ArticleeLife2018
An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
What it found
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Who cites it
122 citing papers in PubMed.
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.Protein science : a publication of the Protein Society · 2026Article
- Structural basis of Fumosorinone-mediated allosteric inhibition of PTP1B for cancer immunotherapy.Communications biology · 2026Article
- An integrated experimental and computational pipeline for crystallographic fragment screening of membrane protein in the lipid cubic phase.Communications chemistry · 2026Article
- High-throughput biochemical phenotyping of SHP2 variants reveals the molecular basis of diseases and allosteric drug inhibition.bioRxiv : the preprint server for biology · 2026Article
- Phosphatase Signaling as a Therapeutic Strategy in Schizophrenia.International journal of molecular sciences · 2026Review
- Cancer-Causing Mutations Alter the Interplay Between Loop Dynamics and Catalysis in the Protein Tyrosine Phosphatases SHP-1 and SHP-2.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms, functions and therapeutic targeting of protein tyrosine phosphatases.Nature reviews. Molecular cell biology · 2026Review
- Unfreezing structural biology for drug discovery.Nature chemical biology · 2026Review
- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- Loop dynamics, allostery, and function in protein tyrosine phosphatases: insights from molecular simulations.Biochemical Society transactions · 2026Review
- Article
- In Silico, In Vitro, and In Vivo Antidiabetic Activity of an Alkaloid, 1, 2-Dimethoxy-12-Methyl-7-(3-Methylbut-2-en-1-yl)-12, 13-Dihydro [1,3] Benzodioxolo [5,6-c] Phenanthridin-13-ol, Isolated From a Zimbabwean Herbal Antidiabetic Medicine.BioMed research international · 2026Article
- Other Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- False Friends in Fluorescence - Simple HPLC Evaluation of False Positive Fragment Hits in a DiFMUP Assay for Protein Tyrosine Phosphatase 1B.Drug design, development and therapy · 2026Article
- Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.Biochemistry · 2025Article
- Sensitive detection of structural dynamics using a statistical framework for comparative crystallography.Science advances · 2025Article
- Epoxy tetrahydrophthalimides as potential bioactive agents: synthesis and computational study.Pest management science · 2025Article
- Article
- Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids.bioRxiv : the preprint server for biology · 2025Article
- Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2025Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here, we have identified allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining multiple-temperature X-ray crystallography experiments and structure determination from hundreds of individual small-molecule fragment soaks. New modeling approaches reveal 'hidden' low-occupancy conformational states for protein and ligands. Our results converge on allosteric sites that are conformationally coupled to the active-site WPD loop and are hotspots for fragment binding. Targeting one of these sites with covalently tethered molecules or mutations allosterically inhibits enzyme activity. Overall, this work demonstrates how the ensemble nature of macromolecular structure, revealed here by multitemperature crystallography, can elucidate allosteric mechanisms and open new doors for long-range control of protein function.
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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.