Evidence map›Paper›PMID 15653769›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Rhabdomeric phototransduction initiated by the vertebrate photopigment melanopsin.

Mauro Cesar Isoldi, Mark D Rollag, Ana Maria de Lauro Castrucci, Ignacio Provencio

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 163 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Melanopsin phototransduction: beyond canonical cascades.The Journal of experimental biology · 2021
    Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Phototransduction in Retinal Ganglion Cells.The Yale journal of biology and medicine · 2018
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Comparison of the isomerization mechanisms of human melanopsin and invertebrate and vertebrate rhodopsins.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Mauro Cesar IsoldiDepartment of Anatomy, Physiology, and Genetics, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814, USA.
Mark D Rollag
Ana Maria de Lauro Castrucci
Ignacio Provencio
Uniformed Services University of the Health Sciences · US

Funding

Photic Regulation of Circadian RhythmsR01NS052112 · NINDS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PROVENCIO, IGNACIO · 2005 to 2009
$1.5M
PHOTIC REGULATION OF CIRCADIAN RHYTHMSR01MH062405 · NIMH · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI PROVENCIO, IGNACIO · 2001 to 2004
$1.1M
NIMH NIH HHS R01 MH062405NIMH NIH HHS R01 MH62405NINDS NIH HHS R01 NS052112
6 · The paper itself

Abstract

Melanopsin is the photopigment that confers light sensitivity on intrinsically photosensitive retinal ganglion cells. Mammalian intrinsically photosensitive retinal ganglion cells are involved in the photic synchronization of circadian rhythms to the day-night cycle. Here, we report molecular components of melanopsin signaling using the cultured Xenopus dermal melanophore system. Photo-activated melanopsin is shown to initiate a phosphoinositide signaling pathway similar to that found in invertebrate photo-transduction. In melanophores, light increases the intracellular level of inositol trisphosphate and causes the dispersion of melanosomes. Inhibition of phospholipase C and protein kinase C and chelation of intracellular calcium block the effect of light on melanophores. At least four proteins, 43, 74, 90, and 134 kDa, are phosphorylated by protein kinase C upon light stimulation. This provides evidence of an invertebrate-like light-activated signaling cascade within vertebrate cells.

Indexed as

Light Signal TransductionAnimalsCalciumCyclic AMPCyclic GMPMelanopsinProtein Kinase CRod OpsinsType C PhospholipasesXenopusCalciumCyclic AMPCyclic GMPMelanopsinProtein Kinase CRod OpsinsType C Phospholipases

Identifiers

PMID15653769
PMCPMC545850
OpenAlexW2048112824

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.