Results 41 to 50 of about 288,899 (312)

Expression of Silencer of Death Domains and Death-Receptor-3 in Normal Human Kidney and in Rejecting Renal Transplants [PDF]

The American Journal of Pathology, 2003
We have previously reported the pattern of cellular expression of tumor necrosis factor receptors (TNFR) in human kidney and their altered expression in transplant rejection. We have extended our studies to examine the expression of Silencer of Death Domains (SODD), a protein that binds to the cytoplasmic portion of TNFR1 to inhibit signaling in the ...
Rafia S, Al-Lamki, Jun, Wang, Sathia, Thiru, Nicholas R, Pritchard, J Andrew, Bradley, Jordan S, Pober, John R, Bradley   +6 more
openaire   +2 more sources

Reciprocal control of viral infection and phosphoinositide dynamics

FEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

The evolutionary conservation of the core components necessary for the extrinsic apoptotic signaling pathway, in Medaka fish

BMC Genomics, 2007
Background Death receptors on the cell surface and the interacting cytosolic molecules, adaptors and initiator caspases, are essential as core components of the extrinsic apoptotic signaling pathway.
Kominami Katsuya, Nozaki Masami, Sakamaki Kazuhiro, Satou Yutaka   +3 more
doaj   +1 more source

Death Domain Signaling by Disulfide-Linked Dimers of the p75 Neurotrophin Receptor Mediates Neuronal Death in the CNS [PDF]

The Journal of Neuroscience, 2016
The p75 neurotrophin receptor (p75 NTR ) mediates neuronal death in response to neural insults by activating a caspase apoptotic pathway. The oligomeric state and activation mechanism that enable p75 NTR to mediate these effects have recently been ...
Kazuhiro Tanaka, Claire E. Kelly, Ket Yin Goh, Kim Buay Lim, Carlos F. Ibáñez   +4 more
openaire   +3 more sources

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

FEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source

Fn14 and TNFR2 as regulators of cytotoxic TNFR1 signaling

Frontiers in Cell and Developmental Biology, 2023
Tumor necrosis factor (TNF) receptor 1 (TNFR1), TNFR2 and fibroblast growth factor-inducible 14 (Fn14) belong to the TNF receptor superfamily (TNFRSF). From a structural point of view, TNFR1 is a prototypic death domain (DD)-containing receptor.
Daniela Siegmund, Olena Zaitseva, Harald Wajant   +2 more
doaj   +1 more source

Fas-associated Protein with Death Domain (FADD)-independent Recruitment of c-FLIPL to Death Receptor 5 [PDF]

Journal of Biological Chemistry, 2004
Here we show a novel mechanism by which FLICE-like inhibitory protein (c-FLIP) regulates apoptosis induced by tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and one of its receptors, DR5. c-FLIP is a critical regulator of the TNF family of cytokine receptor signaling.
Tai-Guang, Jin, Alexei, Kurakin, Nordine, Benhaga, Karon, Abe, Mehrdad, Mohseni, Ferry, Sandra, Keli, Song, Brian K, Kay, Roya, Khosravi-Far   +8 more
openaire   +2 more sources

Apoptosis: Silencing the death receptors

, 1999
Spontaneous signaling from death-domain-containing receptors can result in inappropriate cell death. An inhibitory protein has recently been identified, called silencer of death domains (SODD), that binds to the death domain of tumor necrosis factor ...
Martinon, Fabio, Martinon, F., Hofmann, K., Tschopp, J., Hofmann, Kay, Jürg Tschopp, Kay Hofmann, Tschopp, Jürg, Fabio Martinon   +8 more
core   +1 more source

The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes

FEBS Letters, EarlyView.
Upon lysosomal rupture, an E3 ubiquitin ligase RNF115 translocates from the cytosol to the damaged lysosomal membrane. Moreover, RNF115 depletion impairs the clearance of damaged lysosomes, identifying it as a key regulator of lysosomal quality control.
Sae Nakanaga, Toshiki Takahashi, Akiko Kuma, Hiroyuki Kawahara   +3 more
wiley   +1 more source

Tumor Necrosis Factor Receptor 1 Is an ATPase Regulated by Silencer of Death Domain [PDF]

Molecular and Cellular Biology, 2002
Self-aggregation of tumor necrosis factor receptor type 1 (TNFR1) induces spontaneous downstream signaling and results in cell death. It has been suggested that silencer of death domain (SODD) binds TNFR1 monomers to prevent self-aggregation. We found that SODD binds through its BAG domain to the ATPase domain of Hsp70.
Kiyoshi, Miki, Edward M, Eddy
openaire   +2 more sources