Evidence map›Paper›PMID 23609185›Full record

ArticleJournal of the American Society for Mass Spectrometry2013

Multipurpose dissociation cell for enhanced ETD of intact protein species.

Christopher M Rose, Jason D Russell, Aaron R Ledvina, Graeme C McAlister, Michael S Westphall, Jens Griep-Raming, Jae C Schwartz, Joshua J Coon, John E P Syka

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2013. 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
1.4field-weighted citation impact, top 22% 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, 22 citations in OpenAlex.

  1. Article
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  13. Article
  14. Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2016
    Article
  15. A calibration routine for efficient ETD in large-scale proteomics.Journal of the American Society for Mass Spectrometry · 2015
    Article
  16. Article
  17. Article
  18. Article
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 4 institutions in 2 countries.

Christopher M RoseDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Jason D Russell
Aaron R Ledvina
Graeme C McAlister
Michael S Westphall
Jens Griep-Raming
Jae C Schwartz
Joshua J Coon
John E P Syka
University of Wisconsin–Madison · USEnergy Center of Wisconsin · USThermo Fisher Scientific (United States) · USThermo Fisher Scientific (Germany) · DE

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
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 GM080148NIGMS NIH HHS T32 GM008505NIGMS NIH HHS T32GM008505
6 · The paper itself

Abstract

We describe and characterize an improved implementation of ETD on a modified hybrid linear ion trap-Orbitrap instrument. Instead of performing ETD in the mass-analyzing quadrupole linear ion trap (A-QLT), the instrument collision cell was modified to enable ETD. We partitioned the collision cell into a multi-section rf ion storage and transfer device to enable injection and simultaneous separate storage of precursor and reagent ions. Application of a secondary (axial) confinement voltage to the cell end lens electrodes enables charge-sign independent trapping for ion-ion reactions. The approximately 2-fold higher quadrupole field frequency of this cell relative to that of the A-QLT enables higher reagent ion densities and correspondingly faster ETD reactions, and, with the collision cell's longer axial dimensions, larger populations of precursor ions may be reacted. The higher ion capacity of the collision cell permits the accumulation and reaction of multiple full loads of precursor ions from the A-QLT followed by FT Orbitrap m/z analysis of the ETD product ions. This extends the intra-scan dynamic range by increasing the maximum number of product ions in a single MS/MS event. For analyses of large peptide/small protein precursor cations, this reduces or eliminates the need for spectral averaging to achieve acceptable ETD product ion signal-to-noise levels. Using larger ion populations, we demonstrate improvements in protein sequence coverage and aggregate protein identifications in LC-MS/MS analysis of intact protein species as compared to the standard ETD implementation.

Indexed as

Amino Acid SequenceFungal ProteinsIonsMass SpectrometryMolecular Sequence DataProteinsFungal ProteinsIonsProteins

Identifiers

PMID23609185
PMCPMC3667591
OpenAlexW2051627828

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.