ArticleJournal of the American Chemical Society2014
Human cellular retinaldehyde-binding protein has secondary thermal 9-cis-retinal isomerase activity.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Chromophore-loaded CRALBP mutant proteins restore rod function in chromophore-deficient mice.Molecular therapy. Advances · 2026Article
- Mechanisms and Functions of Chromophore Regeneration in the Classical Visual Cycle: Implications for Retinal Disease Pathogenesis and Therapy.Biomolecules · 2025Review
- Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs.Nature communications · 2023Article
- Vitamin A aldehyde-taurine adduct and the visual cycle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Shedding new light on the generation of the visual chromophore.Proceedings of the National Academy of Sciences of the United States of America · 2020Review
- Photic generation of 11-The Journal of biological chemistry · 2019Article
- Increasing the Stability of Recombinant Human Green Cone Pigment.Biochemistry · 2018Article
- Molecular Basis for Vitamin A Uptake and Storage in Vertebrates.Nutrients · 2016Review
- Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
Abstract
Cellular retinaldehyde-binding protein (CRALBP) chaperones 11-cis-retinal to convert opsin receptor molecules into photosensitive retinoid pigments of the eye. We report a thermal secondary isomerase activity of CRALBP when bound to 9-cis-retinal. UV/vis and (1)H NMR spectroscopy were used to characterize the product as 9,13-dicis-retinal. The X-ray structure of the CRALBP mutant R234W:9-cis-retinal complex at 1.9 Å resolution revealed a niche in the binding pocket for 9-cis-aldehyde different from that reported for 11-cis-retinal. Combined computational, kinetic, and structural data lead us to propose an isomerization mechanism catalyzed by a network of buried waters. Our findings highlight a specific role of water molecules in both CRALBP-assisted specificity toward 9-cis-retinal and its thermal isomerase activity yielding 9,13-dicis-retinal. Kinetic data from two point mutants of CRALBP support an essential role of Glu202 as the initial proton donor in this isomerization reaction.
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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.