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- W2764258509 endingPage "e1382671" @default.
- W2764258509 startingPage "e1382671" @default.
- W2764258509 abstract "Phosphorylation is a dynamic post-translational modification that can alter protein structure, localization, protein-protein interactions and stability. All of the identified tight junction transmembrane proteins can be multiply phosphorylated, but only in a few cases are the consequences of phosphorylation at specific sites well characterized. The goal of this review is to highlight some of the best understood examples of phosphorylation changes in the integral membrane tight junction proteins in the context of more general overview of the effects of phosphorylation throughout the proteome. We expect as that structural information for the tight junction proteins becomes more widely available and the molecular modeling algorithms improve, so will our understanding of the relevance of phosphorylation changes at single and multiple sites in tight junction proteins." @default.
- W2764258509 created "2017-10-20" @default.
- W2764258509 creator A5024216881 @default.
- W2764258509 creator A5059725025 @default.
- W2764258509 date "2017-10-30" @default.
- W2764258509 modified "2023-10-15" @default.
- W2764258509 title "Phosphorylation of tight junction transmembrane proteins: Many sites, much to do" @default.
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