Evidence map›Paper›PMID 32061750›Full record

ReviewBiochimica et biophysica acta. Molecular and cell biology of lipids2020

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases.

Eugenia Poliakov, Sheetal Uppal, Igor B Rogozin, Susan Gentleman, T Michael Redmond

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Functional Analysis of β-Carotene Oxygenase 2 (International journal of molecular sciences · 2024
    Article
  8. Article
  9. Review
  10. Predicting potentially pathogenic effects ofJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  11. Article
  12. Retinal pigment epithelium 65 kDa protein (RPE65): An update.Progress in retinal and eye research · 2022
    Review
  13. Article
  14. Article
  15. Shedding new light on the generation of the visual chromophore.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Review
  16. Palmitoylation of Metazoan Carotenoid Oxygenases.Molecules (Basel, Switzerland) · 2020
    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

5 authors at 2 institutions in 1 country.

Eugenia PoliakovLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: poliakove@nei.nih.gov.
Sheetal UppalLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Igor B RogozinNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Susan GentlemanLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
T Michael RedmondLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
National Eye Institute · USNational Institutes of Health · US

Funding

Molecular Biology Of Outer Retina-specific ProteinsZIAEY000260 · NEI · NATIONAL EYE INSTITUTE · PI REDMOND, T. MICHAEL · 2009 to 2025
$26.0M
MOLECULAR BIOLOGY OF OUTER RETINA-SPECIFIC PROTEINSZ01EY000260 · NEI · NATIONAL EYE INSTITUTE · PI REDMOND, THOMAS M · 1990 to 2008
$3.7M
Intramural NIH HHS Z01 EY000260
6 · The paper itself

Abstract

The carotenoids are terpenoid fat-soluble pigments produced by plants, algae, and several bacteria and fungi. They are ubiquitous components of animal diets. Carotenoid cleavage oxygenase (CCO) superfamily members are involved in carotenoid metabolism and are present in all kingdoms of life. Throughout the animal kingdom, carotenoid oxygenases are widely distributed and they are completely absent only in two unicellular organisms, Monosiga and Leishmania. Mammals have three paralogs 15,15'-β-carotene oxygenase (BCO1), 9',10'-β-carotene oxygenase (BCO2) and RPE65. The first two enzymes are classical carotenoid oxygenases: they cleave carbon‑carbon double bonds and incorporate two atoms of oxygen in the substrate at the site of cleavage. The third, RPE65, is an unusual family member, it is the retinoid isomerohydrolase in the visual cycle that converts all-trans-retinyl ester into 11-cis-retinol. Here we discuss evolutionary aspects of the carotenoid cleavage oxygenase superfamily and their enzymology to deduce what insight we can obtain from their evolutionary conservation.

Indexed as

Evolution, MolecularAnimalsbeta-Carotene 15,15'-MonooxygenaseCarotenoidscis-trans-IsomerasesDioxygenasesLipid MetabolismMammalsOxygenasesRetinoid IsomerohydrolaseBCO1 protein, humanBCO2 protein, humanbeta-Carotene 15,15'-Monooxygenasecarotenoid oxygenaseCarotenoidscis-trans-IsomerasesDioxygenasesOxygenasesRetinoid IsomerohydrolaseBCO2Carotenoid oxygenasesCarotenoidsEnzymesMembrane associated proteinsPalmitoylationPhylogeneticRPE65

Identifiers

PMID32061750
PMCPMC7423639
OpenAlexW3005918486

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.