Results 41 to 50 of about 625,558 (252)
Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart [PDF]
, 2014 The α subunit of the cardiac voltage-gated sodium channel, Naᵥ1.5, provides the rapid sodium inward current that initiates cardiomyocyte action potentials.
Batlle, Montserrat +13 more
core +2 more sources
iProteinDB: An Integrative Database of Drosophila Post-translational Modifications
G3: Genes, Genomes, Genetics, 2019 Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing their stability, interactions, activity and localization, and is critical in many signaling pathways.
Yanhui Hu +10 more
doaj +1 more source
Regulation of Lignin Biosynthesis by Post-translational Protein Modifications
Frontiers in Plant Science, 2020 Post-translational modification of proteins exerts essential roles in many biological processes in plants. The function of these chemical modifications has been extensively characterized in many physiological processes, but how these modifications ...
Daniel B. Sulis, Jack P. Wang
doaj +1 more source
Subcellular trafficking and post-translational modification regulate PIN polarity in plants
Frontiers in Plant Science, 2022 Auxin regulates plant growth and tropism responses. As a phytohormone, auxin is transported between its synthesis sites and action sites. Most natural auxin moves between cells via a polar transport system that is mediated by PIN-FORMED (PIN) auxin ...
Shuyang Cheng +3 more
doaj +1 more source
Post-translational modification by SUMO [PDF]
Toxicology, 2010 Post-translational modifications (PTMs) are chemical alterations to a protein following translation, regulating stability and function. Reversible phosphorylation is an example of an important and well studied PTM involved in a number of cellular processes.
Hannoun, Zara +4 more
openaire +4 more sources
Role of glutathionylation in infection and inflammation [PDF]
, 2019 Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent cellular oxidoreductases, by which the redox state of the cell
Baldelli, S. +5 more
core +1 more source
Protein modification and maintenance systems as biomarkers of ageing [PDF]
, 2015 Changes in the abundance and post-translational modification of proteins and accumulation of some covalently modified proteins have been proposed to represent hallmarks of biological ageing.
Friguet, Bertrand +7 more
core +4 more sources
BMC Genomics, 2017 Background Post-translational modification (PTM) of proteins is central to many cellular processes across all domains of life, but despite decades of study and a wealth of genomic and proteomic data the biological function of many PTMs remains unknown ...
Colin W. Brown +6 more
doaj +1 more source
The post-translational modification, SUMOylation, and cancer (Review)
International Journal of Oncology, 2018 SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis.
Zhi-Jian Han +4 more
semanticscholar +1 more source
Post-translational modifications of tubulin [PDF]
Current Biology, 2014 Microtubules are the largest filamentous components of the eukaryotic cytoskeleton. In spite of their extraordinary level of structural conservation, microtubules fulfill a vast range of different functions in cells. How this functional diversity is achieved remains an open question; however, recent advances point towards post-translational ...
Magiera, Maria M., Janke, Carsten
openaire +2 more sources