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

Allele-specific inhibitors of protein tyrosine phosphatases.

Journal of the American Chemical Society - 9 Mar 2005

Hoffman Hillary E, Blair Elizabeth R, Johndrow James E, Bishop Anthony C

Abstract excerpt

Protein tyrosine phosphatases (PTPs) are critical cell-signaling molecules. Inhibitors that are selective for individual PTPs would be valuable tools for dissecting complicated phosphorylation networks. However, the common architecture of PTP active sites impedes the discovery of such compounds. To achieve target selectivity, we have redesigned a PTP/inhibitor interface. Site-directed mutagenesis of a...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Protein Engineering

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Share to Protein Tyrosine Phosphatases

Share to Substrate Specificity

Source

Identifiers

PMID: 15740097
DOI: 10.1021/ja043378w

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allele-specific inhibitors of protein tyrosine phosphatases.PMID 15740097Read ↗

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

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

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

Tailor-Made Protein Tyrosine Phosphatases: In Vitro Site-Directed Mutagenesis of PTEN and PTPRZ-B.Semantic proximity Read ↗

Evolutionarily Conserved Allosteric Communication in Protein Tyrosine PhosphatasesSemantic proximity Read ↗

Residues distant from the active site influence protein-tyrosine phosphatase 1B inhibitor binding.Semantic proximity Read ↗

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

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

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

Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.Semantic proximity Read ↗

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