ArticleSensors (Basel, Switzerland)2009
Photoreactions and structural changes of anabaena sensory rhodopsin.
Article in Sensors (Basel, Switzerland), 2009. 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.
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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
8 citing papers in PubMed, 42 citations in OpenAlex.
- Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Reversible Photochromic Reactions of Bacteriorhodopsin fromMolecules (Basel, Switzerland) · 2024Article
- Biophysical characterization of microbial rhodopsins with DSE motif.Biophysics and physicobiology · 2023Article
- Excited-state dynamics of all-trans protonated retinal Schiff base in CRABPII-based rhodopsin mimics.Biophysical journal · 2022Article
- Modulation of Light Energy Transfer from Chromophore to Protein in the Channelrhodopsin ReaChR.Biophysical journal · 2020Article
- Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.The Journal of biological chemistry · 2017Article
- Structure of an Inward Proton-Transporting Anabaena Sensory Rhodopsin Mutant: Mechanistic Insights.Biophysical journal · 2016Article
- An inward proton transport using Anabaena sensory rhodopsin.Journal of microbiology (Seoul, Korea) · 2011Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anabaena sensory rhodopsin (ASR) is an archaeal-type rhodopsin found in eubacteria. The gene encoding ASR forms a single operon with ASRT (ASR transducer) which is a 14 kDa soluble protein, suggesting that ASR functions as a photochromic sensor by activating the soluble transducer. This article reviews the detailed photoreaction processes of ASR, which were studied by low-temperature Fourier-transform infrared (FTIR) and UV-visible spectroscopy. The former research reveals that the retinal isomerization is similar to bacteriorhodopsin (BR), but the hydrogen-bonding network around the Schiff base and cytoplasmic region is different. The latter study shows the stable photoproduct of the all-trans form is 100% 13-cis, and that of the 13-cis form is 100% all-trans. These results suggest that the structural changes of ASR in the cytoplasmic domain play important roles in the activation of the transducer protein, and photochromic reaction is optimized for its sensor function.
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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.