ReviewFrontiers in chemistry2022
Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.
Review in Frontiers in chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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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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
15 citing papers in PubMed, 30 citations in OpenAlex.
- Plasmonic Enhancement of Fluorescence and Protein Dynamics in Living Mammalian Cells.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026Article
- Optogenetic engineering of synthetic and natural receptors: design principles, functional mechanisms and biomedical applications.Regenerative biomaterials · 2026Review
- Controlling Single-Emitter Strong Coupling by Sculpting DNA Dye Scaffolds in NPoM Cavities.The journal of physical chemistry. C, Nanomaterials and interfaces · 2025Article
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals.Chemical reviews · 2024Review
- Tuning Two-Photon Absorption in Rhodopsin Chromophore via Backbone Modification: The Story Told by CC2 and TD-DFT.Journal of chemical theory and computation · 2024Article
- Merocyanines form bacteriorhodopsins with strongly bathochromic absorption maxima.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Article
- Association between micronutrients and myopia in American adolescents: evidence from the 2003-2006 National Health and Nutrition Examination Survey.Frontiers in nutrition · 2024Article
- Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023Review
- Combining different ion-selective channelrhodopsins to control water flux by light.Pflugers Archiv : European journal of physiology · 2023Article
- Plastid-localized xanthorhodopsin increases diatom biomass and ecosystem productivity in iron-limited surface oceans.Nature microbiology · 2023Article
- A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.The journal of physical chemistry. B · 2023Article
- Voltage Imaging with Engineered Proton-Pumping Rhodopsins: Insights from the Proton Transfer Pathway.ACS physical chemistry Au · 2023Review
- Biophysical characterization of microbial rhodopsins with DSE motif.Biophysics and physicobiology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential.
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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 Socratic graph.