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- W2810337002 endingPage "1461" @default.
- W2810337002 startingPage "1449" @default.
- W2810337002 abstract "The mammalian genome contains approximately 200 phosphatases that are responsible for catalytically removing phosphate groups from proteins. In this review, we discuss dual specificity phosphatase 5 (DUSP5). DUSP5 belongs to the dual specificity phosphatase (DUSP) family, so named after the family members’ abilities to remove phosphate groups from serine/threonine and tyrosine residues. We provide a comparison of DUSP5’s structure to other DUSPs and, using molecular modeling studies, provide an explanation for DUSP5’s mechanistic interaction and specificity toward phospho-extracellular regulated kinase, its only known substrate. We also discuss new insights from molecular modeling studies that will influence our current thinking of mitogen-activated protein kinase signaling. Finally, we discuss the lessons learned from identifying small molecules that target DUSP5, which might benefit targeting efforts for other phosphatases. © 2017 American Physiological Society. Compr Physiol 7:1449-1461, 2017." @default.
- W2810337002 created "2018-07-10" @default.
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- W2810337002 date "2017-09-12" @default.
- W2810337002 modified "2023-09-26" @default.
- W2810337002 title "Dual Specificity Phosphatase 5‐Substrate Interaction: A Mechanistic Perspective" @default.
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- W2810337002 doi "https://doi.org/10.1002/cphy.c170007" @default.
- W2810337002 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28915331" @default.