ArticleProtein science : a publication of the Protein Society2017
Large cosolutes, small cosolutes, and dihydrofolate reductase activity.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 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
17 citing papers in PubMed, 43 citations in OpenAlex.
- Crowder-specific modulation of hepatitis C virus NS3/4A protease activity and local structural dynamics.Protein science : a publication of the Protein Society · 2026Article
- Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.Protein science : a publication of the Protein Society · 2026Article
- Article
- Dynamic Cytoplasm: A Physical Regulator of Enzymatic Function.Biochemistry · 2025Review
- Modeling Facilitated Diffusion of Proteins in Crowded Environment.Sub-cellular biochemistry · 2025Review
- Cell stress and phase separation stabilize the monomeric state of pseudoisocyanine chloride employed as a self-assembly crowding sensor.Communications chemistry · 2024Article
- Magnetic Nanoparticle Support with an Ultra-Thin Chitosan Layer Preserves the Catalytic Activity of the Immobilized Glucose Oxidase.Nanomaterials (Basel, Switzerland) · 2024Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- Varying molecular interactions explain aspects of crowder-dependent enzyme function of a viral protease.PLoS computational biology · 2023Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.Biochemistry and biophysics reports · 2021Article
- Glucose Oxidase Immobilized on Magnetic Zirconia: Controlling Catalytic Performance and Stability.ACS omega · 2020Article
- An in vitro mimic of in-cell solvation for protein folding studies.Protein science : a publication of the Protein Society · 2020Article
- Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions.Biochemistry · 2019Article
- Protein shape modulates crowding effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
Corrections and comments
- Erratum issuedCORRECTION.2019
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Protein enzymes are the main catalysts in the crowded and complex cellular interior, but their activity is almost always studied in dilute buffered solutions. Studies that attempt to recreate the cellular interior in vitro often utilize synthetic polymers as crowding agents. Here, we report the effects of the synthetic polymer cosolutes Ficoll, dextran, and polyvinylpyrrolidone, and their respective monomers, sucrose, glucose, and 1-ethyl-2-pyrrolidone, on the activity of the 18-kDa monomeric enzyme, Escherichia coli dihydrofolate reductase. At low concentrations, reductase activity increases relative to buffer and monomers, suggesting a macromolecular effect. However, the effect decreases at higher concentrations, approaching, and, in some cases, falling below buffer values. We also assessed activity in terms of volume occupancy, viscosity, and the overlap concentration (where polymers form an interwoven mesh). The trends vary with polymer family, but changes in activity are within threefold of buffer values. We also compiled and analyzed results from previous studies and conclude that alterations of steady-state enzyme kinetics in solutions crowded with synthetic polymers are idiosyncratic with respect to the crowding agent and enzyme.
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.