A peer-reviewed review examines protein acylation as a link among cancer metabolism, tumor plasticity, therapeutic resistance ...

A research team of 37 scientists, led by the Technical University of Munich, has developed a method to interrogate drug-induced post-translational modifications (PTMs) in a time and dose-dependent way ...

A transcriptomic study identified GABARAPL1, PELI1 and NLRP3 as elevated blood RNA markers associated with acute myocardial ...

Chemical changes to histones, the proteins that help to pack and organize DNA inside cells, play a key role in determining what genes will be consistently activated over the course of an animal or ...

In eukaryotes, genomic DNA, which is a very long double helix containing all the genetic information, wraps around a globular protein called a histone and folds it many times before being contained ...

Proteins are subject to post-translational chemical modifications that result in functional diversity. Methylation is one such modification that is generally believed to occur on lysine and arginine ...

The focus of vertebrate studies has mainly been on canonical phosphorylation, but research indicates that phosphorylation of other non-canonical amino acids also regulates integral aspects of cell ...

Post-translational modifications (PTMs) play a key role in dynamic cellular processes, regulating gene expression, protein activity, localization, and degradation, as well as protein interaction.

One of the main goals of proteomics is to unravel the many modifications important for biological activity. Post-translational modifications (PTMs) extend the range of protein function by attaching it ...

The proper assembly and maturation of collagens necessitate the orchestrated hydroxylation and glycosylation of multiple lysyl residues in procollagen chains. Dysfunctions in this multistep ...

The central dogma of molecular biology has expanded well beyond the flow of information from DNA-to-RNA-to-protein into a system of complex interactions and feedback loops among all these ...