ArticleNanoscale advances2025
Preserving enzyme conformation and catalytic efficiency in crowded and active environments.
Article in Nanoscale advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
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Who cites it
1 citing paper in PubMed.
- Enzymatic Nanomotors Integrated with Plant Extracts: Biochemical Mechanisms, Applications, and Clinical Perspectives.Molecules (Basel, Switzerland) · 2026Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins operate in dynamic environments where interactions and fluctuations influence their structure and function. Understanding how these factors contribute to enzyme stability is essential for both fundamental biology and practical applications. Here, we investigate the role of protein-protein interactions and non-thermal active fluctuations in enzyme conformational dynamics and catalytic activity. Our findings reveal that in a dense suspension, enzyme catalytic activity and structural integrity are preserved for extended periods. Additionally, we observed that mechanical fluctuations generated by enzyme catalytic reactions help sustain enzymatic activity over longer timescales.
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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.