Evidence map›Paper›PMID 23463545›Full record

ArticleJournal of the American Society for Mass Spectrometry2013

Gas-phase intramolecular protein crosslinking via ion/ion reactions: ubiquitin and a homobifunctional sulfo-NHS ester.

Ian K Webb, Marija Mentinova, William M McGee, Scott A McLuckey

Abstract 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  3. Article
  4. Article
  5. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Design of a TW-SLIM Module for Dual Polarity Confinement, Transport, and Reactions.Journal of the American Society for Mass Spectrometry · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. C-terminal peptide extension via gas-phase ion/ion reactions.International journal of mass spectrometry · 2015
    Article
  18. Gas-Phase Amidation of Carboxylic Acids with Woodward's Reagent K Ions.Journal of the American Society for Mass Spectrometry · 2015
    Article
  19. Article
  20. 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

4 authors.

Ian K WebbDepartment of Chemistry, Purdue University, West Lafayette, IN 47907-2084, USA.
Marija Mentinova
William M McGee
Scott A McLuckey

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

Gas-phase intra-molecular crosslinking of protein ubiquitin cations has been demonstrated via ion/ion reactions with anions of a homobifunctional N-hydroxysulfosuccinimide (sulfo-NHS) ester reagent. The ion/ion reaction between multiply-protonated ubiquitin and crosslinker monoanions produces a stable, charge-reduced complex. Covalent crosslinking is indicated by the consecutive loss of 2 molecules of sulfo-NHS under ion trap collisional activation conditions. Covalent modification is verified by the presence of covalently crosslinked sequence ions produced by ion-trap collision-induced dissociation of the ion generated from the losses of sulfo-NHS. Analysis of the crosslinked sequence fragments allows for the localization of crosslinked primary amines, enabling proximity mapping of the gas-phase 3-D structures. The presence of two unprotonated reactive sites within the distance constraint of the crosslinker is required for successful crosslinking. The ability to covalently crosslink is, therefore, sensitive to protein charge state. As the charge state increases, fewer reactive sites are available and protein structure is more likely to become extended because of intramolecular electrostatic repulsion. At high charge states, the reagent shows little evidence for covalent crosslinking but does show evidence for 'electrostatic crosslinking' in that the binding of the sulfonate groups to the protein is sufficiently strong that backbone cleavages are favored over reagent detachment under ion trap collisional activation conditions.

Indexed as

Amino Acid SequenceAnimalsCattleErythrocytesIonsMass SpectrometryMolecular Sequence DataProteomicsStatic ElectricitySuccinimidesUbiquitinIonsN-hydroxysulfosuccinimideSuccinimidesUbiquitin

Identifiers

PMID23463545
PMCPMC3644013

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.