Evidence map›Paper›PMID 25944366›Full record

ArticleJournal of the American Society for Mass Spectrometry2015

Transformation of [M + 2H](2+) Peptide Cations to [M - H](+), [M + H + O](+), and M(+•) Cations via Ion/Ion Reactions: Reagent Anions Derived from Persulfate.

Alice L Pilo, Jiexun Bu, Scott A McLuckey

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Gas-phase rearrangement reaction of Schiff-base-modified peptide ions.Rapid communications in mass spectrometry : RCM · 2018
    Article
  5. Article
  6. Gas-Phase Oxidation via Ion/Ion Reactions: Pathways and Applications.Journal of the American Society for Mass Spectrometry · 2017
    Article
  7. Gas-Phase Oxidation of Neutral Basic Residues in Polypeptide Cations by Periodate.Journal of the American Society for Mass Spectrometry · 2016
    Article
  8. Article
  9. Article
  10. 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

3 authors at 1 institution in 1 country.

Alice L PiloDepartment of Chemistry, Purdue University, West Lafayette, IN, 47907-2084, USA.
Jiexun Bu
Scott A McLuckey
Purdue University West Lafayette · US

Funding

Gas-phase Bio-conjugation in the Tandem Mass Spectrometry of Peptides, Proteins,R37GM045372 · NIGMS · PURDUE UNIVERSITY · PI MCLUCKEY, SCOTT A · 2014 to 2023
$3.1M
INSTRUMENTATION FOR ANALYSIS OF HIGH MASS BIOMOLECULESR01GM045372 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI MCLUCKEY, SCOTT A · 1991 to 2012
$2.8M
NIGMS NIH HHS GM 45372NIGMS NIH HHS R01 GM045372NIGMS NIH HHS R37 GM045372
6 · The paper itself

Abstract

The gas-phase oxidation of doubly protonated peptides is demonstrated here using ion/ion reactions with a suite of reagents derived from persulfate. Intact persulfate anion (HS2O8(-)), peroxymonosulfate anion (HSO5(-)), and sulfate radical anion (SO4(-•)) are all either observed directly upon negative nanoelectrospray ionization (nESI) or easily obtained via beam-type collisional activation of persulfate into the mass spectrometer. Ion/ion reactions between each of these reagents and doubly protonated peptides result in the formation of a long-lived complex. Collisional activation of the complex containing a peroxymonosulfate anion results in oxygen transfer from the reagent to the peptide to generate the [M + H + O](+) species. Activation of the complex containing intact persulfate anion either results in oxygen transfer to generate the [M + H + O](+) species or abstraction of two hydrogen atoms and a proton to generate the [M - H](+) species. Activation of the complex containing sulfate radical anion results in abstraction of one hydrogen atom and a proton to form the peptide radical cation, [M](+•). This suite of reagents allows for the facile transformation of the multiply protonated peptides obtained via nESI into a variety of oxidized species capable of providing complementary information about the sequence and structure of the peptide.

Indexed as

AnionsCationsMass SpectrometryOxidation-ReductionPeptidesPeroxidesProtonsSulfatesAnionsCationsPeptidesPeroxidesperoxymonosulfateProtonsSulfates

Identifiers

PMID25944366
PMCPMC4475491
OpenAlexW2473432074

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.