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| http://dx.doi.org/10.3389/fcell.2023.1136992 | DOI Listing |
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Protein shapeshifting in necroptotic cell death signaling.
Trends Biochem Sci
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Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia; Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia. Electronic address:
Necroptosis is a mode of programmed cell death executed by the mixed lineage kinase domain-like (MLKL) pseudokinase following its activation by the upstream receptor-interacting protein kinase-3 (RIPK3), subsequent to activation of death, Toll-like, and pathogen receptors. The pathway originates in innate immunity, although interest has surged in therapeutically targeting necroptosis owing to its dysregulation in inflammatory diseases. Here, we explore how protein conformation and higher order assembly of the pathway effectors - Z-DNA-binding protein-1 (ZBP1), RIPK1, RIPK3, and MLKL - can be modulated by post-translational modifications, such as phosphorylation, ubiquitylation, and lipidation, and intermolecular interactions to tune activities and modulate necroptotic signaling flux.
View Article and Find Full Text PDFFunctional interaction of melatonin with gasotransmitters and ROS in plant adaptation to abiotic stresses.
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Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine.
Melatonin is considered a multifunctional stress metabolite and a novel plant hormone affecting seed germination, root architecture, circadian rhythms, leaf senescence, and fruit ripening. Melatonin functions related to plant adaptation to stress stimuli of various natures are considered especially important. One of the key components of melatonin's stress-protective action is its ability to neutralise reactive oxygen species (ROS) and reactive nitrogen species directly.
View Article and Find Full Text PDFEditorial: Community series in post-translational modifications of proteins in cancer immunity and immunotherapy, volume III.
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School of Pharmaceutical Science and Technology, Faculty of Medicine, Tianjin University, Tianjin, China.
Channel Gating in a Post-Translational Protein Translocase.
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Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, United States.
GalNT2-mediated O-glycosylation affects pancreas development and function in mice.
Sci Rep
November 2024
Department of General, Visceral and Thoracic Surgery, University Medical Center Hamburg-Eppendorf, 20246, Hamburg, Germany.
GALNT2, also known as polypeptide N-acetylgalactosaminyltransferase 2, is an enzyme that catalyzes the initial step of O-linked glycosylation, a crucial posttranslational modification that affects protein folding, stability, and function. Alterations in GALNT2 activity have been implicated in various diseases, such as cancer, metabolic disorders, and cardiovascular diseases, highlighting its importance in maintaining normal physiological functions. To investigate the impact of GalNT2 overexpression in vivo for the first time, we generated a conditional transgenic mouse line in which GalNT2 was expressed specifically in the pancreas.
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