ArticleJournal of molecular biology2009
Illuminating solution responses of a LOV domain protein with photocoupled small-angle X-ray scattering.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 46 citations in OpenAlex.
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Article
- Engineering Photosensory Modules of Non-Opsin-Based Optogenetic Actuators.International journal of molecular sciences · 2020Review
- Directed kinetic transition network model.The Journal of chemical physics · 2019Article
- Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Light induces oxidative damage and protein stability in the fungal photoreceptor Vivid.PloS one · 2018Article
- Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein.PloS one · 2018Article
- Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations.Scientific reports · 2017Article
- Article
- Seeing the world differently: variability in the photosensory mechanisms of two model fungi.Environmental microbiology · 2016Review
- Article
- Short LOV Proteins in Methylocystis Reveal Insight into LOV Domain Photocycle Mechanisms.PloS one · 2015Article
- LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling.Frontiers in molecular biosciences · 2015Review
- The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers.The Plant cell · 2014Article
- Accurate SAXS profile computation and its assessment by contrast variation experiments.Biophysical journal · 2013Article
- Cycles of light and dark co-ordinate reversible colony differentiation in Listeria monocytogenes.Molecular microbiology · 2013Article
- Breaking the radiation damage limit with Cryo-SAXS.Biophysical journal · 2013Article
- The circadian clock of Neurospora crassa.FEMS microbiology reviews · 2012Review
- Function, structure and mechanism of bacterial photosensory LOV proteins.Nature reviews. Microbiology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The PAS-LOV domain is a signal-transducing component found in a large variety of proteins that is responsible for sensing different stimuli such as light, oxygen, and voltage. The LOV protein VVD regulates blue light responses in the filamentous fungi Neurospora crassa. Using photocoupled, time-resolved small-angle X-ray scattering, we extract the solution protein structure in both dark-adapted and light-activated states. Two distinct dark-adapted conformations are detected in the wild-type protein: a compact structure that corresponds to the crystal structure of the dark-state monomer as well as an extended structure that is well modeled by introducing conformational disorder at the N-terminus of the protein. These conformations are accentuated in carefully selected variants, in which a key residue for propagating structural transitions, Cys71, has been mutated or oxidized. Despite different dark-state conformations, all proteins form a common dimer in response to illumination. Taken together, these data support a reaction scheme that describes the mechanism for light-induced dimerization of VVD. Envelope reconstructions of the transient light-state dimer reveal structures that are best described by a parallel arrangement of subunits that have significantly changed conformation compared to the crystal structure.
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.