Results 81 to 90 of about 105,381 (168)
Conservation of post‐translational modifications (PTMs) in histones across six plant species.
Sau‐Shan Cheng +3 more
wiley +1 more source
Reciprocal control of viral infection and phosphoinositide dynamics
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
Specificity of DNA ADP-Ribosylation Reversal by NADARs
Recent discoveries establish DNA and RNA as bona fide substrates for ADP-ribosylation. NADAR (“NAD- and ADP-ribose”-associated) enzymes reverse guanine ADP-ribosylation and serve as antitoxins in the DarT-NADAR operon.
Bara Cihlova +4 more
doaj +1 more source
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho +3 more
wiley +1 more source
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
wiley +1 more source
Cell fate regulation by chromatin ADP-ribosylation
ADP-ribosylation is an evolutionarily conserved complex posttranslational modification that alters protein function and/or interaction. Intracellularly, it is mainly catalyzed by diphtheria toxin-like ADP-ribosyltransferases (ARTDs), which attach one or ...
Michael O. Hottiger +3 more
core +1 more source
The cell‐autonomous roles of interferon type 1 vary based on duration and intensity. While acute, robust signaling results in cancer cell cytotoxic effects, sustained, low‐level signaling is associated with tumor‐promoting effects. This review summarizes current research of IFN‐1 in cancer and within the clinical setting, with an emphasis on female ...
Ashlyn Conant +7 more
wiley +1 more source
ADP-ribosylation is a ubiquitous post-translational addition of either monomers or polymers of ADP-ribose to target proteins by ADP-ribosyltransferases, usually by interferon-inducible diphtheria toxin-like enzymes known as PARPs.
Matthew E Grunewald +9 more
doaj +1 more source
Radiotherapy triggers LTβR N‐glycosylation, enhancing its overall protein stability and nuclear retention. This accumulation drives TRIM28‐mediated PCBP2 SUMOylation, suppressing pyroptosis and conferring gastric cancer radioresistance. Therapeutically, a targeted nanoplatform (cRGD‐Lipo@EMD) effectively disrupts this regulatory axis, offering a highly
Weijie Zang +8 more
wiley +1 more source
ADP-ribosylation factors (ARFs) comprise a family of ∼20 kDa guanine nucleotide-binding proteins that were discovered as one of several cofactors required in cholera toxin-catalyzed ADP-ribosylation of Gsα, the guanine nucleotide-binding protein ...
Moss, Joel +6 more
core +1 more source

