Human protein tyrosine phosphatase 1B (PTP1B): from structure to clinical inhibitor perspectives

R Liu, C Mathieu, J Berthelet, W Zhang… - International Journal of …, 2022 - mdpi.com
Phosphorylation is an essential process in biological events and is considered critical for
biological functions. In tissues, protein phosphorylation mainly occurs on tyrosine (Tyr) …

Free radicals in the physiological control of cell function

W Dröge - Physiological reviews, 2002 - journals.physiology.org
At high concentrations, free radicals and radical-derived, nonradical reactive species are
hazardous for living organisms and damage all major cellular constituents. At moderate …

Genomics and evolution of protein phosphatases

MJ Chen, JE Dixon, G Manning - Science signaling, 2017 - science.org
Protein phosphatases are the essential opposite to protein kinases; together, these enzymes
regulate all protein phosphorylation and most cellular processes. To better understand the …

Protein tyrosine phosphatases–from housekeeping enzymes to master regulators of signal transduction

NK Tonks - The FEBS journal, 2013 - Wiley Online Library
There are many misconceptions surrounding the roles of protein phosphatases in the
regulation of signal transduction, perhaps the most damaging of which is the erroneous view …

Mechanisms of specificity in protein phosphorylation

JA Ubersax, JE Ferrell Jr - Nature reviews Molecular cell biology, 2007 - nature.com
A typical protein kinase must recognize between one and a few hundred bona fide
phosphorylation sites in a background of∼ 700,000 potentially phosphorylatable residues …

Signal transduction through MAP kinase cascades

TS Lewis, PS Shapiro, NG Ahn - Advances in cancer research, 1998 - Elsevier
Publisher Summary The chapter introduces the mitogen-activated protein (MAP) kinase
(MAPK) module. The identification of MAP kinase pathways exemplifies the power of …

[HTML][HTML] Crystal structure of the tyrosine phosphatase SHP-2

P Hof, S Pluskey, S Dhe-Paganon, MJ Eck… - Cell, 1998 - cell.com
The structure of the SHP-2 tyrosine phosphatase, determined at 2.0 Å resolution, shows how
its catalytic activity is regulated by its two SH2 domains. In the absence of a tyrosine …

Reversible inactivation of the tumor suppressor PTEN by H2O2

SR Lee, KS Yang, J Kwon, C Lee, W Jeong… - Journal of Biological …, 2002 - ASBMB
The tumor suppressor PTEN regulates cell migration, growth, and survival by removing the
3′-phosphate of phosphoinositides. Exposure of purified PTEN or of cells to H 2 O 2 …

[HTML][HTML] Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

JO Lee, H Yang, MM Georgescu, A Di Cristofano… - Cell, 1999 - cell.com
The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer
predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and …

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

A Salmeen, JN Andersen, MP Myers, TC Meng… - Nature, 2003 - nature.com
The second messenger hydrogen peroxide is required for optimal activation of numerous
signal transduction pathways, particularly those mediated by protein tyrosine kinases …