The covalent attachment of Ub (ubiquitin) to target proteins (ubiquitylation) represents one of
the most versatile PTMs (post-translational modifications) in eukaryotic cells. Substrate …

Post-translational modifications (PTMs) endow proteins with new properties to respond to
environmental changes or growth needs. With the development of advanced proteomics …

Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is
key to understanding the role of protein phosphorylation. Here we report an efficient method …

Ubiquitination is controlled by a series of E1, E2, and E3 enzymes that can ligate ubiquitin to
cellular proteins and dictate the turnover of a substrate and the outcome of signalling events …

Protein phosphorylation is a ubiquitous post-translational modification used to regulate
cellular processes and proteome architecture by modulating protein-protein interactions …

Ubiquitin (UB) transfer cascades consisting of E1, E2, and E3 enzymes constitute a complex
network that regulates a myriad of biologic processes by modifying protein substrates …

Synthetic biology holds promise to revolutionize the life sciences and biomedicine via
expansion of macromolecular diversity outside the natural chemical space. Use of non …

Selenoproteins contain the amino acid selenocysteine (Sec), co-translationally inserted at a
predefined UGA opal codon by means of Sec-specific translation machineries. In …

Nowadays advanced mass spectrometry techniques make the identification of protein
posttranslational modifications (PTMs) much easier than ever before. A series of proteomic …

Exciting new technological developments have pushed the boundaries of structural biology,
and have enabled studies of biological macromolecules and assemblies that would have …