ArticleNature chemical biology2013
Allosteric inhibition through suppression of transient conformational states.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
67 citing papers in PubMed.
- Non canonical perspectives on AmpR mediated ampC expression in Gram negative bacteria, with particular emphasis on the potential regulatory purview of FtsZ.World journal of microbiology & biotechnology · 2026Review
- Mapping the Binding Landscape of Allosteric Inhibitor G6PDi-1 on Human G6PD.The journal of physical chemistry letters · 2026Article
- An optimizedJournal of biomolecular NMR · 2025Article
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Structure of CFTR bound to (R)-BPO-27 unveils a pore-blockage mechanism.Nature communications · 2025Article
- Advances of Predicting Allosteric Mechanisms Through Protein Contact in New Technologies and Their Application.Molecular biotechnology · 2024Review
- Orthoflaviviral Inhibitors in Clinical Trials, Preclinical In Vivo Efficacy Targeting NS2B-NS3 and Cellular Antiviral Activity via Competitive Protease Inhibition.Molecules (Basel, Switzerland) · 2024Review
- Carbon Monoxide-Sensing Transcription Factors: Regulators of Microbial Carbon Monoxide Oxidation Pathway Gene Expression.Journal of bacteriology · 2023Review
- An NMR portrait of functional and dysfunctional allosteric cooperativity in cAMP-dependent protein kinase A.FEBS letters · 2023Review
- cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor.Journal of microbiology (Seoul, Korea) · 2023Review
- The "violin model": Looking at community networks for dynamic allostery.The Journal of chemical physics · 2023Review
- ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.Science advances · 2022Article
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
- Bacterial Transcriptional Regulators: A Road Map for Functional, Structural, and Biophysical Characterization.International journal of molecular sciences · 2022Review
- Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.Nature communications · 2021Article
- Discriminating between competing models for the allosteric regulation of oncogenic phosphatase SHP2 by characterizing its active state.Computational and structural biotechnology journal · 2021Article
- Conformational states dynamically populated by a kinase determine its function.Science (New York, N.Y.) · 2020Article
- Role of allosteric switches and adaptor domains in long-distance cross-talk and transient tunnel formation.Science advances · 2020Article
- Allosteric control of metal-responsive transcriptional regulators in bacteria.The Journal of biological chemistry · 2020Review
- Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A.Chemical science · 2020Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers several advantages over competitive inhibition, but the mechanisms of action remain poorly understood in most cases. Here we show that allosteric inhibition can be effected by destabilizing a low-populated conformational state that serves as an on-pathway intermediate for ligand binding, without altering the protein's ground-state structure. As standard structural approaches are typically concerned with changes in the ground-state structure of proteins, the presence of such a mechanism can go easily undetected. Our data strongly argue for the routine use of NMR tools suited to detect and characterize transiently formed conformational states in allosteric systems. Structure information on such important intermediates can ultimately result in more efficient design of allosteric inhibitors.
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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.