Protein phosphorylation is a crucial regulator of protein and cellular function, yet, despite
identifying an enormous number of phosphorylation sites, the role of most is still unclear …

The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

Mitochondria in the cell are the center for energy production, essential biomolecule
synthesis, and cell fate determination. Moreover, the mitochondrial functional versatility …

Ubiquitination, the covalent attachment of ubiquitin to proteins, by E3 ligases of the HECT
(homologous to E6AP C terminus) family is critical in controlling diverse physiological …

Highlights•Dha in proteins is easily and flexibly accessible under mild conditions.•Dha
reactivity is used in β, γ-C–S/Se/N/C bond-formation and allows 'zero scar'protein …

Improvement in intrinsic enzymatic features is in many instances a prerequisite for the
scalable applicability of many industrially important biocatalysts. To this end, various …

The phosphorylation of threonine residues in proteins regulates diverse processes in
eukaryotic cells, and thousands of threonine phosphorylations have been identified. An …

Post-translational modifications (PTMs) dynamically regulate cellular processes. Lysine
undergoes a range of acylations, including malonylation, succinylation (SucK) and …

Various post-translational modifications can naturally occur on proteins, regulating the
activity, subcellular localization, interaction, or stability of the proteins. However, it can be …