Evidence map›Paper›PMID 35959706›Full record

ArticleFaraday discussions2022

Bridging length scales from molecules to the whole organism by cryoCLEM and cryoET.

Megan Lovatt, Conny Leistner, René A W Frank

Open access · hybridAbstract read
In one paragraph

Article in Faraday discussions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 13% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

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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 1 institution in 1 country.

Megan LovattAstbury Centre of Structural Molecular Biology, School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK. r.frank@leeds.ac.uk.ORCID 0000-0002-7171-0494
Conny LeistnerAstbury Centre of Structural Molecular Biology, School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK. r.frank@leeds.ac.uk.
René A W FrankAstbury Centre of Structural Molecular Biology, School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK. r.frank@leeds.ac.uk.ORCID 0000-0001-9724-9547
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011151/1Medical Research Council MR/V022644/1Wellcome TrustWellcome Trust 108466/Z/15/ZWellcome Trust 208395/Z/17/Z
6 · The paper itself

Abstract

Resolving atomic structures of isolated proteins has uncovered mechanisms and fundamental processes in biology. However, many functions can only be tested in the context of intact cells and tissues that are many orders of magnitude larger than the macromolecules on which they depend. Therefore, methods that interrogate macromolecular structure

Indexed as

Electron Microscope TomographyElectronsCryoelectron MicroscopyMacromolecular SubstancesMicroscopy, ElectronMacromolecular Substances

Identifiers

PMID35959706
PMCPMC9642002
OpenAlexW4291135548

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.