Evidence map›Paper›PMID 16503151›Full record

ArticleJournal of the American Society for Mass Spectrometry2006

Long-lived electron capture dissociation product ions experience radical migration via hydrogen abstraction.

Peter B O'Connor, Cheng Lin, Jason J Cournoyer, Jason L Pittman, Marina Belyayev, Bogdan A Budnik

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 125 citations in OpenAlex.

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  14. Conformational Space and Stability of ETD Charge Reduction Products of Ubiquitin.Journal of the American Society for Mass Spectrometry · 2017
    Article
  15. Article
  16. Article
  17. Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015
    Article
  18. Article
  19. Mechanistic study on electron capture dissociation of the oligosaccharide-Mg²⁺ complex.Journal of the American Society for Mass Spectrometry · 2014
    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

6 authors at 1 institution in 1 country.

Peter B O'ConnorMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA. poconnor@bu.edu.
Cheng LinMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA.
Jason J CournoyerMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA.
Jason L PittmanMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA.
Marina BelyayevMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA.
Bogdan A BudnikMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany St., Rm. 507, 02118, Boston, MA, USA.
Boston University · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
NHLBI PROTEOMICS INITIATIVEN01HV28178 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · 2007 to 2008
$2.8M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NCRR NIH HHS P41RR10888NHLBI NIH HHS N01HV28178
6 · The paper itself

Abstract

To explore the mechanism of electron capture dissociation (ECD) of linear peptides, a set of 16-mer peptides were synthesized with deuterium labeled on the alpha-carbon position of four glycines. The ECD spectra of these peptides showed that such peptides exhibit a preference for the radical to migrate to the alpha-carbon position on glycine via hydrogen (or deuterium) abstraction before the final cleavage and generation of the detected product ions. The data show c-type fragment ions, ions corresponding to the radical cation of the c-type fragments, c*, and they also show c*-1 peaks in the deuterated peptides only. The presence of the c*-1 peaks is best explained by radical-mediated scrambling of the deuterium atoms in the long-lived, metastable, radical intermediate complex formed by initial electron capture, followed by dissociation of the complex. These data suggest the presence of at least two mechanisms, one slow, one fast. The abundance of H* and -CO losses from the precursor ion changed upon deuterium labeling indicating the presence of a kinetic isotope effect, which suggests that the values reported here represent an underestimation of radical migration and H/D scrambling in the observed fragments.

Indexed as

Amino Acid SequenceDeuteriumFree RadicalsGlycineHydrogenMass SpectrometryMolecular StructurePeptidesDeuteriumFree RadicalsGlycineHydrogenPeptides

Identifiers

PMID16503151
OpenAlexW2025325267

What OpenQuestion holds

Textmetadata
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.