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hepatitis B virus (HBV) X protein (HBx) restricts TNFSF10 (show TNFSF10 ELISA Kits) receptor signaling via macroautophagy/autophagy-mediated degradation of TNFRSF10B/DR5, a TNFSF10 (show TNFSF10 ELISA Kits) death receptor.
Results show that downregulation of DR4 and DR5 by SLC26A2 (show SLC26A2 ELISA Kits) confers resistance to TRAIL.
Study provides direct biophysical evidence that Death Receptor 5 disulfide-linked transmembrane (TM)-dimers open in response to ligand binding. Then, to probe the importance of the closed-to-open TM domain transition in the overall energetics of receptor activation, point-mutants (alanine to phenylalanine) in the predicted, tightly packed TM domain dimer interface were designed and tested.
High-order TRAIL oligomer formation in TRAIL-coated lipid nanoparticles enhances DR5 cross-linking and increases antitumour effect against colon cancer cells and xenograft tumors.
Oridonin analog CYD (show CYBB ELISA Kits)-6-28 induces apoptosis at least partially by inducing the expression of death receptor 5 in breast neoplasms.
The authors show that cholesterol is necessary for the covalent dimerization of DR5 transmembrane domains.
Mono treatment with lexatumumab was not sufficient to induce apoptosis in pancreatic cancer cells, whereas focal adhesion kinase inhibitor PF573228 significantly sensitized lexatumumab-induced apoptosis. Western blotting analysis revealed that lexatumumab and PF573228 combination treatment increased death receptor 5 but decreased Bcl-xL (show BCL2L1 ELISA Kits) expression.
We demonstrate that PBOX-15 can enhance TRAIL-induced apoptosis by upregulation of DR5, reduction of cellular mitochondrial potential, activation of the caspase (show CASP3 ELISA Kits) cascade and downregulation of PI3K (show PIK3CA ELISA Kits)/Akt (show AKT1 ELISA Kits), c-FLIP (show CFLAR ELISA Kits), Mcl-1 (show MCL1 ELISA Kits) and IAP (show ALPI ELISA Kits) survival pathways
The nanovectorization of TRAIL enhanced its binding to both DR4 and DR5 receptors at 37 degrees C and could potentially sensitized cancer cells to TRAIL induced apoptosis through simultaneous activation of DR4 and DR5 as described in this paper for the non-small lung carcinoma cell line (H1703), the two hepatocarcinoma cell lines (SK-Hep1, HUH) and the colon carcinoma cell line (HCT116WT).
we found that CQ decreased the expression of Cbl (show CBL ELISA Kits), an E3 ligase of DR5, and knock-down of Cbl (show CBL ELISA Kits) markedly enhanced DR5 up-regulation. Other lysosomal inhibitors, including monensin and nigericin, also up-regulated DR5 and sensitized TRAIL-mediated apoptosis
Death receptor5 pathway and mitochondrial pathway, which are likely mediated by HIF-1alpha (show HIF1A ELISA Kits), contribute to hypoxia-induced spermatocyte apoptosis.
Authors demonstrate, for the first time, expression of TNF-related apoptosis-inducing ligand (TRAIL (show TNFSF10 ELISA Kits)) and its signaling death receptor 5 (DR5) in the murine inner ear.
Malignant transformation in the endometrium is related to reduction of membrane DR4 and DR5 expression.
TRAIL expression by osteoclast-like cells is increased in the presence of RANKL (show TNFSF11 ELISA Kits) and after scraping; DcR2 (show TNFRSF10D ELISA Kits) expression peaks at 24 hours, and and decreases at 5 days; DR5 expression peaks at 5 days
Induction of death receptor 5 expression in tumor vasculature by perifosine restores the vascular disruption activity of TRAIL-expressing CD34 (show CD34 ELISA Kits)(+) cells.
TRAIL-DR5 interaction promoted malignant behaviors of B16F10 cells.
results suggest that the transmembrane domains together with their adjacent stalk regions can play a major role in control of death receptor activation thereby contributing to cell type specific differences in TRAILR1 and TRAILR2 signaling
DR5 is selectively expressed by neuroprogenitor cells and newborn neurons.
Results suggest that excessive iodine could induce TRAIL and DR5 abnormal expression in thyroid. TRAIL band with DR5 to promote follicular cells apoptosis thus mediate thyroid destruction in EAT.
NK cells inhibit dendritic cell cross-priming, but not direct priming, in a TRAIL/DR5-dependent manner.
The protein encoded by this gene is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces an apoptosis signal. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. Two transcript variants encoding different isoforms and one non-coding transcript have been found for this gene.
tumor necrosis factor receptor superfamily, member 10b
, death receptor-M2
, death receptor-M1
, Fas-like protein
, TNF-related apoptosis-inducing ligand receptor 2
, apoptosis inducing protein TRICK2A/2B
, apoptosis inducing receptor TRAIL-R2
, cytotoxic TRAIL receptor-2
, death domain containing receptor for TRAIL/Apo-2L
, death receptor 5
, p53-regulated DNA damage-inducible cell death receptor(killer)
, tumor necrosis factor receptor superfamily member 10B
, tumor necrosis factor receptor-like protein ZTNFR9
, KILLER/DR5 TRAIL death-inducing receptor