Evidence map›Paper›PMID 28752478›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Coming to Grips with Ambiguity: Ion Mobility-Mass Spectrometry for Protein Quaternary Structure Assignment.

Joseph D Eschweiler, Aaron T Frank, Brandon T Ruotolo

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. 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
–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

19 citing papers in PubMed.

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  18. On the Effect of Sphere-Overlap on Super Coarse-Grained Models of Protein Assemblies.Journal of the American Society for Mass Spectrometry · 2019
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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.

Joseph D EschweilerDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.
Aaron T FrankDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.
Brandon T RuotoloDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA. bruotolo@umich.edu.

Funding

Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
NIGMS NIH HHS GM095832NIGMS NIH HHS R01 GM095832
6 · The paper itself

Abstract

Multiprotein complexes are central to our understanding of cellular biology, as they play critical roles in nearly every biological process. Despite many impressive advances associated with structural characterization techniques, large and highly-dynamic protein complexes are too often refractory to analysis by conventional, high-resolution approaches. To fill this gap, ion mobility-mass spectrometry (IM-MS) methods have emerged as a promising approach for characterizing the structures of challenging assemblies due in large part to the ability of these methods to characterize the composition, connectivity, and topology of large, labile complexes. In this Critical Insight, we present a series of bioinformatics studies aimed at assessing the information content of IM-MS datasets for building models of multiprotein structure. Our computational data highlights the limits of current coarse-graining approaches, and compelled us to develop an improved workflow for multiprotein topology modeling, which we benchmark against a subset of the multiprotein complexes within the PDB. This improved workflow has allowed us to ascertain both the minimal experimental restraint sets required for generation of high-confidence multiprotein topologies, and quantify the ambiguity in models where insufficient IM-MS information is available. We conclude by projecting the future of IM-MS in the context of protein quaternary structure assignment, where we predict that a more complete knowledge of the ultimate information content and ambiguity within such models will undoubtedly lead to applications for a broader array of challenging biomolecular assemblies. Graphical Abstract ᅟ.

Indexed as

Models, MolecularProtein Structure, QuaternaryActin-Related Protein 2-3 ComplexComputational BiologyDatabases, ProteinIon Mobility SpectrometryMass SpectrometryActin-Related Protein 2-3 ComplexBioinformaticsMolecular dynamics simulationsNative mass spectrometryProtein networkStructural proteomics

Identifiers

PMID28752478
PMCPMC5693686

What OpenQuestion holds

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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.