ArticleACS omega2025
Can Macromolecular Crowding Help Regulate Glutamate Dehydrogenase Activity?
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Crowder-specific modulation of hepatitis C virus NS3/4A protease activity and local structural dynamics.Protein science : a publication of the Protein Society · 2026Article
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate dehydrogenase (GDH) is an important mitochondrial enzyme that is positioned at the intersection of several central metabolic pathways. Since this enzyme influences the flux of crucial metabolites, GDH activity is tightly controlled by a complex network of allosteric effectors, and disruption of this regulation has been correlated with a growing list of diseases. To better understand how the crowded environment and pH fluctuations of the mitochondrial matrix contribute to the fine-tuning of GDH regulation, Michaelis-Menten kinetics were measured in the presence of both synthetic and protein crowding agents. The results show a pH-dependent decrease in the GDH activity regardless of crowder identity. Specifically, macromolecular crowding favors the closed GDH conformation, thereby slowing product release. In addition, the presence of dextran increases the p
Identifiers
What Socratic 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 Socratic graph.