ArticleNature communications2020
Retrieving functional pathways of biomolecules from single-particle snapshots.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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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Who cites it
65 citing papers in PubMed, 108 citations in OpenAlex.
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- Signal extraction in SWAXS data for the compact X-ray light sources: a machine learning approach.Scientific reports · 2026Article
- Comparing cryo-EM methods and molecular dynamics simulation to investigate heterogeneity in ligand-bound TRPV1.Nature communications · 2025Article
- The Inaugural Flatiron Institute Cryo-EM Conformational Heterogeneity Challenge.bioRxiv : the preprint server for biology · 2025Article
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- Computational Exploration of Bacterial Compounds Targeting Arginine-Specific Mono-Adp-Ribosyl-Transferase 1 (Art1): A Pathway to Novel Therapeutic Anticancer Strategies.Current issues in molecular biology · 2025Article
- CryoDRGN-AI: neural ab initio reconstruction of challenging cryo-EM and cryo-ET datasets.Nature methods · 2025Article
- RNA sample optimization for cryo-EM analysis.Nature protocols · 2025Review
- Structure-based mechanism of RyR channel operation by calcium and magnesium ions.PLoS computational biology · 2025Article
- Rhodamine6G and Hœchst33342 narrow BmrA conformational spectrum for a more efficient use of ATP.Nature communications · 2025Article
- Filling data analysis gaps in time-resolved crystallography by machine learning.Structural dynamics (Melville, N.Y.) · 2025Article
- Roodmus: a toolkit for benchmarking heterogeneous electron cryo-microscopy reconstructions.IUCrJ · 2024Article
- DynaMight: estimating molecular motions with improved reconstruction from cryo-EM images.Nature methods · 2024Article
- Structural basis for ryanodine receptor type 2 leak in heart failure and arrhythmogenic disorders.Nature communications · 2024Article
- Learning structural heterogeneity from cryo-electron sub-tomograms with tomoDRGN.Nature methods · 2024Article
- CLEAPA: a framework for exploring the conformational landscape of cryo-EM using energy-aware pathfinding algorithm.Bioinformatics (Oxford, England) · 2024Article
- Article
- Accurate global and local 3D alignment of cryo-EM density maps using local spatial structural features.Nature communications · 2024Article
- Application of Monolayer Graphene to Cryo-Electron Microscopy Grids for High-resolution Structure Determination.Journal of visualized experiments : JoVE · 2023Article
- Understanding IPCell calcium · 2023Review
5 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
10 authors at 5 institutions in 1 country.
Funding
Abstract
A primary reason for the intense interest in structural biology is the fact that knowledge of structure can elucidate macromolecular functions in living organisms. Sustained effort has resulted in an impressive arsenal of tools for determining the static structures. But under physiological conditions, macromolecules undergo continuous conformational changes, a subset of which are functionally important. Techniques for capturing the continuous conformational changes underlying function are essential for further progress. Here, we present chemically-detailed conformational movies of biological function, extracted data-analytically from experimental single-particle cryo-electron microscopy (cryo-EM) snapshots of ryanodine receptor type 1 (RyR1), a calcium-activated calcium channel engaged in the binding of ligands. The functional motions differ substantially from those inferred from static structures in the nature of conformationally active structural domains, the sequence and extent of conformational motions, and the way allosteric signals are transduced within and between domains. Our approach highlights the importance of combining experiment, advanced data analysis, and molecular simulations.
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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.