Evidence map›Paper›PMID 22408389›Full record

ArticleInternational journal of mass spectrometry2012

Dissociation Behavior of Tryptic and Intramolecular Disulfide-linked Peptide Ions Modified in the Gas Phase via Ion/Ion Reactions.

John R Stutzman, Kerry M Hassell, Scott A McLuckey

Abstract read
In one paragraph

Article in International journal of mass spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

  1. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  2. Article
  3. Article
  4. Gas-phase rearrangement reaction of Schiff-base-modified peptide ions.Rapid communications in mass spectrometry : RCM · 2018
    Article
  5. Gas-Phase Oxidation of Neutral Basic Residues in Polypeptide Cations by Periodate.Journal of the American Society for Mass Spectrometry · 2016
    Article
  6. Gas-Phase Amidation of Carboxylic Acids with Woodward's Reagent K Ions.Journal of the American Society for Mass Spectrometry · 2015
    Article
  7. Article
  8. Gas phase reactivity of carboxylates with N-hydroxysuccinimide esters.Journal of the American Society for Mass Spectrometry · 2015
    Article
  9. Oxidation of methionine residues in polypeptide ions via gas-phase ion/ion chemistry.Journal of the American Society for Mass Spectrometry · 2014
    Article
  10. Gas Phase Dissociation Behavior of Acyl-Arginine Peptides.International journal of mass spectrometry · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Gas-phase reactivity of carboxylic acid functional groups with carbodiimides.Journal of the American Society for Mass Spectrometry · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Solution versus gas-phase modification of peptide cations with NHS-ester reagents.Journal of the American Society for Mass Spectrometry · 2012
    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.

John R StutzmanDepartment of Chemistry, Purdue University, West Lafayette, IN 47907-2084.
Kerry M Hassell
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 R01 GM045372NIGMS NIH HHS R37 GM045372
6 · The paper itself

Abstract

Protonated tryptic peptides, somatostatin-14, and oxytocin have been subjected to reactions with doubly deprotonated 4-formyl-1,3-benzenedisulfonic acid (FBDSA) in the gas phase. The major product is a negatively-charged complex comprised of the peptide and the reagent. Upon dehydration of the complex, all peptides show evidence for Schiff base formation involving a primary amine of the peptide. Some peptides also show evidence for the formation of a relatively strong electrostatic interaction without Schiff base formation (i.e., a mixture of isomeric precursor ions is generated upon dehydration of the complex). Ion trap collision-induced dissociation of the dehydration products from all peptides examined gave distinct product ion spectra relative to the deprotonated and protonated forms of the peptides. The distinct behavior of the modified ions is attributed to the highly stable charge carrying sulfonate group, which tends to inhibit intramolecular proton transfer in negatively charged species. Modified anions of the peptides with an intramolecular disulfide linkage show evidence for cleavage of both the disulfide linkage and an amide bond in the loop defined by the disulfide bond. Modification of protonated peptides via charge inversion with FBDSA is a useful means for generating novel and distinct ion-types that can provide complementary structural information upon subsequent activation to that obtained from dissociation of protonated or deprotonated forms of the peptide.

Identifiers

PMID22408389
PMCPMC3297198
OpenAlexW2071579201

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.