ArticleProceedings of the National Academy of Sciences of the United States of America2012
Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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
78 citing papers in PubMed.
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026Review
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.IUCrJ · 2025Article
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- Deconvolution of dynamic heterogeneity in protein structure.Structural dynamics (Melville, N.Y.) · 2024Review
- Appraising protein conformational changes by resampling time-resolved serial x-ray crystallography data.Structural dynamics (Melville, N.Y.) · 2024Article
- KINNTREX: a neural network to unveil protein mechanisms from time-resolved X-ray crystallography.IUCrJ · 2024Article
- Watching a signaling protein function: What has been learned over four decades of time-resolved studies of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2024Review
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Blue and red in the protein world: Photoactive yellow protein and phytochromes as revealed by time-resolved crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Sample-minimizing co-flow cell for time-resolved pump-probe X-ray solution scattering.Journal of synchrotron radiation · 2023Article
- Biological function investigated by time-resolved structure determination.Structural dynamics (Melville, N.Y.) · 2023Article
- Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Article
- Macromolecular movies, storybooks written by nature.Biophysical reviews · 2021Review
- Using photocaging for fast time-resolved structural biology studies.Acta crystallographica. Section D, Structural biology · 2021Review
- Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021Review
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
To understand how signaling proteins function, it is crucial to know the time-ordered sequence of events that lead to the signaling state. We recently developed on the BioCARS 14-IDB beamline at the Advanced Photon Source the infrastructure required to characterize structural changes in protein crystals with near-atomic spatial resolution and 150-ps time resolution, and have used this capability to track the reversible photocycle of photoactive yellow protein (PYP) following trans-to-cis photoisomerization of its p-coumaric acid (pCA) chromophore over 10 decades of time. The first of four major intermediates characterized in this study is highly contorted, with the pCA carbonyl rotated nearly 90° out of the plane of the phenolate. A hydrogen bond between the pCA carbonyl and the Cys69 backbone constrains the chromophore in this unusual twisted conformation. Density functional theory calculations confirm that this structure is chemically plausible and corresponds to a strained cis intermediate. This unique structure is short-lived (∼600 ps), has not been observed in prior cryocrystallography experiments, and is the progenitor of intermediates characterized in previous nanosecond time-resolved Laue crystallography studies. The structural transitions unveiled during the PYP photocycle include trans/cis isomerization, the breaking and making of hydrogen bonds, formation/relaxation of strain, and gated water penetration into the interior of the protein. This mechanistically detailed, near-atomic resolution description of the complete PYP photocycle provides a framework for understanding signal transduction in proteins, and for assessing and validating theoretical/computational approaches in protein biophysics.
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.