Evidence map›Paper›PMID 16689545›Full record

ArticleAnalytical chemistry2006

Mass defect labeling of cysteine for improving peptide assignment in shotgun proteomic analyses.

Hilda Hernandez, Sarah Niehauser, Stacey A Boltz, Vijay Gawandi, Robert S Phillips, I Jonathan Amster

Abstract read
In one paragraph

Article in Analytical chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Mass Defect from Nuclear Physics to Mass Spectral Analysis.Journal of the American Society for Mass Spectrometry · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Simultaneous quantitation of amino acid mixtures using clustering agents.Journal of the American Society for Mass Spectrometry · 2011
    Article
  14. Article
  15. Oxidative protein labeling in mass-spectrometry-based proteomics.Analytical and bioanalytical chemistry · 2010
    Review
  16. Shifting unoccupied spectral space in mass spectrum of peptide fragment ions.Journal of the American Society for Mass Spectrometry · 2009
    Article
  17. 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

6 authors.

Hilda HernandezDepartment of Chemistry, University of Georgia, Athens, GA 30602, USA.
Sarah Niehauser
Stacey A Boltz
Vijay Gawandi
Robert S Phillips
I Jonathan Amster

Funding

Proteomic Analysis Using FTICR/MSR01RR019767 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AMSTER, I JONATHAN · 2003 to 2006
$1.1M
NCRR NIH HHS R01 RR019767NCRR NIH HHS R01 RR 019767-03
6 · The paper itself

Abstract

A method for improving the identification of peptides in a shotgun proteome analysis using accurate mass measurement has been developed. The improvement is based upon the derivatization of cysteine residues with a novel reagent, 2,4-dibromo-(2'-iodo)acetanilide. The derivitization changes the mass defect of cysteine-containing proteolytic peptides in a manner that increases their identification specificity. Peptide masses were measured using matrix-assisted laser desorption/ionization Fourier transform ion cyclotron mass spectrometry. Reactions with protein standards show that the derivatization of cysteine is rapid and quantitative, and the data suggest that the derivatized peptides are more easily ionized or detected than unlabeled cysteine-containing peptides. The reagent was tested on a 15N-metabolically labeled proteome from M. maripaludis. Proteins were identified by their accurate mass values and from their nitrogen stoichiometry. A total of 47% of the labeled peptides are identified versus 27% for the unlabeled peptides. This procedure permits the identification of proteins from the M. maripaludis proteome that are not usually observed by the standard protocol and shows that better protein coverage is obtained with this methodology.

Indexed as

AlkylationCysteineMass SpectrometryMethanococcusMolecular WeightPeptidesProteinsProteomicsSpectroscopy, Fourier Transform InfraredCysteinePeptidesProteins

Identifiers

PMID16689545
PMCPMC1482400

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.