ArticleDrug design, development and therapy2016
Druggability analysis and classification of protein tyrosine phosphatase active sites.
Article in Drug design, development and therapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 51 citations in OpenAlex.
- Shifting paradigms: phosphatases from basic biology to druggable targets.Biology open · 2026Article
- Novel cyclic heptapeptides as potential therapeutics against methicillin-resistant Staphylococcus aureus infections.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Characterization of prevalent genetic variants in the Estonian Biobank body-mass index GWAS.Nature communications · 2025Article
- Identification ofMicrobiology spectrum · 2025Article
- Computational exploration of palmitoyl-protein thioesterase 1 inhibition byJournal of Taibah University Medical Sciences · 2024Article
- Development of Novel Phosphonodifluoromethyl-Containing Phosphotyrosine Mimetics and a First-In-Class, Potent, Selective, and Bioavailable Inhibitor of Human CDC14 Phosphatases.Journal of medicinal chemistry · 2024Article
- Can Allostery Be a Key Strategy for Targeting PTP1B in Drug Discovery? A Lesson from Trodusquemine.International journal of molecular sciences · 2023Review
- Structure-based discovery and in vitro validation of inhibitors of chloride intracellular channel 4 protein.Computational and structural biotechnology journal · 2023Article
- Fludarabine, a Potential DNA-Dependent RNA Polymerase Inhibitor, as a Prospective Drug against Monkeypox Virus: A Computational Approach.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Recent applications of computational methods to allosteric drug discovery.Frontiers in molecular biosciences · 2022Review
- In Silico Screening of Available Drugs Targeting Non-Small Cell Lung Cancer Targets: A Drug Repurposing Approach.Pharmaceutics · 2021Article
- High-throughput screening to identify potential inhibitors of the Zα domain of the adenosine deaminase 1 (ADAR1).Saudi journal of biological sciences · 2021Article
- NICEdrug.ch, a workflow for rational drug design and systems-level analysis of drug metabolism.eLife · 2021Article
- Article
- Therapeutic Targeting of Protein Tyrosine Phosphatases fromMicroorganisms · 2020Review
- PTPσ inhibitors promote hematopoietic stem cell regeneration.Nature communications · 2019Article
- High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.Acta crystallographica. Section D, Structural biology · 2018Article
- Novel benzamido derivatives as PTP1B inhibitors with anti-hyperglycemic and lipid-lowering efficacy.Acta pharmaceutica Sinica. B · 2018Article
- Article
- MptpB Promotes Mycobacteria Survival by Inhibiting the Expression of Inflammatory Mediators and Cell Apoptosis in Macrophages.Frontiers in cellular and infection microbiology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein tyrosine phosphatases (PTP) play important roles in the pathogenesis of many diseases. The fact that no PTP inhibitors have reached the market so far has raised many questions about their druggability. In this study, the active sites of 17 PTPs were characterized and assessed for its ability to bind drug-like molecules. Consequently, PTPs were classified according to their druggability scores into four main categories. Only four members showed intermediate to very druggable pocket; interestingly, the rest of them exhibited poor druggability. Particularly focusing on PTP1B, we also demonstrated the influence of several factors on the druggability of PTP active site. For instance, the open conformation showed better druggability than the closed conformation, while the tight-bound water molecules appeared to have minimal effect on the PTP1B druggability. Finally, the allosteric site of PTP1B was found to exhibit superior druggability compared to the catalytic pocket. This analysis can prove useful in the discovery of new PTP inhibitors by assisting researchers in predicting hit rates from high throughput or virtual screening and saving unnecessary cost, time, and efforts via prioritizing PTP targets according to their predicted druggability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.