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

Specific inhibition of sensitized protein tyrosine phosphatase 1B (PTP1B) with a biarsenical probe.

Bioconjugate chemistry - 15 Feb 2012

Davis Oliver B, Bishop Anthony C

Abstract excerpt

Protein tyrosine phosphatase 1B (PTP1B) is a key regulator of the insulin-receptor and leptin-receptor signaling pathways, and it has therefore emerged as a critical antitype-II-diabetes and antiobesity drug target. Toward the goal of generating a covalent modulator of PTP1B activity that can be used for investigating its roles in cell signaling and disease progression, we report that the biarsenical probe...

Read the complete abstract on PubMed

Topics

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

Share to Arsenicals
Share to Escherichia coli
Share to Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Probes

Share to Molecular Structure

Share to Protein Engineering

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 22263876
DOI: 10.1021/bc200562y
PMCID: PMC3288891

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Specific inhibition of sensitized protein tyrosine phosphatase 1B (PTP1B) with a biarsenical probe.PMID 22263876Read ↗

Optimized allosteric inhibition of engineered protein tyrosine phosphatases with an expanded palette of biarsenical small molecules.Semantic proximity Read ↗

Target-specific control of lymphoid-specific protein tyrosine phosphatase (Lyp) activity.Semantic proximity Read ↗

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

Allele-specific inhibition of divergent protein tyrosine phosphatases with a single small molecule.Semantic proximity Read ↗

Chemical rescue of protein tyrosine phosphatase activity.Semantic proximity Read ↗

Identification of substrates of the protein tyrosine phosphatase PTP1B using <i>in situ</i> site-specific photo-crosslinkingSemantic proximity Read ↗

Substrate-derived peptides for selective covalent inhibition of protein tyrosine kinasesSemantic proximity Read ↗

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

Expanding the ligandable proteome by paralog hopping with covalent probesSemantic proximity Read ↗

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

Electrophile scanning by chemical proteomics reveals a potent pan-active DUB probe for investigation of deubiquitinase activity in live cellsSemantic proximity Read ↗

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

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