Evidence map›Paper›PMID 26216303›Full record

ReviewGene2015

Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15).

Igor Ivanov, Hartmut Kuhn, Dagmar Heydeck

Open access · greenAbstract readReview
In one paragraph

Review in Gene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

128 citing papers in PubMed, 214 citations in OpenAlex.

  1. PROTACs in cancer therapy: targeted degradation of GPX4, PARP and epigenetic regulators.Journal of enzyme inhibition and medicinal chemistry · 2026
    Review
  2. Article
  3. Article
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  7. Article
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  9. Review
  10. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  11. Allosteric properties of mammalian ALOX15 orthologs.The Journal of biological chemistry · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

68 more citing papers are in PubMed but not listed here.

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.

Igor IvanovInstitute of Biochemistry, Charité - University Medicine Berlin, Charitéplatz 1, CCO-Building, Virchowweg 6, D-10117 Berlin, Germany.
Hartmut KuhnInstitute of Biochemistry, Charité - University Medicine Berlin, Charitéplatz 1, CCO-Building, Virchowweg 6, D-10117 Berlin, Germany. Electronic address: hartmut.kuehn@charite.de.
Dagmar HeydeckInstitute of Biochemistry, Charité - University Medicine Berlin, Charitéplatz 1, CCO-Building, Virchowweg 6, D-10117 Berlin, Germany.
Charité - Universitätsmedizin Berlin · DE

Funding

The Gene Wiki: Community intelligence applied to gene annotationR01GM089820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I · 2010 to 2021
$5.2M
NIGMS NIH HHS GM089820NIGMS NIH HHS R01 GM089820
6 · The paper itself

Abstract

Lipoxygenases (LOX) form a family of lipid peroxidizing enzymes, which have been implicated in a number of physiological processes and in the pathogenesis of inflammatory, hyperproliferative and neurodegenerative diseases. They occur in two of the three domains of terrestrial life (bacteria, eucarya) and the human genome involves six functional LOX genes, which encode for six different LOX isoforms. One of these isoforms is ALOX15, which has first been described in rabbits in 1974 as enzyme capable of oxidizing membrane phospholipids during the maturational breakdown of mitochondria in immature red blood cells. During the following decades ALOX15 has extensively been characterized and its biological functions have been studied in a number of cellular in vitro systems as well as in various whole animal disease models. This review is aimed at summarizing the current knowledge on the protein-chemical, molecular biological and enzymatic properties of ALOX15 in various species (human, mouse, rabbit, rat) as well as its implication in cellular physiology and in the pathogenesis of various diseases.

Indexed as

AnimalsArachidonate 15-LipoxygenaseHumansIsoenzymesProtein ConformationArachidonate 15-LipoxygenaseIsoenzymesEicosanoidsEnzymologyEvolutionLeukotrienesLipid metabolismLipoxygenase

Identifiers

PMID26216303
PMCPMC6728142
OpenAlexW2184888523

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.