Evidence map›Paper›PMID 34726898›Full record

ReviewChemical reviews2022

Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.

Dalton T Snyder, Sophie R Harvey, Vicki H Wysocki

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.7field-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

54 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  9. Other Techniques.Advances in biochemical engineering/biotechnology · 2026
    Review
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  14. Review
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  16. Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.Journal of the American Society for Mass Spectrometry · 2025
    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

3 authors at 1 institution in 1 country.

The Ohio State University · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
15 Tesla Bruker solariX FTICR MSS10OD018507 · OD · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2014 to 2014
$2.0M
New Algorithms and Software for Mass Spectrometric Analysis of Intact Proteins and ComplexesR44GM133239 · NIGMS · PROTEIN METRICS, LLC · PI BERN, MARSHALL WAYNE · 2021 to 2022
$1.6M
Development of Surface-Induced Dissociation Ion Mobility MS, a Structrl Biol ToolR01GM113658 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2015 to 2018
$1.1M
Advancing native top-down protein analysis with hybrid SID/ECD technologyR43GM140749 · NIGMS · E-MSION, INC. · PI SHAW, JARED BRYAN · 2021 to 2021
$252k
NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM113658NIGMS NIH HHS R43 GM140749NIGMS NIH HHS R44 GM133239NIH HHS S10 OD018507
6 · The paper itself

Abstract

Native mass spectrometry (nMS) is evolving into a workhorse for structural biology. The plethora of online and offline preparation, separation, and purification methods as well as numerous ionization techniques combined with powerful new hybrid ion mobility and mass spectrometry systems has illustrated the great potential of nMS for structural biology. Fundamental to the progression of nMS has been the development of novel activation methods for dissociating proteins and protein complexes to deduce primary, secondary, tertiary, and quaternary structure through the combined use of multiple MS/MS technologies. This review highlights the key features and advantages of surface collisions (surface-induced dissociation, SID) for probing the connectivity of subunits within protein and nucleoprotein complexes and, in particular, for solving protein structure in conjunction with complementary techniques such as cryo-EM and computational modeling. Several case studies highlight the significant role SID, and more generally nMS, will play in structural elucidation of biological assemblies in the future as the technology becomes more widely adopted. Cases are presented where SID agrees with solved crystal or cryoEM structures or provides connectivity maps that are otherwise inaccessible by "gold standard" structural biology techniques.

Indexed as

Tandem Mass SpectrometryBiologyCryoelectron MicroscopyHumansProteinsProteins

Identifiers

PMID34726898
PMCPMC9282826
OpenAlexW3209410582

What OpenQuestion holds

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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.