Evidence map›Paper›PMID 35275191›Full record

ArticleMicroscopy (Oxford, England)2022

Forty years in cryoEM of membrane proteins.

Werner Kühlbrandt

Open access · hybridAbstract read
In one paragraph

Article in Microscopy (Oxford, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Compartment-guided assembly of large-scale molecular models with Bentopy.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
  5. Article
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  10. CHARMM-GUIJournal of chemical theory and computation · 2023
    Review
  11. Review
  12. Review
  13. PreparingFrontiers in plant science · 2023
    Article
  14. Article
  15. eGFP as an All-in-One Tag for Purification of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Review
  17. Review
  18. Review
  19. 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

1 author at 1 institution in 1 country.

Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, Frankfurt am Main 60438, Germany.
Max Planck Institute of Biophysics · DE

Funding

Max Planck Society
6 · The paper itself

Abstract

In a surprisingly short time, electron cryo-microscopy (cryoEM) has developed from a niche technique in structural biology to a mainstream method practiced in a rapidly growing number of laboratories around the world. From its beginnings about 40 years ago, cryoEM has had a major impact on the study of membrane proteins, in particular the energy-converting systems from bacterial, mitochondrial and chloroplast membranes. Early work on two-dimensional crystals attained resolutions ∼3.5 Å, but at present, single-particle cryoEM delivers much more detailed structures without crystals. Electron cryo-tomography of membranes and membrane-associated proteins adds valuable context, usually at lower resolution. The review ends with a brief outlook on future prospects.

Indexed as

Electron Microscope TomographyMembrane ProteinsCryoelectron MicroscopySingle Molecule ImagingMembrane ProteinsATP synthaseelectron cryo-microscopyelectron cryo-tomographymembrane structurephotosynthesisrespiratory chain complexes

Identifiers

PMID35275191
PMCPMC8855526
OpenAlexW4214733723

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.