Evidence map›Paper›PMID 27020925›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.

David Z Keifer, Tina Motwani, Carolyn M Teschke, Martin F Jarrold

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

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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

4 authors.

David Z KeiferDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Tina MotwaniDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, 06269, USA.
Carolyn M TeschkeDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, 06269, USA.
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA. mfj@indiana.edu.

Funding

Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022
$7.2M
NIGMS NIH HHS R01 GM076661
6 · The paper itself

Abstract

Charge detection mass spectrometry (CDMS) is a single-molecule technique particularly well-suited to measuring the mass and charge distributions of heterogeneous, MDa-sized ions. In this work, CDMS has been used to analyze the assembly products of two coat protein variants of bacteriophage P22. The assembly products show broad mass distributions extending from 5 to 15 MDa for A285Y and 5 to 25 MDa for A285T coat protein variants. Because the charge of large ions generated by electrospray ionization depends on their size, the charge can be used to distinguish hollow shells from more compact structures. A285T was found to form T = 4 and T = 7 procapsids, and A285Y makes a small number of T = 3 and T = 4 procapsids. Owing to the decreased stability of the A285Y and A285T particles, chemical cross-linking was required to stabilize them for electrospray CDMS.Graphical Abstract.

Indexed as

Mass SpectrometryCapsidCapsid ProteinsVirionVirus AssemblyCapsid ProteinsBacteriophage P22Charge detection mass spectrometryCoat proteinProcapsidVirus capsid

Identifiers

PMID27020925
PMCPMC5095694

What OpenQuestion holds

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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.