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Cited by 975Circadian rhythm and melatoninmelanin and skin pigmentationPhotoreceptor and optogenetics research

The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.

Melanopsin: An opsin in melanophores, brain, and eye

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Provencio, Ignacio, Jiang, Guisen, De Grip, Willem J., Hayes, William Pär, Rollag, Mark D.·1998·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.95.1.340PMC PMC18217
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Abstract

We have identified an opsin, melanopsin, in photosensitive dermal melanophores of Xenopus laevis . Its deduced amino acid sequence shares greatest homology with cephalopod opsins. The predicted secondary structure of melanopsin indicates the presence of a long cytoplasmic tail with multiple putative phosphorylation sites, suggesting that this opsin’s function may be finely regulated. Melanopsin mRNA is expressed in hypothalamic sites thought to contain deep brain photoreceptors and in the iris, a structure known to be directly photosensitive in amphibians. Melanopsin message is also localized in retinal cells residing in the outermost lamina of the inner nuclear layer where horizontal cells are typically found. Its expression in retinal and nonretinal tissues suggests a role in vision and nonvisual photoreceptive tasks, such as photic control of skin pigmentation, pupillary aperture, and circadian and photoperiodic physiology.

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Crossref · 10.1073/pnas.95.1.340

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Research works printed but not linked: 4

  1. K Hofmann, W Stoffel Biol Chem Hoppe-Seyler 347, 166 (1993).
  2. N Saitou, M Nei Mol Biol Evol 4, 406–425 (1987).
  3. T Yoshikawa, Y Yashiro, T Oishi, K Kokame, Y Fukada Zool Sci 11, 675–680 (1994).
  4. M Jiang, S Pandey, H K Fong Invest Ophthalmol Visual Sci 34, 3669–3678 (1993).

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Metadata

Authors
Provencio, I., Jiang, G., De Grip, W. J., Hayes, W. P., & Rollag, M. D.
Affiliations
  • Uniformed Services University of the Health Sciences (US)
  • Department of Anatomy and Cell Biology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814; Institute of Cellular Signaling, University of Nijmegen, 6500 HB Nijmegen, The Netherlands; and Department of Biology, The Catholic University of America, Washington, DC 20064
ORCID
Provencio, Ignacio
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1998-01-06
Volume
95
Issue
1
Pages
340-345
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.95.1.340
PMC
PMC18217
OpenAlex
W1971524741
Semantic Scholar
65bdc3eb7e2fb5d60b2f8f75ea76a9d735399611
Cited by
975
References
43
Citations by year
2026: 20 · 2025: 42 · 2024: 27 · 2023: 50 · 2022: 43 · 2021: 46 · 2020: 48 · 2019: 28 · 2018: 39 · 2017: 52 · 2016: 47 · 2015: 36 · 2014: 48 · 2013: 41 · 2012: 41
FWCI
6.98
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Radboud Repository (Radboud University) (submittedVersion)
Topics
  • Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Keywords
melanopsin, opsin, melanophores, Xenopus laevis, amino acid sequence homology, cytoplasmic tail, phosphorylation sites, retinal horizontal cells, inner nuclear layer, non-visual photoreception, circadian physiology
MeSH terms
Melanopsin, Amino Acid Sequence, Animals, Brain Chemistry, Cells, Cultured, Eye, Melanophores, Molecular Sequence Data, Xenopus laevis, Sequence Alignment, Rod Opsins, In Situ Hybridization, Protein Structure, Secondary, DNA, Complementary

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