ArticleJournal of biological physics2012
Conformational changes in the archaerhodopsin-3 proton pump: detection of conserved strongly hydrogen bonded water networks.
Article in Journal of biological physics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 19 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
- On the fluorescence enhancement of arch neuronal optogenetic reporters.Nature communications · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- Exploring the Retinal Binding Cavity of Archaerhodopsin-3 by Replacing the Retinal Chromophore With a Dimethyl Phenylated Derivative.Frontiers in molecular biosciences · 2021Article
- Contemporary strategies for dissecting the neuronal basis of neurodevelopmental disorders.Neurobiology of learning and memory · 2019Review
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Redshifted and Near-infrared Active Analog Pigments Based upon Archaerhodopsin-3.Photochemistry and photobiology · 2019Article
- Orientation of non-spherical protonated water clusters revealed by infrared absorption dichroism.Nature communications · 2018Article
- Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K.Biochemistry · 2017Article
- Comparison of the structural changes occurring during the primary phototransition of two different channelrhodopsins from Chlamydomonas algae.Biochemistry · 2015Article
- Mechanism divergence in microbial rhodopsins.Biochimica et biophysica acta · 2014Review
- Near-IR resonance Raman spectroscopy of archaerhodopsin 3: effects of transmembrane potential.The journal of physical chemistry. B · 2012Article
- A dynamic role for water in biological systems.Journal of biological physics · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Archaerhodopsin-3 (AR3) is a light-driven proton pump from Halorubrum sodomense, but little is known about its photocycle. Recent interest has focused on AR3 because of its ability to serve both as a high-performance, genetically-targetable optical silencer of neuronal activity and as a membrane voltage sensor. We examined light-activated structural changes of the protein, retinal chromophore, and internal water molecules during the photocycle of AR3. Low-temperature and rapid-scan time-resolved FTIR-difference spectroscopy revealed that conformational changes during formation of the K, M, and N photocycle intermediates are similar, although not identical, to bacteriorhodopsin (BR). Positive/negative bands in the region above 3,600 cm( - 1), which have previously been assigned to structural changes of weakly hydrogen bonded internal water molecules, were substantially different between AR3 and BR. This included the absence of positive bands recently associated with a chain of proton transporting water molecules in the cytoplasmic channel and a weakly hydrogen bonded water (W401), which is part of a hydrogen-bonded pentagonal cluster located near the retinal Schiff base. However, many of the broad IR continuum absorption changes below 3,000 cm( - 1) assigned to networks of water molecules involved in proton transport through cytoplasmic and extracellular portions in BR were very similar in AR3. This work and subsequent studies comparing BR and AR3 structural changes will help identify conserved elements in BR-like proton pumps as well as bioengineer AR3 to optimize neural silencing and voltage sensing.
Indexed as
Identifiers
What OpenQuestion holds
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.