Chidambaram Ramachandran

TL;DR: In this article, the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP−1B+/+ littermates.

TL;DR: The results show that vanadate is a competitive inhibitor for the protein-tyrosine phosphatase PTP1B, with a Ki of 0.38 ± 0.02 μM, and reducing agents such as dithiothreitol that are used in PTP assays to keep the catalytic cysteine reduced and active were found to convert pervanadate rapidly toVanadate.

TL;DR: This commentary reviews the current knowledge of PTP-1B in insulin signaling and its role in diabetes and discusses the development of potent and selective PTP -1B inhibitors.

TL;DR: In this article, the crystal structures of protein tyrosine phosphatase 1B (PTP1B) in complex with first and second generation aryldifluoromethyl-phosphonic acid inhibitors were reported.

TL;DR: The feasibility of using mass spectrometric detection to quantitate peptides rapidly and reproducibly is demonstrated as an alternative to quantitation by peptide sequencing, and the approach described here should prove applicable to protein tyrosine phosphatases in general as well as for the study of nonpeptidyl combinatorial libraries.