Evidence map›Paper›PMID 26589699›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation.

Nicholas M Riley, Christopher Mullen, Chad R Weisbrod, Seema Sharma, Michael W Senko, Vlad Zabrouskov, Michael S Westphall, John E P Syka, Joshua J Coon

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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
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  5. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
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  13. Optimal Dissociation Methods Differ forJournal of proteome research · 2020
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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

9 authors at 3 institutions in 1 country.

Nicholas M RileyDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Christopher MullenThermo Fisher Scientific, San Jose, CA, 95134, USA.
Chad R WeisbrodThermo Fisher Scientific, San Jose, CA, 95134, USA.
Seema SharmaThermo Fisher Scientific, San Jose, CA, 95134, USA.
Michael W SenkoThermo Fisher Scientific, San Jose, CA, 95134, USA.
Vlad ZabrouskovThermo Fisher Scientific, San Jose, CA, 95134, USA.
Michael S WestphallDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
John E P SykaThermo Fisher Scientific, San Jose, CA, 95134, USA.
Joshua J CoonDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA. jcoon@chem.wisc.edu.
Thermo Fisher Scientific (United States) · USUniversity of Wisconsin–Madison · USEnergy Center of Wisconsin · US

Funding

Sequential Ion/Ion Reactions for Large Peptide and Whole Protein CharacterizationR01GM080148 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2007 to 2015
$3.0M
NIGMS NIH HHS R01 GM080148
6 · The paper itself

Abstract

Electron transfer dissociation (ETD) is a valuable tool for protein sequence analysis, especially for the fragmentation of intact proteins. However, low product ion signal-to-noise often requires some degree of signal averaging to achieve high quality MS/MS spectra of intact proteins. Here we describe a new implementation of ETD on the newest generation of quadrupole-Orbitrap-linear ion trap Tribrid, the Orbitrap Fusion Lumos, for improved product ion signal-to-noise via ETD reactions on larger precursor populations. In this new high precursor capacity ETD implementation, precursor cations are accumulated in the center section of the high pressure cell in the dual pressure linear ion trap prior to charge-sign independent trapping, rather than precursor ion sequestration in only the back section as is done for standard ETD. This new scheme increases the charge capacity of the precursor accumulation event, enabling storage of approximately 3-fold more precursor charges. High capacity ETD boosts the number of matching fragments identified in a single MS/MS event, reducing the need for spectral averaging. These improvements in intra-scan dynamic range via reaction of larger precursor populations, which have been previously demonstrated through custom modified hardware, are now available on a commercial platform, offering considerable benefits for intact protein analysis and top down proteomics. In this work, we characterize the advantages of high precursor capacity ETD through studies with myoglobin and carbonic anhydrase.

Indexed as

AlgorithmsCarbonic AnhydrasesElectronsMyoglobinProteinsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryUbiquitinCarbonic AnhydrasesMyoglobinProteinsUbiquitinElectron transfer dissociationInstrumentationIntact proteinsIon–ion reactions

Identifiers

PMID26589699
PMCPMC4758868
OpenAlexW2175435082

What OpenQuestion holds

Textmetadata
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.