Prediction and verification of novel peptide targets of protein tyrosine phosphatase 1B
نویسندگان
چکیده
منابع مشابه
Protein Tyrosine Phosphatase 1B Inhibitors: Catechols
As most intracellular signaling takes place via cascades of phosphorylation and dephosphorylation of tyrosines, protein tyrosine phosphatases have emerged as new and promising targets. Among them, protein tyrosine phosphatase 1B (PTP1B) negatively regulates insulin signaling by dephosphorylation of key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor, ther...
متن کاملThe Mechanism of Allosteric Inhibition of Protein Tyrosine Phosphatase 1B
As the prototypical member of the PTP family, protein tyrosine phosphatase 1B (PTP1B) is an attractive target for therapeutic interventions in type 2 diabetes. The extremely conserved catalytic site of PTP1B renders the design of selective PTP1B inhibitors intractable. Although discovered allosteric inhibitors containing a benzofuran sulfonamide scaffold offer fascinating opportunities to overc...
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By imitating the scaffold of lithocholic acid (LCA), a natural steroidal compound displaying Protein Tyrosine Phosphatase 1B (PTP1B) inhibitory activity, a series of stilbene derivatives containing phenyl-substituted isoxazoles were designed and synthesized. The structures of the title compounds were confirmed by ¹H-NMR, 13C-NMR and HRMS. Activities of the title compounds were evaluated on PTP1...
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Protein tyrosine phosphatases (PTPs) are cysteine-dependent enzymes that play a central role in cell signaling. Organic hydroperoxides cause thiol-reversible, oxidative inactivation of PTP1B in a manner that mirrors the endogenous signaling agent hydrogen peroxide.
متن کاملRedox regulation of protein tyrosine phosphatase 1B by peroxymonophosphate (=O3POOH).
Reversible phosphorylation of tyrosine residues serves as a biochemical “switch” that alters the functional properties of many proteins involved in cellular signal transduction processes.1,2 The phosphorylation status of tyrosine residues in target proteins is controlled by the opposing actions of protein tyrosine kinases that catalyze the addition of phosphoryl groups and protein tyrosine phos...
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ژورنال
عنوان ژورنال: Bioorganic & Medicinal Chemistry
سال: 2016
ISSN: 0968-0896
DOI: 10.1016/j.bmc.2016.03.030