Evidence map›Paper›PMID 30541924›Full record

ArticleThe Journal of biological chemistry2019

Electron microscopy snapshots of single particles from single cells.

Xiunan Yi, Eric J Verbeke, Yiran Chang, Daniel J Dickinson, David W Taylor

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2019. 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
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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  15. Structural Biology in the Multi-Omics Era.Journal of chemical information and modeling · 2020
    Article
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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

5 authors at 2 institutions in 1 country.

Xiunan YiDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas 78712; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712.
Eric J VerbekeDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas 78712; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712.
Yiran ChangDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas 78712; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712.
Daniel J DickinsonDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas 78712; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712. Electronic address: daniel.dickinson@austin.utexas.edu.
David W TaylorDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas 78712; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712; LIVESTRONG Cancer Institute, Dell Medical School, Austin, Texas 78712. Electronic address: dtaylor@utexas.edu.
The University of Texas at Austin · USLivestrong Foundation · US

Funding

Biochemical Basis of Cell Polarization by the PAR Protein SystemR00GM115964 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI DICKINSON, DANIEL J · 2018 to 2020
$747k
NIGMS NIH HHS R00 GM115964
6 · The paper itself

Abstract

Cryo-electron microscopy (cryo-EM) has become an indispensable tool for structural studies of biological macromolecules. Two additional predominant methods are available for studying the architectures of multiprotein complexes: 1) single-particle analysis of purified samples and 2) tomography of whole cells or cell sections. The former can produce high-resolution structures but is limited to highly purified samples, whereas the latter can capture proteins in their native state but has a low signal-to-noise ratio and yields lower-resolution structures. Here, we present a simple, adaptable method combining microfluidic single-cell extraction with single-particle analysis by EM to characterize protein complexes from individual

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsEmbryo, NonmammalianMacromolecular SubstancesMicroscopy, ElectronModels, BiologicalRibosomesSingle-Cell AnalysisCaenorhabditis elegans ProteinsMacromolecular SubstancesCaenorhabditis elegans (C. elegans)cryo-electron microscopyproteasomeribosomesingle-particle analysis

Identifiers

PMID30541924
PMCPMC6364765
OpenAlexW2904335520

What OpenQuestion 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 OpenQuestion graph.