Matches in SemOpenAlex for { <https://semopenalex.org/work/W2090179002> ?p ?o ?g. }
- W2090179002 abstract "Abstract Abstract Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80–90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. Publication history Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com )." @default.
- W2090179002 created "2016-06-24" @default.
- W2090179002 creator A5047001450 @default.
- W2090179002 creator A5062111609 @default.
- W2090179002 creator A5072417653 @default.
- W2090179002 date "2008-10-01" @default.
- W2090179002 modified "2023-10-09" @default.
- W2090179002 title "Deubiquitylating enzymes and disease" @default.
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- W2090179002 doi "https://doi.org/10.1186/1471-2091-9-s1-s3" @default.
- W2090179002 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2582804" @default.
- W2090179002 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19007433" @default.
- W2090179002 hasPublicationYear "2008" @default.
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