English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Reversible phosphorylation of tyrosine residues serves as a biochemical “switch” that alters the functional properties of many proteins involved in cellular signal transduction processes. Protein tyrosine phosphatases (PTPs) catalyze the removal of phosphoryl groups from tyrosine residues in target proteins, thereby playing a central role in the regulation of diverse cellular processes including glucose metabolism, cell cycle control, and immune responses. Accordingly, small molecules capable of inactivating PTPs may find use as therapeutic agents and tools for the study of diverse signal transduction pathways. In the work reported here, peroxymonophosphate (2-O3POOH) was reported to be an exceptional inactivator of PTP1B, an archetypal member of the PTP enzyme family (KI = 6.6 × 10-7 M and kinact = 0.043 s-1). In this regard, peroxymonophosphate is over 7000 times more potent than hydrogen peroxide, the endogenous regulator of PTP1B. Inactivation of PTP1B by peroxymonophosphate is active site directed an...

Redox Regulation of Protein Tyrosine Phosphatase 1B by Peroxymonophosphate (O3POOH)

Redox Regulation of Protein Tyrosine Phosphatase 1B by Peroxymonophosphate (O₃POOH)