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
Open accessAbstract
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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“Visible light synchronizes the human biological clock in the suprachiasmatic nuclei of the hypothalamus to the solar 24‐hour cycle.”
From The inner clock-Blue light sets the human rhythm (2019) · cites this paper as [2]
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“It was not until 1998, when a new type of photoreceptor in the human eye was discovered 2 and later identified to be especially sensitive to blue light.”
From The inner clock-Blue light sets the human rhythm (2019) · cites this paper as [2]
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Action Spectrum for Melatonin Regulation in Humans: Evidence for a Novel Circadian Photoreceptor
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Self-citationStructure and Function of DNA Photolyase and Cryptochrome Blue-Light Photoreceptors
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A Novel Human Opsin in the Inner Retina
Provencio, I., Rodriguez, I. R., Jiang, G., Hayes, W. P., Moreira, E. F., & Rollag, M. D. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00600.2000 · Cited by 1,290
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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
- 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
- green
- europepmc.org
- 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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