Evidence map›Paper›PMID 32814034›Full record

ArticleStructure (London, England : 1993)2020

Multi-scale 3D Cryo-Correlative Microscopy for Vitrified Cells.

Gong-Her Wu, Patrick G Mitchell, Jesus G Galaz-Montoya, Corey W Hecksel, Emily M Sontag, Vimal Gangadharan, Jeffrey Marshman, David Mankus, Margaret E Bisher, Abigail K R Lytton-Jean and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. Cryogenic electron tomography by the numbers: Charting underexplored lineages in structural cell biology.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
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  6. Article
  7. Review
  8. Article
  9. Article
  10. Recent advances in correlative cryo-light and electron microscopy.Current opinion in structural biology · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 1 country.

Gong-Her WuDepartment of Bioengineering, James H. Clark Center, Stanford University, Stanford, CA 94305, USA.
Patrick G MitchellDivision of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Jesus G Galaz-MontoyaDepartment of Bioengineering, James H. Clark Center, Stanford University, Stanford, CA 94305, USA.
Corey W HeckselDivision of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Emily M SontagDepartment of Biology, James H. Clark Center, Stanford University, Stanford, CA 94305, USA.
Vimal GangadharanZeiss Research Microscopy Solutions, White Plains, NY 10601, USA.
Jeffrey MarshmanZeiss Research Microscopy Solutions, White Plains, NY 10601, USA.
David MankusDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Margaret E BisherDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Abigail K R Lytton-JeanDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Judith FrydmanDepartment of Biology, James H. Clark Center, Stanford University, Stanford, CA 94305, USA.
Kirk CzymmekAdvanced Bioimaging Laboratory, Donald Danforth Plant Science Center, Saint Louis, MO 63132, USA.
Wah ChiuDepartment of Bioengineering, James H. Clark Center, Stanford University, Stanford, CA 94305, USA; Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA. Electronic address: wahc@stanford.edu.
Clark University · USMassachusetts Institute of Technology · USCarl Zeiss (United States) · USSLAC National Accelerator Laboratory · USDonald Danforth Plant Science Center · US

Funding

3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
The proteasome in aging and neurodegenerative diseaseP01AG054407 · NIA · NORTHWESTERN UNIVERSITY · PI FINLEY, DANIEL J · 2018 to 2022
$14.0M
Project 3: TRiC modulation of CNS pathogenesis in HD mouse modelsP01NS092525 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI THOMPSON, LESLIE MICHELS · 2016 to 2020
$6.3M
Molecular Interactions of HIV-1 with the Nuclear Pore ComplexR01AI148382 · NIAID · EMORY UNIVERSITY · PI MELIKIAN, GREGORY B, SARAFIANOS, STEFAN G · 2019 to 2022
$5.5M
PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLR01GM056433 · NIGMS · STANFORD UNIVERSITY · PI Judith Frydman · 1997 to 2026
$5.0M
Acquisition of a 300 kV Electron Microscope for Structural BiologyS10OD021600 · OD · STANFORD UNIVERSITY · PI CHIU, WAH · 2016 to 2016
$2.0M
Defining protein quality control for neurodegenerative disease-related proteinsF32NS086253 · NINDS · STANFORD UNIVERSITY · PI SONTAG, EMILY MITCHELL · 2013 to 2016
$160k
NIAID NIH HHS R01 AI148382NIA NIH HHS P01 AG054407NIGMS NIH HHS P41 GM103832NIGMS NIH HHS R01 GM056433NIH HHS S10 OD021600NINDS NIH HHS F32 NS086253NINDS NIH HHS P01 NS092525
6 · The paper itself

Abstract

Three-dimensional (3D) visualization of vitrified cells can uncover structures of subcellular complexes without chemical fixation or staining. Here, we present a pipeline integrating three imaging modalities to visualize the same specimen at cryogenic temperature at different scales: cryo-fluorescence confocal microscopy, volume cryo-focused ion beam scanning electron microscopy, and transmission cryo-electron tomography. Our proof-of-concept benchmark revealed the 3D distribution of organelles and subcellular structures in whole heat-shocked yeast cells, including the ultrastructure of protein inclusions that recruit fluorescently-labeled chaperone Hsp104. Since our workflow efficiently integrates imaging at three different scales and can be applied to other types of cells, it could be used for large-scale phenotypic studies of frozen-hydrated specimens in a variety of healthy and diseased conditions with and without treatments.

Indexed as

BiomarkersCryoelectron MicroscopyCytoplasmic StructuresGene ExpressionGenes, ReporterGreen Fluorescent ProteinsHeat-Shock ProteinsImaging, Three-DimensionalMicroscopy, Electron, ScanningMicroscopy, FluorescenceRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVitrificationBiomarkersGreen Fluorescent ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsAiryscan microscopyamyloidcryo-correlative light and electron microscopy (cryoCLEM)cryo-electron tomography (cryoET)cryo mill and view (cryoMAV).Hsp104 chaperoneprotein aggregationprotein misfoldingSaccharomyces cerevisiae (yeast)volume cryo-focused ion bean scanning electron microscopy (cryoFIB-SEM)

Identifiers

PMID32814034
PMCPMC7642057
OpenAlexW3057609096

What OpenQuestion holds

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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.