Evidence map›Paper›PMID 19251690›Full record

ArticleThe Journal of biological chemistry2009

Hydrolase regulates NAD+ metabolites and modulates cellular redox.

Lei Tong, Susan Lee, John M Denu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 70 citations in OpenAlex.

  1. Structural genome variation drives adaptation of the xylose-fermenting yeast Scheffersomyces stipitis to lignocellulosic hydrolysates.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. CD38/ADP-ribose/TRPM2-mediated nuclear CaExperimental & molecular medicine · 2023
    Article
  8. Dual amplification strategy turns TRPM2 channels into supersensitive central heat detectors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. SIRT3 Enhances Mesenchymal Stem Cell Longevity and Differentiation.Oxidative medicine and cellular longevity · 2017
    Article
  17. Article
  18. Article
  19. Review
  20. Loss of SIRT3 Provides Growth Advantage for B Cell Malignancies.The Journal of biological chemistry · 2016
    Article
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

3 authors at 1 institution in 1 country.

Lei TongDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706, USA.
Susan Lee
John M Denu
University of Wisconsin–Madison · US

Funding

Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
NIGMS NIH HHS R01 GM065386
6 · The paper itself

Abstract

Although the classical redox functions of co-enzyme NAD(+) are firmly established in metabolism, there are numerous enzymes that catalyze cleavage of NAD(+) to yield free ADP-ribose (ADPr) or related metabolites, whose functions remain largely unknown. Here we show that the Nudix (nucleoside diphosphate linked to another moiety X) hydrolase Ysa1 from Saccharomyces cerevisiae is a major regulator of cellular ADPr and O-acetyl-ADP-ribose (OAADPr). OAADPr is the direct product of NAD(+)-dependent protein deacetylases (sirtuins) and is readily converted to ADPr. Ysa1 cleaves ADPr/OAADPr into ribose phosphate/acetyl-ribose phosphate and AMP. In cells lacking Ysa1 (Deltaysa1), ADPr and OAADPr levels increased approximately 50%, with a corresponding decrease in AMP. Strikingly, Deltaysa1 cells display higher resistance to exogenous reactive oxygen species (ROS) and 40% lower basal levels of endogenous ROS, compared with wild type. The biochemical basis for these differences in ROS-related phenotypes was investigated, and the results provide evidence that increased ADPr/OAADPr levels protect cells via the following two pathways: (i) lower ROS production through inhibition of complex I of the mitochondrial electron transport chain, and (ii) generation of higher levels of NADPH to suppress ROS damage. The latter occurs through diverting glucose into the pentose phosphate pathway by ADPr inhibition of glyceraldehyde-3-phosphate dehydrogenase, a central enzyme of glycolysis.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, FungalOxidation-ReductionGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisHydrolasesKineticsMembrane PotentialsModels, BiologicalNADNudix HydrolasesPhenotypePyrophosphatasesReactive Oxygen SpeciesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)HydrolasesNADNudix HydrolasesPyrophosphatasesReactive Oxygen SpeciesSaccharomyces cerevisiae ProteinsTDH1 protein, S cerevisiaeYsa1 protein, S cerevisiae

Identifiers

PMID19251690
PMCPMC2670130
OpenAlexW2008483777

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.