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- W2035606479 endingPage "4350" @default.
- W2035606479 startingPage "4337" @default.
- W2035606479 abstract "N-terminal methionine-linked ubiquitin (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. The molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled the identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how nondegradative ubiquitin modifications control proinflammatory responses mediated by nuclear factor-κB and mitogen-activated protein kinases. In this review, we discuss the current data on Met1-Ub function and regulation, and point to some of the questions that still remain unanswered." @default.
- W2035606479 created "2016-06-24" @default.
- W2035606479 creator A5026464853 @default.
- W2035606479 creator A5028349890 @default.
- W2035606479 date "2014-08-12" @default.
- W2035606479 modified "2023-10-03" @default.
- W2035606479 title "Met1‐linked ubiquitination in immune signalling" @default.
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- W2035606479 doi "https://doi.org/10.1111/febs.12944" @default.
- W2035606479 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4286102" @default.
- W2035606479 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25060092" @default.
- W2035606479 hasPublicationYear "2014" @default.
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