Evidence map›Paper›PMID 36806476›Full record

ArticleJournal of molecular biology2023

Integrating Molecular Models Into CryoEM Heterogeneity Analysis Using Scalable High-resolution Deep Gaussian Mixture Models.

Muyuan Chen, Bogdan Toader, Roy Lederman

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
7.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. CryoJAX: a cryo-electron microscopy image-simulation library in JAX.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Subspace Method of Moments forSIAM journal on imaging sciences · 2026
    Article
  5. cryoJAX: A Cryo-electron Microscopy Image Simulation Library In JAX.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025
    Article
  8. Efficient high-resolution refinement in cryo-EM with stochastic gradient descent.Acta crystallographica. Section D, Structural biology · 2025
    Article
  9. Article
  10. Article
  11. InstaMap: instant-NGP for cryo-EM density maps.Acta crystallographica. Section D, Structural biology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Muyuan ChenDivision of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
Bogdan ToaderDepartment of Statistics and Data Science, Yale University, New Haven, CT, USA.
Roy LedermanDepartment of Statistics and Data Science, Yale University, New Haven, CT, USA.
Yale University · USStanford University · US

Funding

SUPPORT AND DEVELOPMENT OF EMAN FOR ELECTRON MICROSCOPY IMAGE PROCESSINGR01GM080139 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LUDTKE, STEVEN J · 2006 to 2022
$5.4M
Reconstruction of heterogeneous and small macromolecules by cyro-EMR01GM136780 · NIGMS · PRINCETON UNIVERSITY · PI SINGER, AMIT · 2020 to 2023
$1.3M
Determining structure and organization of neurofilaments in situ using cryo-electron tomographyR21MH125285 · NIMH · STANFORD UNIVERSITY · PI CHEN, MUYUAN · 2021 to 2022
$425k
NIGMS NIH HHS R01 GM080139NIGMS NIH HHS R01 GM136780NIMH NIH HHS R21 MH125285
6 · The paper itself

Abstract

Resolving the structural variability of proteins is often key to understanding the structure-function relationship of those macromolecular machines. Single particle analysis using Cryogenic electron microscopy (CryoEM), combined with machine learning algorithms, provides a way to reveal the dynamics within the protein system from noisy micrographs. Here, we introduce an improved computational method that uses Gaussian mixture models for protein structure representation and deep neural networks for conformation space embedding. By integrating information from molecular models into the heterogeneity analysis, we can analyze continuous protein conformational changes using structural information at the frequency of 1/3 Å

Indexed as

AlgorithmsNeural Networks, ComputerCryoelectron MicroscopyMicroscopy, ElectronModels, MolecularCryoEMdeep neural networksGaussian mixture modelsingle particle analysisstructure heterogeneity

Identifiers

PMID36806476
PMCPMC10164680
OpenAlexW4320883684

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.