Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy
Sign Up to like & getrecommendations! Published in 2019 at "Chembiochem"
DOI: 10.1002/cbic.201900146
Abstract: As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct… read more here.
Keywords: artificially linked; dimers characterised; ubiquitin dimers; nmr spectroscopy ... See more keywords
Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers
Sign Up to like & getrecommendations! Published in 2019 at "Scientific Reports"
DOI: 10.1038/s41598-019-56458-z
Abstract: Ubiquitylation is an eminent posttranslational modification referring to the covalent attachment of single ubiquitin molecules or polyubiquitin chains to a target protein dictating the fate of such labeled polypeptide chains. Here, we have biochemically produced… read more here.
Keywords: artificially conjugated; functional characterization; ubiquitin dimers; ubiquitin ... See more keywords
Towards a molecular basis of ubiquitin signaling: A dual-scale simulation study of ubiquitin dimers
Sign Up to like & getrecommendations! Published in 2018 at "PLoS Computational Biology"
DOI: 10.1371/journal.pcbi.1006589
Abstract: Covalent modification of proteins by ubiquitin or ubiquitin chains is one of the most prevalent post-translational modifications in eukaryotes. Different types of ubiquitin chains are assumed to selectively signal respectively modified proteins for different fates.… read more here.
Keywords: basis ubiquitin; molecular basis; ubiquitin dimers; ubiquitin signaling ... See more keywords