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- W2541489296 endingPage "509" @default.
- W2541489296 startingPage "496" @default.
- W2541489296 abstract "Ubiquitination is a type of posttranslational modification of intracellular proteins characterized by covalent attachment of one (monoubiquitination) or several (polyubiquitination) of ubiquitin molecules to target proteins. In the case of polyubiquitination, linear or branched polyubiquitin chains are formed. Their formation involves various lysine residues of monomeric ubiquitin. The best studied is Lys48-polyubiquitination, which targets proteins for proteasomal degradation. In this review we have considered examples of so-called atypical polyubiquitination, which mainly involves other lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys63) and also N-terminal methionine. The considered examples convincingly demonstrate that polyubiquitination of proteins not necessarily targets proteins for their proteolytic degradation in proteasomes. Atypically polyubiquitinated proteins are involved in regulation of various processes and altered polyubiquitination of certain proteins is crucial for development of serious diseases." @default.
- W2541489296 created "2016-11-04" @default.
- W2541489296 creator A5047627564 @default.
- W2541489296 creator A5066560041 @default.
- W2541489296 date "2016-01-01" @default.
- W2541489296 modified "2023-10-12" @default.
- W2541489296 title "Atypical ubiquitination of proteins" @default.
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