Residues Distant From the Active Site Influence Protein-Tyrosine Phosphatase 1B Inhibitor Binding

Journal of Biological Chemistry - United States
doi 10.1074/jbc.m511546200
Full Text
Abstract

Available in full text

Date
Authors
Publisher

American Society for Biochemistry & Molecular Biology (ASBMB)

Related search

Structure-Based Optimization of Protein Tyrosine Phosphatase 1B Inhibitors: From the Active Site to the Second Phosphotyrosine Binding Site

English

Conformation-Assisted Inhibition of Protein-Tyrosine Phosphatase-1b Elicits Inhibitor Selectivity Over T-Cell Protein-Tyrosine Phosphatase

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2006English

Minimally Disruptive Optical Control of Protein Tyrosine Phosphatase 1B

Nature Communications
AstronomyGeneticsMolecular BiologyBiochemistryChemistryPhysics
2020English

Suramin Is an Active Site-Directed, Reversible, and Tight-Binding Inhibitor of Protein-Tyrosine Phosphatases

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
1998English

Podocyte Protein, Nephrin, Is a Substrate of Protein Tyrosine Phosphatase 1B

Journal of Signal Transduction
BiochemistryMolecular NeuroscienceCell BiologyCellular
2011English

Inhibitory Potential of Polyhydroxylated Fullerenes Against Protein Tyrosine Phosphatase 1B

Ukrainian Biochemical Journal
Biochemistry
2015English

Discovery and Study of Novel Protein Tyrosine Phosphatase 1B Inhibitors

2017English

Gαi2Enhances Insulin Signaling via Suppression of Protein-Tyrosine Phosphatase 1B

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2001English

Redox Regulation of Protein Tyrosine Phosphatase 1B by Peroxymonophosphate (dO3POOH)

English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy