ArticleProtein science : a publication of the Protein Society2025
PEGASUS: Prediction of MD-derived protein flexibility from sequence.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Inferring dynamic information from protein structures by Gaussian integrals and deep learning.Bioinformatics (Oxford, England) · 2026Article
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- PEGASUS: Prediction of MD-derived protein flexibility from sequence.Protein science : a publication of the Protein Society · 2025Article
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.
Funding
Abstract
Protein flexibility is essential to its biological function. However, experimental methods for its assessment, such as X-ray crystallography and nuclear magnetic resonance spectroscopy, are often limited by experimental variability and high cost, leading to a gap between the number of identified protein sequences and the available experimental information on protein dynamics. On the other hand, molecular dynamics (MD) simulations provide a uniform and detailed description of the expected protein flexibility, and the availability and quality of such data are increasing significantly during the last years. In this study, we use the recently released ATLAS database to develop ProtEin lanGuAge models for prediction of SimUlated dynamicS (PEGASUS), a sequence-based predictor of MD-derived information on protein flexibility (https://dsimb.inserm.fr/PEGASUS). PEGASUS integrates four different representations of protein sequences generated by Protein Language Models to predict residue-wise MD-derived values of backbone fluctuation (root mean square fluctuation), Phi and Psi dihedral angles standard deviation, and average Local Distance Difference Test across the trajectory. The PEGASUS web server was optimized to perform instantaneous predictions for an individual protein sequence and also allows batch submission of up to 100 sequences of 1 k residues each. For more complex queries, we also release PEGASUS as a user-friendly standalone utility (https://github.com/DSIMB/PEGASUS).
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.