Evidence map›Paper›PMID 30794800›Full record

ReviewChemico-biological interactions2019

Loss of ALDH1L1 folate enzyme confers a selective metabolic advantage for tumor progression.

Sergey A Krupenko, Natalia I Krupenko

Abstract readReview
In one paragraph

Review in Chemico-biological interactions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. ALDH1L1 reverses CD8Journal of translational medicine · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. DHFR2 RNA directly regulates dihydrofolate reductase and its expression level impacts folate one carbon metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Sergey A KrupenkoDepartment of Nutrition, UNC-Chapel Hill, UNC Nutrition Research Institute, Kannapolis, NC, 28081, United States. Electronic address: sergey_krupenko@unc.edu.
Natalia I KrupenkoDepartment of Nutrition, UNC-Chapel Hill, UNC Nutrition Research Institute, Kannapolis, NC, 28081, United States.
University of North Carolina Health Care · US

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
Ceramide signaling in the regulation of cellular response to folate stressR01CA193782 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KRUPENKO, NATALIA IVANOVNA · 2015 to 2019
$1.7M
NCI NIH HHS R01 CA095030NCI NIH HHS R01 CA193782NIDDK NIH HHS R01 DK054388
6 · The paper itself

Abstract

ALDH1L1 (cytosolic 10-formyltetrahydrofolate dehydrogenase) is the enzyme in folate metabolism commonly downregulated in human cancers. One of the mechanisms of the enzyme downregulation is methylation of the promoter of the ALDH1L1 gene. Recent studies underscored ALDH1L1 as a candidate tumor suppressor and potential marker of aggressive cancers. In agreement with the ALDH1L1 loss in cancer, its re-expression leads to inhibition of proliferation and to apoptosis, but also affects migration and invasion of cancer cells through a specific folate-dependent mechanism involved in invasive phenotype. A growing body of literature evaluated the prognostic value of ALDH1L1 expression for cancer disease, the regulatory role of the enzyme in cellular proliferation, and associated metabolic and signaling cellular responses. Overall, there is a strong indication that the ALDH1L1 silencing provides metabolic advantage for tumor progression at a later stage when unlimited proliferation and enhanced motility become critical processes for the tumor expansion. Whether the ALDH1L1 loss is involved in tumor initiation is still an open question.

Indexed as

Aldehyde DehydrogenaseApoptosisDisease ProgressionDNA MethylationFolic AcidFormyltetrahydrofolate DehydrogenaseHumansNeoplasmsOxidoreductases Acting on CH-NH Group DonorsRNA InterferenceSignal TransductionTumor Suppressor Protein p53Aldehyde DehydrogenaseFolic AcidFormyltetrahydrofolate DehydrogenaseOxidoreductases Acting on CH-NH Group DonorsTumor Suppressor Protein p53ALDH1L1 promoter methylationCofilinFolate metabolismJNKp53Tumor suppression

Identifiers

PMID30794800
PMCPMC6433412
OpenAlexW2917654560

What OpenQuestion holds

Textmetadata
LicenceTDM
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.