Chaperones support protein folding in different cellular compartments and some chaperones associate with ribosomes to help fold newly synthesized proteins. Two studies by Koplin et al. and Albanèse et ...

Intrinsically disordered proteins (IDPs) lack well-defined structure but are widely represented in eukaryotic proteomes. Although the functions of most IDPs are not understood, some have been shown to ...

A recent study from CU Boulder researchers shows that cells must actively work to keep sticky molecules, known as ribonucleic acid (RNA), apart, or they may form large assemblies that could cause ...

This is a preview. Log in through your library . Abstract Group I and II introns self-splice in vitro, but require proteins for efficient splicing in vivo, to stabilize the catalytically active RNA ...

The biology of histone proteins encompasses their synthesis in the cytosol, nuclear import and incorporation into nucleosomes, as well as subsequent eviction from chromatin, redeposition, storage or ...

A paper focusing on the role of co-chaperones involved in ribonucleotide reductase (RNR) activity was recently published in PLOS Genetics and made reference to StressMarq’s Mouse Anti-Yeast HSP40, ...