Evidence map›Paper›PMID 24702029›Full record

ReviewRedox report : communications in free radical research2014

Determination of oxidative protein modifications using mass spectrometry.

Mark J Raftery

Open access · bronzeAbstract readReview
In one paragraph

Review in Redox report : communications in free radical research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Antioxidant Supplementation ReducesCurrent developments in nutrition · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
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

1 author at 1 institution in 1 country.

Mark J Raftery
University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous oxidative modifications to proteins and amino acids have been identified with most susceptible, to varying degrees, of some form of oxidative modification. The consequence of oxidation on protein structure and function reveals that some of these modifications are functionally important. The discovery and accurate characterization/description of existing and new modifications requires modern instrumentation, great care, and attention to detail, especially if the modifications are present in low stoichiometric quantities or they only exist transiently. The focus of this brief review is on the use of mass spectrometry, protein chemistry, and proteomics methods and tools to identify oxidatively modified proteins and peptides along with the characterization of specific sites. Many of the specialized mass spectrometry technologies and techniques are becoming more widely available in research laboratories with mass spectrometry or proteomics facilities allowing even non-expert researchers in the field to accurately determine modifications. Illustrative examples of some approaches are provided from the author's work, collaborative research projects, and elsewhere.

Indexed as

AnimalsHumansMass SpectrometryOxidation-ReductionProteinsProteomicsProteinsOxidationProteomicsTandem mass spectrometry

Identifiers

PMID24702029
PMCPMC6837444
OpenAlexW2083475407

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.