Evidence map›Paper›PMID 26416885›Full record

ArticleThe Journal of biological chemistry2015

Retinal Attachment Instability Is Diversified among Mammalian Melanopsins.

Hisao Tsukamoto, Yoshihiro Kubo, David L Farrens, Mitsumasa Koyanagi, Akihisa Terakita, Yuji Furutani

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Divergence of Melanopsin's Intrinsic Properties and Downstream Actions.bioRxiv : the preprint server for biology · 2026
    Article
  2. Minimal Mimics and Maps of Natural Light for Mammals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  3. Article
  4. Spectral Tuning in Mammalian Melanopsins.Molecular biology and evolution · 2025
    Article
  5. Article
  6. A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  7. A self-inactivating invertebrate opsin optically drives biased signaling toward Gβγ-dependent ion channel modulation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. The Multistable Melanopsins of Mammals.Frontiers in ophthalmology · 2023
    Article
  9. Article
  10. Optogenetic Modulation of Ion Channels by Photoreceptive Proteins.Advances in experimental medicine and biology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Ectopic Expression of Mouse Melanopsin inThe Journal of biological chemistry · 2017
    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

6 authors at 5 institutions in 2 countries.

Hisao TsukamotoDepartment of Life and Coordination-Complex Molecular Science, Institute for Molecular Science, Okazaki, 444-8585, Japan,; Department of Structural Molecular Science, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa 240-0193, Japan,. Electronic address: tsukamoh@ims.ac.jp.
Yoshihiro KuboDivision of Biophysics and Neurobiology, Department of Molecular Physiology, National Institute for Physiological Sciences, Okazaki, Aichi 444-8585, Japan,; Department of Physiological Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa 240-0193, Japan.
David L FarrensDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239-3098.
Mitsumasa KoyanagiDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan.
Akihisa TerakitaDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan.
Yuji FurutaniDepartment of Life and Coordination-Complex Molecular Science, Institute for Molecular Science, Okazaki, 444-8585, Japan,; Department of Structural Molecular Science, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa 240-0193, Japan.
Osaka City University · JPInstitute for Molecular Science · JPNational Institute for Physiological Sciences · JPOregon Health & Science University · USThe Graduate University for Advanced Studies, SOKENDAI · JP

Funding

Structural Dynamics of Retinal Binding and ReleaseR01EY015436 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI FARRENS, DAVID L · 2006 to 2014
$2.6M
NEI NIH HHS R01 EY015436NEI NIH HHS R01EY015436
6 · The paper itself

Abstract

Melanopsins play a key role in non-visual photoreception in mammals. Their close phylogenetic relationship to the photopigments in invertebrate visual cells suggests they have evolved to acquire molecular characteristics that are more suited for their non-visual functions. Here we set out to identify such characteristics by comparing the molecular properties of mammalian melanopsin to those of invertebrate melanopsin and visual pigment. Our data show that the Schiff base linking the chromophore retinal to the protein is more susceptive to spontaneous cleavage in mammalian melanopsins. We also find this stability is highly diversified between mammalian species, being particularly unstable for human melanopsin. Through mutagenesis analyses, we find that this diversified stability is mainly due to parallel amino acid substitutions in extracellular regions. We propose that the different stability of the retinal attachment in melanopsins may contribute to functional tuning of non-visual photoreception in mammals.

Indexed as

Amino Acid SequenceAnimalsEvolution, MolecularFemaleGalagoGenetic VariationHumansLanceletsMammalsMelanopsinMiceModels, MolecularMolecular Sequence DataOocytesPapio anubisPhotoreceptor Cells, VertebrateMelanopsinRecombinant ProteinsRetinaldehydeRetinal PigmentsRod OpsinsSchiff Baseselectrophysiologymembrane proteinmolecular evolutionnon-visual photoreceptionphotoreceptorrhodopsinultraviolet-visible spectroscopy (UV-visible spectroscopy)

Identifiers

PMID26416885
PMCPMC4646394
OpenAlexW2254068170

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.