ArticleeLife2022
Creation of photocyclic vertebrate rhodopsin by single amino acid substitution.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Interferometric imaging of the reversible rhodopsin dynamics in the living rat eye.Nature communications · 2025Article
- Discovery and design of photocyclic animal opsins: potential application to gene therapy from non-visual opsin research.Eye and vision (London, England) · 2025Review
- On the physiological processes underlying optoretinography [Invited].Biomedical optics express · 2025Review
- Modulating signalling lifetime to optimise a prototypical animal opsin for optogenetic applications.Pflugers Archiv : European journal of physiology · 2023Article
- Functional diversity and evolution in animal rhodopsins: Report for the session 11.Biophysics and physicobiology · 2023Article
- Convergent evolution of animal and microbial rhodopsins.RSC advances · 2023Review
- Structural view of G protein-coupled receptor signaling in the retinal rod outer segment.Trends in biochemical sciences · 2023Review
- Welcome to the borderless rhodopsin world.Biophysics and physicobiology · 2023Article
- Whole genome assembly of the armored loricariid catfish Ancistrus triradiatus highlights herbivory signatures.Molecular genetics and genomics : MGG · 2022Article
- Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Opsins are universal photoreceptive proteins in animals and can be classified into three types based on their photoreaction properties. Upon light irradiation, vertebrate rhodopsin forms a metastable active state, which cannot revert back to the original dark state via either photoreaction or thermal reaction. By contrast, after photoreception, most opsins form a stable active state which can photoconvert back to the dark state. Moreover, we recently found a novel type of opsins whose activity is regulated by photocycling. However, the molecular mechanism underlying this diversification of opsins remains unknown. In this study, we showed that vertebrate rhodopsin acquired the photocyclic and photoreversible properties upon introduction of a single mutation at position 188. This revealed that the residue at position 188 contributes to the diversification of photoreaction properties of opsins by its regulation of the recovery from the active state to the original dark state.
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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.