Evidence map›Paper›PMID 21472585›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Characterization and diagnostic value of amino acid side chain neutral losses following electron-transfer dissociation.

Qiangwei Xia, M Violet Lee, Christopher M Rose, Alyce J Marsh, Shane L Hubler, Craig D Wenger, Joshua J Coon

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Near-Edge Soft X-ray Absorption Mass Spectrometry of Protonated Melittin.Journal of the American Society for Mass Spectrometry · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. S- to N-Palmitoyl Transfer During Proteomic Sample Preparation.Journal of the American Society for Mass Spectrometry · 2016
    Article
  13. A calibration routine for efficient ETD in large-scale proteomics.Journal of the American Society for Mass Spectrometry · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. ETD fragmentation features improve algorithm.Expert review of proteomics · 2012
    Article
  18. Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Qiangwei XiaDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
M Violet Lee
Christopher M Rose
Alyce J Marsh
Shane L Hubler
Craig D Wenger
Joshua J Coon
University of Wisconsin–Madison · US

Funding

Wisconsin Center of Excellence in Genomics ScienceP50HG004952 · NHGRI · TEXAS BIOMEDICAL RESEARCH INSTITUTE · PI OLIVIER, MICHAEL · 2009 to 2013
$13.0M
The Epigenotype of Human ES CellsP01GM081629 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI THOMSON, JAMES ALEXANDER · 2008 to 2012
$8.9M
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
NHGRI NIH HHS P50 HG004952NIGMS NIH HHS P01 GM081629NIGMS NIH HHS P01GM081629NIGMS NIH HHS R01 GM080148NIGMS NIH HHS R01GM080148
6 · The paper itself

Abstract

Using a large set of high mass accuracy and resolution ETD tandem mass spectra, we characterized ETD-induced neutral losses. From these data we deduced the chemical formula for 20 of these losses. Many of them have been previously observed in electron-capture dissociation (ECD) spectra, such as losses of the side chains of arginine, aspartic acid, glutamic acid, glutamine, asparagine, leucine, histidine, and carbamidomethylated cysteine residues. With this information, we examined the diagnostic value of these amino acid-specific losses. Among 1285 peptide-spectrum matches, 92.5% have agreement between neutral loss-derived peptide amino acid composition and the peptide sequences. Moreover, we show that peptides can be uniquely identified by using only the accurate precursor mass and amino acid composition based on neutral losses; the median number of sequence candidates from an accurate mass query is reduced from 21 to 8 by adding side chain loss information. Besides increasing confidence in peptide identification, our findings suggest the potential use of these diagnostic losses in ETD spectra to improve false discovery rate estimation and to enhance the performance of scoring functions in database search algorithms.

Indexed as

Amino AcidsCationsCell ExtractsDatabases, ProteinElectronsEmbryonic Stem CellsHumansMetalloendopeptidasesPeptide FragmentsTandem Mass SpectrometryAmino AcidsCationsCell ExtractsMetalloendopeptidasesPeptide Fragmentspeptidyl-Lys metalloendopeptidase

Identifiers

PMID21472585
PMCPMC3074364
OpenAlexW2027281030

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.