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- W2007904980 endingPage "689" @default.
- W2007904980 startingPage "674" @default.
- W2007904980 abstract "Ubiquitination is an important post-translational process involving attachment of the ubiquitin molecule to lysine residue/s on a substrate protein or on another ubiquitin molecule, leading to the formation of protein mono-, multi- or polyubiquitination. Protein ubiquitination requires a cascade of three enzymes, where the interplay between different ubiquitin-conjugating and ubiquitin-ligase enzymes generates diverse ubiquitinated proteins topologies. Structurally diverse ubiquitin conjugates are recognized by specific proteins with ubiquitin-binding domains (UBDs) to target the substrate proteins of different pathways. The mechanism/s for generating the different ubiquitinated proteins topologies is not well understood. Here, we will discuss our current understanding of the mechanisms underpinning the generation of mono- or polyubiquitinated substrates. In addition, we will discuss how linkage-specific polyubiquitin chains through lysines-11, -48 or -63 are formed to target proteins to different fates by binding specific UBD proteins." @default.
- W2007904980 created "2016-06-24" @default.
- W2007904980 creator A5002992439 @default.
- W2007904980 creator A5008914538 @default.
- W2007904980 creator A5017768833 @default.
- W2007904980 creator A5029330166 @default.
- W2007904980 date "2014-07-01" @default.
- W2007904980 modified "2023-10-08" @default.
- W2007904980 title "Mechanisms of Generating Polyubiquitin Chains of Different Topology" @default.
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- W2007904980 doi "https://doi.org/10.3390/cells3030674" @default.
- W2007904980 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4197637" @default.
- W2007904980 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24987835" @default.
- W2007904980 hasPublicationYear "2014" @default.
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