Evidence map›Paper›PMID 19307608›Full record

ArticleGenetics2009

Quantifying interactions within the NADP(H) enzyme network in Drosophila melanogaster.

Thomas J S Merritt, Caitlin Kuczynski, Efe Sezgin, Chen-Tseh Zhu, Seiji Kumagai, Walter F Eanes

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Significance of Malic Enzyme 1 in Cancer: A Review.Current issues in molecular biology · 2025
    Review
  3. SREBP modulates the NADPNature communications · 2023
    Article
  4. Article
  5. Article
  6. Article
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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

6 authors at 3 institutions in 2 countries.

Thomas J S MerrittDepartment of Ecology and Evolution, Stony Brook University, Stony Brook, NY 11794, USA. tmerritt@laurentian.ca
Caitlin Kuczynski
Efe Sezgin
Chen-Tseh Zhu
Seiji Kumagai
Walter F Eanes
Stony Brook University · USDuke University · USLaurentian University · CA

Funding

METABOLIC CONTROL AND MOLECULAR ADAPTATION IN DROSOPHILAR01GM045247 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI EANES, WALTER F. · 1991 to 2005
$1.3M
NIGMS NIH HHS GM-45247NIGMS NIH HHS R01 GM045247
6 · The paper itself

Abstract

In this report, we use synthetic, activity-variant alleles in Drosophila melanogaster to quantify interactions across the enzyme network that reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH. We examine the effects of large-scale variation in isocitrate dehydrogenase (IDH) or glucose-6-phosphate dehydrogenase (G6PD) activity in a single genetic background and of smaller-scale variation in IDH, G6PD, and malic enzyme across 10 different genetic backgrounds. We find significant interactions among all three enzymes in adults; changes in the activity of any one source of a reduced cofactor generally result in changes in the other two, although the magnitude and directionality of change differs depending on the gene and the genetic background. Observed interactions are presumably through cellular mechanisms that maintain a homeostatic balance of NADPH/NADP, and the magnitude of change in response to modification of one source of reduced cofactor likely reflects the relative contribution of that enzyme to the cofactor pool. Our results suggest that malic enzyme makes the largest single contribution to the NADPH pool, consistent with the results from earlier experiments in larval D. melanogaster using naturally occurring alleles. The interactions between all three enzymes indicate functional interdependence and underscore the importance of examining enzymes as components of a network.

Indexed as

AllelesAnimalsChromosomesDrosophila melanogasterGenetic VariationGenotypeGlucosephosphate DehydrogenaseIsocitrate DehydrogenaseMalate DehydrogenaseNADPOxidation-ReductionProtein BindingTriglyceridesGlucosephosphate DehydrogenaseIsocitrate DehydrogenaseMalate DehydrogenaseNADPTriglycerides

Identifiers

PMID19307608
PMCPMC2691764
OpenAlexW2167496721

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.