ArticleJournal of visualized experiments : JoVE2016
Measuring In Vitro ATPase Activity for Enzymatic Characterization.
Article in Journal of visualized experiments : JoVE, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
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- A comprehensive structural analysis of the ATPase domain of human DNA topoisomerase II beta bound to AMPPNP, ADP, and the bisdioxopiperazine, ICRF193.Structure (London, England : 1993) · 2022Article
- Measuring the impact of cofactors on RNA helicase activities.Methods (San Diego, Calif.) · 2022Article
- PMS2 variant results in loss of ATPase activity without compromising mismatch repair.Molecular genetics & genomic medicine · 2022Article
- PTEN/AKT/mTOR pathway involvement in autophagy, mediated by miR-99a-3p and energy metabolism in ammonia-exposed chicken bursal lymphocytes.Poultry science · 2021Article
- Chronic cardiac structural damage, diastolic and systolic dysfunction following acute myocardial injury due to bromine exposure in rats.Archives of toxicology · 2021Article
- Decanoic acid inhibits mTORC1 activity independent of glucose and insulin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Description of Druglike Properties of Safranal and Its Chemistry behind Low Oral Exposure.ACS omega · 2020Article
- Measurement of ATPase Activity of Valosin-containing Protein/p97.Bio-protocol · 2020Article
- A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors.Journal of visualized experiments : JoVE · 2019Article
- Rab5-dependent autophagosome closure by ESCRT.The Journal of cell biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. The protocol described here is a basic assay for measuring the in vitro activity of purified ATPases for functional characterization. Proteins hydrolyze ATP in a reaction that results in inorganic phosphate release, and the amount of phosphate liberated is then quantitated using a colorimetric assay. This highly adaptable protocol can be adjusted to measure ATPase activity in kinetic or endpoint assays. A representative protocol is provided here based on the activity and requirements of EpsE, the AAA+ ATPase involved in Type II Secretion in the bacterium Vibrio cholerae. The amount of purified protein needed to measure activity, length of the assay and the timing and number of sampling intervals, buffer and salt composition, temperature, co-factors, stimulants (if any), etc. may vary from those described here, and thus some optimization may be necessary. This protocol provides a basic framework for characterizing ATPases and can be performed quickly and easily adjusted as necessary.
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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.