and the transmembrane region but dissimilar outside these regions. We have dubbed this protein PLAIDD, for p75-like apoptosis-inducing death domain protein.
Harald, Frankowski, Susana, Castro-Obregon, Gabriel, del Rio, Rammohan V, Rao, Dale E, Bredesen   +4 more
openaire   +2 more sources

[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, 2004
To 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, Yan-xin, Liu, Shi-lian, Liu, De-xian, Zheng   +3 more
openaire   +1 more source

Induction of cell death by myristylated death domain of p55 TNF receptor is not abolished by Iprcg-like point mutation in death domain.

Journal of inflammation, 1997
We transiently expressed the intracellular domains of p55 TNF receptor (TNFR1) as either a cytosolic- or a membrane-associated form and examined their effects on the endogenous receptor-mediated gene expression as well as on cell viability. We found that gene expression as measured by luciferase activity under NF-kappa B-controlling elements was ...
C H, Kim, Y H, Song, K, Park, Y, Oh, T H, Lee   +4 more
openaire   +1 more source

A novel domain within the 55 kd TNF receptor signals cell death

Cell, 1993
Deletion mutagenesis of the intracellular region of the 55 kd TNF receptor (TNF-R1) identified an approximately 80 amino acid domain near the C-terminus responsible for signaling cytotoxicity. This domain shows weak homology with the intracellular domain of Fas antigen, a transmembrane polypeptide that can also initiate a signal for cytotoxicity ...
L A, Tartaglia, T M, Ayres, G H, Wong, D V, Goeddel   +3 more
openaire   +2 more sources

Structural Characterizations of the Fas Receptor and the Fas-Associated Protein with Death Domain Interactions

The Protein Journal, 2016
The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems.
openaire   +2 more sources

Death domain fold proteins in immune signaling and transcriptional regulation

FEBS Journal, 2022
Sun Hur
exaly