Evidence map›Paper›PMID 17583533›Full record

ArticleJournal of the American Society for Mass Spectrometry2007

Improved sequencing of oxidized cysteine and methionine containing peptides using electron transfer dissociation.

R Srikanth, Jonathan Wilson, Juma D Bridgewater, Jason R Numbers, Jihyeon Lim, Mark R Olbris, Ali Kettani, Richard W Vachet

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Article in Journal of the American Society for Mass Spectrometry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

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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

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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.

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Analytical chemistry · 2020
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  20. Electron-capture-induced dissociation of protoporphyrin IX ions.Journal of the American Society for Mass Spectrometry · 2008
    Article
4 · The record

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5 · Who and what money

Authors and funding

8 authors.

R SrikanthDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Jonathan Wilson
Juma D Bridgewater
Jason R Numbers
Jihyeon Lim
Mark R Olbris
Ali Kettani
Richard W Vachet

Funding

Copper-Induced Amyloidosis Studied by Mass SpectrometryR01GM075092 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI VACHET, RICHARD W · 2005 to 2020
$4.0M
NIGMS NIH HHS R01 GM075092
6 · The paper itself

Abstract

Oxidative modifications to the side chains of sulfur-containing amino acids often limit the number of product ions formed during collision-induced dissociation (CID) and thus make it difficult to obtain sequence information for oxidized peptides. In this work, we demonstrate that electron-transfer dissociation (ETD) can be used to improve the sequence information obtained from peptides with oxidized cysteine and methionine residues. In contrast to CID, ETD is found to be much less sensitive to the side-chain chemistry, enabling extensive sequence information to be obtained in cases where CID fails to provide this information. These results indicate that ETD is a valuable technique for studying oxidatively modified peptides and proteins. In addition, we report a unique and very abundant product ion that is formed in the CID spectra of peptides having N-terminal cysteine sulfinic acid residues. The mechanism for this unique dissociation pathway involves a six-membered cyclic intermediate and leads to the facile loss of NH(3) and SO(2), which corresponds to a mass loss of 81 Da. While the facile nature of this dissociation pathway limits the sequence information present in CID spectra of peptides with N-terminal cysteine sulfinic acid residues, extensive sequence information for these peptides can be obtained with ETD.

Indexed as

Amino Acid SequenceCystineMass SpectrometryMethionineMolecular StructureMolecular WeightOxidation-ReductionPeptidesSulfinic AcidsCystineMethioninePeptidesSulfinic Acids

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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.