Evidence map›Paper›PMID 28646653›Full record

ReviewCurrent opinion in structural biology2017

Cryo-EM: beyond the microscope.

Lesley A Earl, Veronica Falconieri, Jacqueline Ls Milne, Sriram Subramaniam

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 110 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024
    Review
  19. Article
  20. 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

4 authors at 3 institutions in 1 country.

Lesley A EarlLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Veronica FalconieriLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Jacqueline Ls MilneLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Sriram SubramaniamLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: ss1@nih.gov.
Center for Cancer Research · USNational Cancer Institute · USNational Institutes of Health · US

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 BC010278Intramural NIH HHS ZIA BC010824Intramural NIH HHS ZIA BC010826
6 · The paper itself

Abstract

The pace at which cryo-EM is being adopted as a mainstream tool in structural biology has continued unabated over the past year. Initial successes in obtaining near-atomic resolution structures with cryo-EM were enabled to a large extent by advances in microscope and detector technology. Here, we review some of the complementary technical improvements that are helping sustain the cryo-EM revolution. We highlight advances in image processing that permit high resolution structure determination even in the presence of structural and conformational heterogeneity. We also review selected examples where biochemical strategies for membrane protein stabilization facilitate cryo-EM structure determination, and discuss emerging approaches for further improving the preparation of reliable plunge-frozen specimens.

Indexed as

Cryoelectron MicroscopyHumansMembrane ProteinsMembrane Proteins

Identifiers

PMID28646653
PMCPMC5683925
OpenAlexW2686877571

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.