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- W4366147112 abstract "Since the discovery of tyrosine phosphorylation being a critical modulator of cancer signaling, proteins regulating phosphotyrosine levels in cells have fast become targets of therapeutic intervention. The nonreceptor protein tyrosine phosphatase (PTP) coded by the PTPN11 gene SHP2 integrates phosphotyrosine signaling from growth factor receptors into the RAS/RAF/ERK pathway and is centrally positioned in processes regulating cell development and oncogenic transformation. Dysregulation of SHP2 expression or activity is linked to tumorigenesis and developmental defects. Even as a compelling anti-cancer target, SHP2 was considered undruggable for a long time owing to its conserved catalytic PTP domain that evaded drug development. Recently, SHP2 has risen from the undruggable curse with the discovery of small molecules that manipulate its intrinsic allostery for effective inhibition. SHP2's unique domain arrangement and conformation(s) allow for a truly novel paradigm of inhibitor development relying on skillful targeting of noncatalytic sites on proteins. In this review we summarize the biological functions, signaling properties, structural attributes, allostery and inhibitors of SHP2." @default.
- W4366147112 created "2023-04-19" @default.
- W4366147112 creator A5026001109 @default.
- W4366147112 creator A5028245832 @default.
- W4366147112 creator A5030956462 @default.
- W4366147112 date "2023-01-01" @default.
- W4366147112 modified "2023-10-14" @default.
- W4366147112 title "Setting sail: Maneuvering SHP2 activity and its effects in cancer" @default.
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