Evidence map›Paper›PMID 20880841›Full record

ArticleThe Journal of biological chemistry2010

Time-resolved measurements of intracellular ATP in the yeast Saccharomyces cerevisiae using a new type of nanobiosensor.

Veli C Ozalp, Tina R Pedersen, Lise J Nielsen, Lars F Olsen

Open access · hybridAbstract readEvaluation Study
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 118 citations in OpenAlex.

  1. Inositol biosynthesis is inversely regulated by glycolytic activity.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Article
  2. Article
  3. An optical BOD biosensor based on intracellular ATP measurements in genetically modified Saccharomyces cerevisiae.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Article
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  12. Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)Archives of biochemistry and biophysics · 2021
    Article
  13. Review
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  15. Nucleic-Acid Structures as Intracellular Probes for Live Cells.Advanced materials (Deerfield Beach, Fla.) · 2020
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Veli C OzalpDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK5230 Odense M, Denmark.
Tina R Pedersen
Lise J Nielsen
Lars F Olsen
University of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenosine 5'-triphosphate is a universal molecule in all living cells, where it functions in bioenergetics and cell signaling. To understand how the concentration of ATP is regulated by cell metabolism and in turn how it regulates the activities of enzymes in the cell it would be beneficial if we could measure ATP concentration in the intact cell in real time. Using a novel aptamer-based ATP nanosensor, which can readily monitor intracellular ATP in eukaryotic cells with a time resolution of seconds, we have performed the first on-line measurements of the intracellular concentration of ATP in the yeast Saccharomyces cerevisiae. These ATP measurements show that the ATP concentration in the yeast cell is not stationary. In addition to an oscillating ATP concentration, we also observe that the concentration is high in the starved cells and starts to decrease when glycolysis is induced. The decrease in ATP concentration is shown to be caused by the activity of membrane-bound ATPases such as the mitochondrial F(0)F(1) ATPase-hydrolyzing ATP and the plasma membrane ATPase (PMA1). The activity of these two ATPases are under strict control by the glucose concentration in the cell. Finally, the measurements of intracellular ATP suggest that 2-deoxyglucose (2-DG) may have more complex function than just a catabolic block. Surprisingly, addition of 2-DG induces only a moderate decline in ATP. Furthermore, our results suggest that 2-DG may inhibit the activation of PMA1 after addition of glucose.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBiosensing TechniquesGlycolysisIntracellular SpaceNanotechnologySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateSaccharomyces cerevisiae Proteins

Identifiers

PMID20880841
PMCPMC2988363
OpenAlexW2099215399

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.