ArticleBiophysical journal2013
Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 59 citations in OpenAlex.
- Phage-assisted evolution of allosteric protein switches.Nature communications · 2026Article
- Hydraulic Activation of the AsLOV2 Photoreceptor.bioRxiv : the preprint server for biology · 2025Article
- β-sheets mediate the conformational change and allosteric signal transmission between the AsLOV2 termini.Journal of computational chemistry · 2024Article
- Light-inducible protein degradation ineLife · 2024Article
- Machine Learning-Assisted Engineering of Light, Oxygen, Voltage Photoreceptor Adduct Lifetime.JACS Au · 2023Article
- Machine learning and protein allostery.Trends in biochemical sciences · 2023Review
- Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- LILAC: enhanced actin imaging with an optogenetic Lifeact.Nature methods · 2023Article
- Ensemble origins and distance-dependence of long-range mutational effects in proteins.iScience · 2022Article
- The roles of highly conserved, non-catalytic residues in class A β-lactamases.Protein science : a publication of the Protein Society · 2022Article
- Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.Nature communications · 2022Article
- Dynamics of hydrogen bonds in the secondary structures of allosteric proteinComputational and structural biotechnology journal · 2022Article
- Resonance energy transfer sensitises and monitors in situ switching of LOV2-based optogenetic actuators.Nature communications · 2020Article
- Optogenetic activation of heterotrimeric G-proteins by LOV2GIVe, a rationally engineered modular protein.eLife · 2020Article
- Engineering Photosensory Modules of Non-Opsin-Based Optogenetic Actuators.International journal of molecular sciences · 2020Review
- Modulation of allosteric coupling by mutations: from protein dynamics and packing to altered native ensembles and function.Current opinion in structural biology · 2019Review
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Directly light-regulated binding of RGS-LOV photoreceptors to anionic membrane phospholipids.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A light- and calcium-gated transcription factor for imaging and manipulating activated neurons.Nature biotechnology · 2017Article
- Whole-protein alanine-scanning mutagenesis of allostery: A large percentage of a protein can contribute to mechanism.Human mutation · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To investigate the relationship between a protein's sequence and its biophysical properties, we studied the effects of more than 100 mutations in Avena sativa light-oxygen-voltage domain 2, a model protein of the Per-Arnt-Sim family. The A. sativa light-oxygen-voltage domain 2 undergoes a photocycle with a conformational change involving the unfolding of the terminal helices. Whereas selection studies typically search for winners in a large population and fail to characterize many sites, we characterized the biophysical consequences of mutations throughout the protein using NMR, circular dichroism, and ultraviolet/visible spectroscopy. Despite our intention to introduce highly disruptive substitutions, most had modest or no effect on function, and many could even be considered to be more photoactive. Substitutions at evolutionarily conserved sites can have minimal effect, whereas those at nonconserved positions can have large effects, contrary to the view that the effects of mutations, especially at conserved positions, are predictable. Using predictive models, we found that the effects of mutations on biophysical function and allostery reflect a complex mixture of multiple characteristics including location, character, electrostatics, and chemistry.
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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.