Serine/threonine phosphatases: mechanism through structure.
By Yigong Shi. Cell, 2009
1,478 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/081c1ad8fbb641732e4103baa778993c3d015199
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In Molecular Biology
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Citations in the corpus
- The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review) (2017, neutral): “PPP and PMP groups are responsible for most dephosphorylation reactions of phosphoserine and phos-photreonine (pSer/pThr) and they can also dephosphorylate phosphotyrosine (pTyr) (35,36).”
- SOcK, MiSTs, MASK and STicKs: the GCKIII (germinal centre kinase III) kinases and their heterologous protein-protein interactions. (2013, background): “, Shinzato, M., Machida, N., Uezato, H., Nonaka, S. and Kariya, K. (2004) The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton. J. Biol. Chem. 279, 49488–49496 100 Huang, E. J. and Reichardt, L. F. (2003) Trk receptors: roles in neuronal signal transduc”
- Structure and dynamics of molecular networks: A novel paradigm of drug discovery: A comprehensive review (2012, background): “…specificity is achieved through docking of the phosphatase complex at a site distant from the dephosphorylated amino acid (Roy & Cyert, 2009; Shi, 2009); (iii) the targeted sequences are highly charged, and many of the interacting compounds are not hydrophobic enough to cross the membrane…”