ArticleVision research2006
Palmitylation of cone opsins.
Article in Vision research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Visual pigment evolution in Characiformes: The dynamic interplay of teleost whole-genome duplication, surviving opsins and spectral tuning.Molecular ecology · 2020Article
- Palmitoylation is a prerequisite for dimerization-dependent raftophilicity of rhodopsin.The Journal of biological chemistry · 2017Article
- The Degeneration and Apoptosis Patterns of Cone Photoreceptors inJournal of ophthalmology · 2017Article
- New insights into retinoid metabolism and cycling within the retina.Progress in retinal and eye research · 2013Review
- Binding of more than one retinoid to visual opsins.Biophysical journal · 2010Article
- Palmitoylation stabilizes unliganded rod opsin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Rpe65-/- and Lrat-/- mice: comparable models of leber congenital amaurosis.Investigative ophthalmology & visual science · 2008Article
- Quantitation of the effect of hydroxylamine on rhodopsin palmitylation.Photochemistry and photobiologyArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Palmitylation is a widespread modification in G-protein-coupled receptors and often a dynamic process. In rhodopsins, palmitylation is static on C322/C323. Red/green (M/LWS) cone opsins have no cysteines at corresponding positions and no palmitylation. Blue (SWS2) cone opsins have a single corresponding cysteine and mass spectrometric analysis showed partial palmitylation of salamander SWS2 cone opsin. Ultraviolet (SWS1) cone opsins have one corresponding cysteine, but only unpalmitylated opsin was observed for mouse and salamander. The results show that the static palmitylation found on rhodopsin is not found on cone opsins and suggest the possibility of an unidentified role for opsin palmitylation in cones.
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What OpenQuestion holds
Registered trials
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.