ArticleStructure (London, England : 1993)2010
Nanometer propagation of millisecond motions in V-type allostery.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- Boosting Reversible Photocontrol of a Photoxenase by an Engineered Conformational Shift.Angewandte Chemie (International ed. in English) · 2026Article
- A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025Review
- Illuminating Protein Allostery by Chemically Accurate Contact Response Analysis (ChACRA).Journal of chemical theory and computation · 2024Article
- Catalytic Effects of Active Site Conformational Change in the Allosteric Activation of Imidazole Glycerol Phosphate Synthase.ACS catalysis · 2023Article
- Mixed, nonclassical behavior in a classic allosteric protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase.Nature communications · 2023Article
- Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase.Journal of the American Chemical Society · 2022Article
- A simple method to determine changes in the affinity between HisF and HisH in the Imidazole Glycerol Phosphate Synthase heterodimer.PloS one · 2022Article
- Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.Nature communications · 2021Article
- Community Network Analysis of Allosteric Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- NMR and computational methods for molecular resolution of allosteric pathways in enzyme complexes.Biophysical reviews · 2020Review
- Propagation of the Allosteric Signal in Phosphofructokinase fromBiochemistry · 2019Article
- Light Regulation of Enzyme Allostery through Photo-responsive Unnatural Amino Acids.Cell chemical biology · 2019Article
- Reaching the sparse-sampling limit for reconstructing a single peak in a 2D NMR spectrum using iterated maps.Journal of biomolecular NMR · 2019Article
- Accelerating 2D NMR relaxation dispersion experiments using iterated maps.Journal of biomolecular NMR · 2019Article
- Mechanism of allosteric activation of human mRNA cap methyltransferase (RNMT) by RAM: insights from accelerated molecular dynamics simulations.Nucleic acids research · 2019Article
- Review
- Exploring Allosteric Pathways of a V-Type Enzyme with Dynamical Perturbation Networks.The journal of physical chemistry. B · 2019Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Imidazole glycerol phosphate synthase (IGPS) is a V-type allosteric enzyme, which is catalytically inactive for glutamine hydrolysis until the allosteric effector, N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) binds 30 Å away. In the apo state, NMR relaxation dispersion experiments indicate the absence of millisecond (ms) timescale motions. Binding of the PRFAR to form the active ternary complex is endothermic with a large positive entropy change. In addition, there is a protein wide enhancement of conformational motions in the ternary complex, which connect the two active sites. NMR chemical shift changes and acrylamide quenching experiments suggest that little in the way of structural changes accompany these motions. The data indicate that enzyme activation in the ternary complex is primarily due to an enhancement of ms motions that allows formation of a population of enzymatically active conformers.
Indexed as
Identifiers
What OpenQuestion holds
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.