"Retinaldehyde" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.
| Descriptor ID |
D012172
|
| MeSH Number(s) |
D02.047.850 D02.455.326.271.665.202.495.690 D02.455.426.392.368.367.379.249.700.690 D02.455.849.131.495.690 D23.767.261.700.690
|
| Concept/Terms |
Retinaldehyde- Retinaldehyde
- Vitamin A Aldehyde
- Aldehyde, Vitamin A
- Retinene
- Axerophthal
- Retinal
|
Below are MeSH descriptors whose meaning is more general than "Retinaldehyde".
Below are MeSH descriptors whose meaning is more specific than "Retinaldehyde".
This graph shows the total number of publications written about "Retinaldehyde" by people in this website by year, and whether "Retinaldehyde" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 3 | 1 | 4 |
| 1995 | 1 | 0 | 1 |
| 1996 | 1 | 2 | 3 |
| 1999 | 3 | 0 | 3 |
| 2000 | 2 | 0 | 2 |
| 2001 | 1 | 0 | 1 |
| 2002 | 1 | 0 | 1 |
| 2003 | 0 | 2 | 2 |
| 2004 | 3 | 0 | 3 |
| 2005 | 4 | 3 | 7 |
| 2006 | 2 | 1 | 3 |
| 2007 | 1 | 0 | 1 |
| 2008 | 2 | 1 | 3 |
| 2009 | 2 | 0 | 2 |
| 2010 | 2 | 1 | 3 |
| 2011 | 2 | 1 | 3 |
| 2012 | 2 | 1 | 3 |
| 2013 | 0 | 1 | 1 |
| 2014 | 1 | 0 | 1 |
| 2015 | 1 | 0 | 1 |
| 2017 | 2 | 0 | 2 |
| 2020 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "Retinaldehyde" by people in Profiles.
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Relative Contributions of All-Trans and 11-Cis Retinal to Formation of Lipofuscin and A2E Accumulating in Mouse Retinal Pigment Epithelium. Invest Ophthalmol Vis Sci. 2021 02 01; 62(2):1.
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Photooxidation mediated by 11-cis and all-trans retinal in single isolated mouse rod photoreceptors. Photochem Photobiol Sci. 2020 Oct 14; 19(10):1300-1307.
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Interphotoreceptor retinoid-binding protein removes all-trans-retinol and retinal from rod outer segments, preventing lipofuscin precursor formation. J Biol Chem. 2017 11 24; 292(47):19356-19365.
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Biochemical Measurements of Free Opsin in Macular Degeneration Eyes: Examining the 11-CIS Retinal Deficiency Hypothesis of Delayed Dark Adaptation (An American Ophthalmological Society Thesis). Trans Am Ophthalmol Soc. 2017 Aug; 115:T1.
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The 11-cis Retinal Origins of Lipofuscin in the Retina. Prog Mol Biol Transl Sci. 2015; 134:e1-12.
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Ligand control of g protein-coupled receptor activity: new insights. Chem Biol. 2014 Mar 20; 21(3):309-10.
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Explant cultures of Rpe65-/- mouse retina: a model to investigate cone opsin trafficking. Mol Vis. 2013; 19:1149-57.
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Low aqueous solubility of 11-cis-retinal limits the rate of pigment formation and dark adaptation in salamander rods. J Gen Physiol. 2012 Jun; 139(6):493-505.
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Lipofuscin and N-retinylidene-N-retinylethanolamine (A2E) accumulate in retinal pigment epithelium in absence of light exposure: their origin is 11-cis-retinal. J Biol Chem. 2012 Jun 22; 287(26):22276-86.
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All-trans retinal mediates light-induced oxidation in single living rod photoreceptors. Photochem Photobiol. 2012 Nov-Dec; 88(6):1356-61.