ArticleACS central science2019
Single-Molecule Mechanistic Study of Enzyme Hysteresis.
Article in ACS central science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- Single-molecule kinetic exploration of functional sub-states in an evolving phosphotriesterase.Nature communications · 2026Article
- Development of Cathepsin B‑Activatable Cell-Penetrating Peptides for Tumor Targeting.ACS pharmacology & translational science · 2026Article
- Anfinsen Redux: Ribonuclease Folding in the Single-Molecule Regime.Journal of the American Chemical Society · 2025Article
- Time-Dependent Kinetic Complexities in Enzyme Assays: A Review.Biomolecules · 2025Review
- Dietary flavonoids form supramolecular assemblies, alter biochemistry, and enhance cell resilience.Frontiers in nutrition · 2025Article
- Functional analysis of single enzymes combining programmable molecular circuits with droplet-based microfluidics.Nature nanotechnology · 2024Article
- Digital Cascade Assays for ADP- or ATP-Producing Enzymes Using a Femtoliter Reactor Array Device.ACS sensors · 2023Article
- Genetic Perturbation Alters Functional Substates in Alkaline Phosphatase.Journal of the American Chemical Society · 2023Article
- Abnormal Expression of an Insulin Synthesizing Enzyme in Islets of Adult Autoantibody Positive Donors.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2022Article
- Single-molecule studies reveal method for tuning the heterogeneous activity of alkaline phosphatase.Biophysical journal · 2022Article
- Amphiphilic Membrane Environments Regulate Enzymatic Behaviors ofACS bio & med chem Au · 2022Article
- A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities.Antimicrobial agents and chemotherapy · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hysteresis is an important feature of enzyme-catalyzed reactions, as it reflects the influence of enzyme regulation in the presence of ligands such as substrates or allosteric molecules. In typical kinetic studies of enzyme activity, hysteretic behavior is observed as a "lag" or "burst" in the time course of the catalyzed reaction. These lags and bursts are due to the relatively slow transition from one state to another state of the enzyme molecule, with different states having different kinetic properties. However, it is difficult to understand the underlying mechanism of hysteresis by observing bulk reactions because the different enzyme molecules in the population behave stochastically. In this work, we studied the hysteretic behavior of mutant β-glucuronidase (GUS) using a high-throughput single-molecule array platform and investigated the effect of thermal treatment on the hysteresis.
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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.