ArticleThe journal of physical chemistry. B2025
Allostery without Conformational Change: A Native Mass Spectrometry Perspective.
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Solution Phase Protein Dynamics: Influences of ESI Buffers on Hydration.Analytical chemistry · 2026Article
- Identification of Key Residues in Allosteric Signaling of Photoactivated Adenylyl Cyclase.bioRxiv : the preprint server for biology · 2026Article
- IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?The journal of physical chemistry. A · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Native electrospray ionization-mass spectrometry (nESI-MS) enables studies of intact proteins, protein complexes, and protein-ligand complexes. Variable temperature (vT)-nESI-MS, where the temperature of the solution contained in the ESI emitter can be varied from 2 to 100 °C, adds new capabilities for dissecting the thermodynamics for protein-ligand binding. Here, vT-nESI-MS and ion mobility spectrometry (IMS) are used to compare the effects of temperature and nESI buffers on nucleotide (ADP) binding for the GroEL single ring mutant (SR1). Temperature-dependent shifts for average charge states (
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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.