Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.

The Journal of biological chemistry - 24 Mar 2006

Asante-Appiah Ernest, Patel Sangita, Desponts Caroline, Taylor Jillian M, Lau Cheuk, Dufresne Claude, Therien Michel, Friesen Rick, Becker Joseph W, Leblanc Yves, Kennedy Brian P, Scapin Giovanna

Abstract excerpt

PTP-1B represents an attractive target for the treatment of type 2 diabetes and obesity. Given the role that protein phosphatases play in the regulation of many biologically relevant processes, inhibitors against PTP-1B must be not only potent, but also selective. It has been extremely difficult to synthesize inhibitors that are selective over the highly homologous TCPTP. We have successfully exploited the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Inhibitory Concentration 50

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Leucine

Share to Models, Chemical

Share to Molecular Conformation

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Share to Protein Tyrosine Phosphatases

Share to Valine

Source

Identifiers

PMID: 16407290
DOI: 10.1074/jbc.M511827200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.PMID 16407290Read ↗

Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta.Semantic proximity Read ↗

Allele-specific inhibitors of protein tyrosine phosphatases.Semantic proximity Read ↗

Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B.Semantic proximity Read ↗

Structural analysis of protein tyrosine phosphatase 1B reveals potentially druggable allosteric binding sites.Semantic proximity Read ↗

Targeting Nonconserved and Pathogenic Cysteines of Protein Tyrosine Phosphatases with Small Molecules.Semantic proximity Read ↗

Protein Tyrosine Phosphatase 1B (PTP1B): Insights into its New Implications in TumorigenesisSemantic proximity Read ↗

Discovery of a novel series of inhibitors of lymphoid tyrosine phosphatase with activity in human T cells.Semantic proximity Read ↗

Microbially guided discovery and biosynthesis of biologically active natural productsSemantic proximity Read ↗

Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Semantic proximity Read ↗

Covalent Allosteric Inactivation of Protein Tyrosine Phosphatase 1B (PTP1B) by an Inhibitor-Electrophile Conjugate.Semantic proximity Read ↗

Use of Dominant-Negative/Substrate Trapping PTP Mutations to Search for PTP Interactors/Substrates.Semantic proximity Read ↗

Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.