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Death Receptors and Apoptosis

Dermatologic Clinics, 2007
Interactions between death receptors from the tumor necrosis factor superfamily and their ligands play a crucial role in the development and the integrity of the epidermis. The major consequence resulting from death receptor targeting is apoptosis.
Contassot E, Gaide O, French LE
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Death receptors

Essays in Biochemistry, 2003
Death receptors [Fas/Apo-1/CD95, TNF-R1 [tumour necrosis factor (TNF) receptor 1], DR3 [death receptor 3], TRAIL-R1 [TNF-related apoptosis-inducing ligand receptor 1], TRAIL-R2, DR6, p75-NGFR [p75-nerve growth factor receptor], EDAR [ectodermal dysplasia receptor]] form a subgroup of the TNF-R superfamily that can induce apoptosis (programmed cell ...
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Death Receptors: Signaling and Modulation

Science, 1998
REVIEW Apoptosis is a cell suicide mechanism that enables metazoans to control cell number in tissues and to eliminate individual cells that threaten the animal's survival. Certain cells have unique sensors, termed death receptors, on their surface.
A, Ashkenazi, V M, Dixit
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Apoptosis induced by death receptors

Pharmaceutica Acta Helvetiae, 2000
Death receptors belong to the TNF receptor family and are characterised by an intracellular death domain that serves to recruit adapter proteins such as TRADD and FADD and cysteine proteases such as Caspase-8. Activation of Caspase-8 on the aggregated receptor leads to apoptosis. Triggering of death receptors is mediated through the binding of specific
Schneider P, Tschopp J
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Death Receptor Ligands in Tumors

Journal of Immunotherapy, 2002
Activation of apoptosis via death receptors is a tightly regulated event, and the death pathway itself is open to interference on the part of soluble or membrane-bound decoy receptors. The aggregation state of the death-inducing ligand is a crucial factor, particularly when these molecules are used as recombinant drugs against tumors.
Paola, Cappello   +3 more
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Targeting TRAIL death receptors

Current Opinion in Pharmacology, 2008
The natural occurring tumor necrosis factor related apoptosis-inducing ligand (TRAIL) induces apoptosis following binding to the two TRAIL death receptors (DRs). Its recombinant form and monoclonal antibodies against the TRAIL DRs induce cell death in a wide variety of tumor cell lines and xenografts without causing toxicity to normal cells and are ...
C N A M, Oldenhuis   +4 more
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Death Receptor 5 and Neuroproliferation

Cellular and Molecular Neurobiology, 2011
Tumor necrosis factor-related apoptosis-inducing ligand or Apo2 ligand is a member of the tumor necrosis factor superfamily of cytokines that induces apoptosis upon binding to its death domain-containing transmembrane receptors, death receptors 4 and 5 (DR4, DR5).
Yanli, Niu   +7 more
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Death Receptor Signaling and Autoimmunity

Immunologic Research, 2003
In recent years, it has become clear that self-nonself discrimination by the immune system is driven not so much by the specificities of the antigen receptors themselves, but by ligand-receptor systems that sense the presence of foreign pathogens (toll-like receptors) and those that regulate the balance between cellular proliferation and programmed ...
Richard M, Siegel   +4 more
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Homomeric and heteromeric interactions of the extracellular domains of death receptors and death decoy receptors

Biochemical and Biophysical Research Communications, 2005
Death receptors (DRs) can induce apoptosis by oligomerization with TRAIL, whereas death decoy receptors (DcRs) cannot, due to their lack of functional intracellular death domains. However, it is not known whether DRs and DcRs can interact with one another to form oligomeric complexes prior to TRAIL binding.
Hyun-Wook, Lee   +5 more
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Death receptor 3 mediates necroptotic cell death

Cellular and Molecular Life Sciences, 2016
Death receptor 3 (DR3) was initially identified as a T cell co-stimulatory and pro-inflammatory molecule, but further studies revealed a more complex role of DR3 and its ligand TL1A. Although being a death receptor, DR3 gained to date predominantly attention as a contributor to inflammation-driven diseases.
Sebastian Bittner   +2 more
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