ArticleACS chemical biology2015
A Fluorescent, Reagentless Biosensor for ATP, Based on Malonyl-Coenzyme A Synthetase.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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
9 citing papers in PubMed, 15 citations in OpenAlex.
- Rational design framework for fluorescent biosensors from periplasmic binding proteins.Bioscience reports · 2026Article
- Detection of Biomarker Using Aptasensors to Determine the Type of Diabetes.Diagnostics (Basel, Switzerland) · 2023Review
- Measurement of Nucleotide Hydrolysis Using Fluorescent Biosensors for Phosphate.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Review
- New frontiers in probing the dynamics of purinergic transmitters in vivo.Neuroscience research · 2020Review
- Crystallographic and kinetic analyses of human IPMK reveal disordered domains modulate ATP binding and kinase activity.Scientific reports · 2018Article
- Development of a range of fluorescent reagentless biosensors for ATP, based on malonyl-coenzyme A synthetase.PloS one · 2017Article
- Imaging Adenosine Triphosphate (ATP).The Biological bulletin · 2016Review
- "Click on the bidirectional switch": the aptasensor for simultaneous detection of lysozyme and ATP with high sensitivity and high selectivity.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A fluorescent reagentless biosensor for ATP has been developed, based on malonyl-coenzyme A synthetase from Rhodopseudomonas palustris as the protein scaffold and recognition element. Two 5-iodoacetamidotetramethylrhodamines were covalently bound to this protein to provide the readout. This adduct couples ATP binding to a 3.7-fold increase in fluorescence intensity with excitation at 553 nm and emission at 575 nm. It measures ATP concentrations with micromolar sensitivity and is highly selective for ATP relative to ADP. Its ability to monitor enzymatic ATP production or depletion was demonstrated in steady-state kinetic assays in which ATP is a product or substrate, respectively.
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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.