Evidence map›Paper›PMID 20169556›Full record

ArticleRapid communications in mass spectrometry : RCM2010

Conversion of methionine into homocysteic acid in heavily oxidized proteomics samples.

Marshall Bern, Jessica Saladino, Joshua S Sharp

Open access · greenAbstract read
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Constrained de novo sequencing of conotoxins.Journal of proteome research · 2012
    Article
  7. 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 2 institutions in 1 country.

Marshall BernPalo Alto Research Center, 3333 Coyote Hill Rd., Palo Alto, CA 94304, USA. bern@parc.com
Jessica Saladino
Joshua S Sharp
University of Georgia · USPalo Alto Research Center · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Algorithms and Software for Difficult Proteomics ProblemsR21GM085718 · NIGMS · PALO ALTO RESEARCH CENTER · PI BERN, MARSHALL WAYNE · 2008 to 2009
$750k
NCRR NIH HHS RR05357NIGMS NIH HHS GM085718NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R21 GM085718
6 · The paper itself

Abstract

Analysis of protein oxidation is necessary in numerous areas of biochemistry, including hydroxyl radical surface mapping, oxidative stress assays, and pharmaceutical stability testing. Mass spectrometry is one of the tools most often used to identify protein oxidation products, and previous studies have attempted to identify and characterize all of the major oxidation products detected by mass spectrometry for each amino acid residue. In this note, we present evidence that in heavily oxidized protein samples, such as those produced by hydroxyl radical surface mapping, a major oxidation product of methionine is homocysteic acid. The formation of homocysteic acid from methionine was previously unrecognized in other mass spectrometric analyses, and has important implications for the analysis of oxidized samples, as well as potential implications as to the functional consequences of methionine oxidation.

Indexed as

HomocysteineMethionineOxidation-ReductionPeptidesProteomicsReproducibility of ResultsTandem Mass Spectrometryhomocysteic acidHomocysteineMethioninePeptides

Identifiers

PMID20169556
PMCPMC2935272
OpenAlexW2026164833

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.