Evidence map›Paper›PMID 11158606›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Analysis of the blind Drosophila mutant ninaB identifies the gene encoding the key enzyme for vitamin A formation invivo.

J von Lintig, A Dreher, C Kiefer, M F Wernet, K Vogt

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

63 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. A Loss-of-Function Mutation inAnimals : an open access journal from MDPI · 2026
    Article
  3. Functional Analysis of theBiotech (Basel (Switzerland)) · 2026
    Article
  4. Article
  5. Vitamin A supply in the eye and establishment of the visual cycle.Current topics in developmental biology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Aster proteins mediate carotenoid transport in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  17. Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  18. The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  19. Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Review

3 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

5 authors at 1 institution in 1 country.

J von LintigAlbert-Ludwig University of Freiburg, Institute for Biology I, Neurobiology and Animal Physiology, Hauptstrasse 1, D-79104 Freiburg, Germany. lintig@uni-freiburg.de
A Dreher
C Kiefer
M F Wernet
K Vogt
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Visual pigments (rhodopsins) are composed of a chromophore (vitamin A derivative) bound to a protein moiety embedded in the retinal membranes. Animals cannot synthesize the visual chromophore de novo but rely on the uptake of carotenoids, from which vitamin A is formed enzymatically by oxidative cleavage. Despite its importance, the enzyme catalyzing the key step in vitamin A formation resisted molecular analyses until recently, when the successful cloning of a cDNA encoding an enzyme with beta,beta-carotene-15,15'-dioxygenase activity from Drosophila was reported. To prove its identity with the key enzyme for vitamin A formation in vivo, we analyzed the blind Drosophila mutant ninaB. In two independent ninaB alleles, we found mutations in the gene encoding the beta,beta-carotene-15,15'-dioxygenase. These mutations lead to a defect in vitamin A formation and are responsible for blindness of these flies.

Indexed as

MutationAmino Acid SequenceAmino Acid SubstitutionAnimalsBase Sequencebeta-Carotene 15,15'-MonooxygenaseBlindnessChickensCloning, MolecularCrosses, GeneticDrosophila melanogasterDrosophila ProteinsFemaleHeterozygoteHumansMalebeta-Carotene 15,15'-MonooxygenaseDrosophila ProteinsninaB protein, DrosophilaOxygenasesRecombinant ProteinsRhodopsinRNA, MessengerVitamin A

Identifiers

PMID11158606
PMCPMC14720
OpenAlexW2153265210

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.