Evidence map›Paper›PMID 23110852›Full record

ArticleJournal of structural biology2013

A collaborative framework for 3D alignment and classification of heterogeneous subvolumes in cryo-electron tomography.

Oleg Kuybeda, Gabriel A Frank, Alberto Bartesaghi, Mario Borgnia, Sriram Subramaniam, Guillermo Sapiro

Abstract readComparative StudyValidation Study
In one paragraph

Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. Article
  3. High-resolution structure determination using high-throughput electron cryo-tomography.Acta crystallographica. Section D, Structural biology · 2022
    Review
  4. Article
  5. Gum-Net: Unsupervised Geometric Matching for Fast and Accurate 3D Subtomogram Image Alignment and Averaging.Proceedings. IEEE Computer Society Conference on Computer Vision and Pattern Recognition · 2020
    Article
  6. Article
  7. Phantoms models to characterize influenza hemagglutinin-based vaccines.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2017
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. HIV-1 envelope glycoprotein structure.Current opinion in structural biology · 2013
    Review
  17. Article
  18. Article
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

6 authors.

Oleg KuybedaOffice of High Performance Computing and Communications, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Gabriel A Frank
Alberto Bartesaghi
Mario Borgnia
Sriram Subramaniam
Guillermo Sapiro

Funding

Technology Development for 3D Electron MicroscopyZIABC010826 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$9.1M
Imaging cellular assemblies with three-dimensional electron microscopyZIABC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Molecular structures of membrane protein assembliesZIABC010824 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Intramural NIH HHS ZIA BC010826
6 · The paper itself

Abstract

The limitation of using low electron doses in non-destructive cryo-electron tomography of biological specimens can be partially offset via averaging of aligned and structurally homogeneous subsets present in tomograms. This type of sub-volume averaging is especially challenging when multiple species are present. Here, we tackle the problem of conformational separation and alignment with a "collaborative" approach designed to reduce the effect of the "curse of dimensionality" encountered in standard pair-wise comparisons. Our new approach is based on using the nuclear norm as a collaborative similarity measure for alignment of sub-volumes, and by exploiting the presence of symmetry early in the processing. We provide a strict validation of this method by analyzing mixtures of intact simian immunodeficiency viruses SIV mac239 and SIV CP-MAC. Electron microscopic images of these two virus preparations are indistinguishable except for subtle differences in conformation of the envelope glycoproteins displayed on the surface of each virus particle. By using the nuclear norm-based, collaborative alignment method presented here, we demonstrate that the genetic identity of each virus particle present in the mixture can be assigned based solely on the structural information derived from single envelope glycoproteins displayed on the virus surface.

Indexed as

AlgorithmsProtein ConformationCryoelectron MicroscopyElectron Microscope TomographyImaging, Three-DimensionalSimian Immunodeficiency VirusViral Envelope ProteinsViral Envelope Proteins

Identifiers

PMID23110852
PMCPMC3565063

What OpenQuestion holds

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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.