Results 61 to 70 of about 292,990 (265)
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
Activation of an atypical plant NLR with an N-terminal deletion initiates cell death at the vacuole
EMBO ReportsPlants evolve nucleotide-binding leucine-rich repeat receptors (NLRs) to induce immunity. Activated coiled-coil (CC) domain containing NLRs (CNLs) oligomerize and form apparent cation channels promoting calcium influx and cell death, with the alpha-1 ...
Sruthi Sunil +15 more
doaj +1 more source
The Role of Necroptosis in Cardiovascular Disease
Frontiers in Pharmacology, 2018 A newly discovered mechanism of cell death, programmed necrosis (necroptosis), combines features of both necrosis and apoptosis. Necroptosis is tightly modulated by a series of characteristic signaling pathways. Activating necroptosis by ligands of death
Shi Zhe-Wei, Ge Li-Sha, Li Yue-Chun
doaj +1 more source
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 +2 more
wiley +1 more source
NLRC5, AT THE HEART OF ANTIGEN PRESENTATION
Frontiers in Immunology, 2013 Nucleotide-binding domain and leucine-rich repeat containing receptors (NLRs) are intracellular proteins mainly involved in pathogen recognition, inflammatory responses, and cell death.
Andreas eNeerincx +3 more
doaj +1 more source
Identification and functional characterization of DR6, a novel death domain‐containing TNF receptor [PDF]
FEBS Letters, 1998 Tumor nectosis factor (TNF) receptors are key players in inflammation and immune regulation. A new member of this family, termed death receptor‐6 (DR6), has been identified. Like other death receptors, DR6 is a type I transmembrane receptor, possesses four extracellular cysteine‐rich motifs and a cytoplasmic death domain. DR6 is expressed in most human
Pan, Guohua +9 more
openaire +3 more sources
FEBS Letters, EarlyView.Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley +1 more source
The Fas–FADD death domain complex structure unravels signalling by receptor clustering [PDF]
Nature, 2008 The death inducing signalling complex (DISC) formed by Fas receptor, FADD (Fas-associated death domain protein) and caspase 8 is a pivotal trigger of apoptosis. The Fas-FADD DISC represents a receptor platform, which once assembled initiates the induction of programmed cell death.
Scott, Fiona L. +9 more
openaire +2 more sources
FEBS Letters, EarlyView.Embryo‐like structures (stembryos) are an innovative tool, but they are hindered by experimental variability and limited developmental potential. DNA methylation is crucial for mammalian development, but its status in stembryo models is poorly characterized.
Sara Canil +4 more
wiley +1 more source
Cell Death DiscoveryUltraviolet B (UVB) is recognized for inducing inflammation and death of keratinocytes through the activation of death receptors and pattern recognition receptors (PRRs).
Tairan Hu +9 more
doaj +1 more source