Evidence map›Paper›PMID 25549576›Full record

ArticleChemico-biological interactions2015

Aldehyde dehydrogenase homologous folate enzymes: Evolutionary switch between cytoplasmic and mitochondrial localization.

Natalia I Krupenko, Roger S Holmes, Yaroslav Tsybovsky, Sergey A Krupenko

Abstract read
In one paragraph

Article in Chemico-biological interactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Peripheral catecholamine systems: an evolutionary perspective.American journal of physiology. Regulatory, integrative and comparative physiology · 2025
    Review
  2. Review
  3. Versatile function of NF-ĸB in inflammation and cancer.Experimental hematology & oncology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
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.

Natalia I KrupenkoDepartment of Nutrition, UNC-Chapel Hill, UNC Nutrition Research Institute, Kannapolis, NC 28081, United States.
Roger S HolmesThe Eskitis Institute for Drug Discovery and School of Natural Sciences, Griffith University, Nathan, 4111 Brisbane, Queensland, Australia.
Yaroslav TsybovskyDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, United States.
Sergey A KrupenkoDepartment of Nutrition, UNC-Chapel Hill, UNC Nutrition Research Institute, Kannapolis, NC 28081, United States. Electronic address: sergey_krupenko@unc.edu.

Funding

MECHANISM OF ACTIONS OF A MAJOR FOLATE ENZYMER01DK054388 · NIDDK · VANDERBILT UNIVERSITY · PI KRUPENKO, SERGEY A · 1998 to 2015
$4.7M
FDH: A Novel Determinant of Tumor SuppressionR01CA095030 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KRUPENKO, SERGEY A · 2005 to 2014
$2.5M
NCI NIH HHS CA095030NCI NIH HHS R01 CA095030NIDDK NIH HHS DK054388NIDDK NIH HHS R01 DK054388
6 · The paper itself

Abstract

Cytosolic and mitochondrial 10-formyltetrahydrofolate dehydrogenases are products of separate genes in vertebrates but only one such gene is present in invertebrates. There is a significant degree of sequence similarity between the two enzymes due to an apparent origin of the gene for the mitochondrial enzyme (ALDH1L2) from the duplication of the gene for the cytosolic enzyme (ALDH1L1). The primordial ALDH1L gene originated from a natural fusion of three unrelated genes, one of which was an aldehyde dehydrogenase. Such structural organization defined the catalytic mechanism of these enzymes, which is similar to that of aldehyde dehydrogenases. Here we report the analysis of ALDH1L1 and ALDH1L2 genes from different species and their phylogeny and evolution. We also performed sequence and structure comparison of ALDH1L enzymes possessing aldehyde dehydrogenase catalysis to those lacking this feature in an attempt to explain mechanistic differences between cytoplasmic ALDH1L1 and mitochondrial ALDH1L2 enzymes and to better understand their functional roles.

Indexed as

Aldehyde DehydrogenaseAmino Acid SequenceAnimalsCytoplasmEvolution, MolecularFolic AcidHumansInvertebratesMitochondriaPhylogenyVertebratesZebrafishAldehyde DehydrogenaseFolic AcidAldehyde dehydrogenasesALDH1L enzymesEnzyme mechanismEvolutionFolate metabolismMitochondria

Identifiers

PMID25549576
PMCPMC4414694

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Registered trials

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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.