Evidence map›Paper›PMID 24818247›Full record

ReviewMass spectrometry reviews

Protein modifications by electrophilic lipoxidation products: adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification.

Yury V Vasil'ev, Shin-Chen Tzeng, Lin Huang, Claudia S Maier

Abstract readReview
In one paragraph

Review in Mass spectrometry reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Methylglyoxal Formation-Metabolic Routes and Consequences.Antioxidants (Basel, Switzerland) · 2025
    Review
  4. Review
  5. Review
  6. Mass spectrometry-based retina proteomics.Mass spectrometry reviews · 2023
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Antioxidant Effects of Sheep Whey Protein on Endothelial Cells.Oxidative medicine and cellular longevity · 2016
    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 at 1 institution in 1 country.

Yury V Vasil'ev
Shin-Chen Tzeng
Lin Huang
Claudia S Maier
Oregon State University · US

Funding

Reducing Susceptibility to Environmental Stress Throughout the Life SpanP30ES000210 · NIEHS · OREGON STATE UNIVERSITY · PI BECKMAN, JOSEPH S · 1985 to 2015
$21.4M
Mitochondrial Proteomics of the Aging HeartR01AG025372 · NIA · OREGON STATE UNIVERSITY · PI MAIER, CLAUDIA S · 2004 to 2008
$1.4M
A Universal Electromagnetostatic Tandem-Mass-Spectrometric Dissociation-Cell forR01RR026275 · NCRR · OREGON STATE UNIVERSITY · PI BAROFSKY, DOUGLAS F · 2010 to 2011
$708k
Ion Mobility Time-of-flight Mass Spectrometry SystemS10RR025628 · NCRR · OREGON STATE UNIVERSITY · PI MAIER, CLAUDIA S, STEVENS, JAN FREDERIK · 2009 to 2009
$440k
NCRR NIH HHS R01 RR026275NCRR NIH HHS R01RR026275NCRR NIH HHS S10 RR025628NCRR NIH HHS S10RR025628NIA NIH HHS R01 AG025372NIA NIH HHS R01AG025372NIEHS NIH HHS P30 ES000210NIEHS NIH HHS P30ES000210.
6 · The paper itself

Abstract

The post-translational modification of proteins by electrophilic oxylipids is emerging as an important mechanism that contributes to the complexity of proteomes. Enzymatic and non-enzymatic oxidation of biological lipids results in the formation of chemically diverse electrophilic carbonyl compounds, such as 2-alkenals and 4-hydroxy alkenals, epoxides, and eicosanoids with reactive cyclopentenone structures. These lipoxidation products are capable of modifying proteins. Originally considered solely as markers of oxidative insult, more recently the modifications of proteins by lipid peroxidation products are being recognized as a new mechanism of cell signaling with relevance to redox homeostasis, adaptive response and inflammatory resolution. The growing interest in protein modifications by reactive oxylipid species necessitates the availability of methods that are capable of detecting, identifying and characterizing these protein adducts in biological samples with high complexity. However, the efficient analysis of these chemically diverse protein adducts presents a considerable analytical challenge. We first provide an introduction into the chemistry and biological relevance of protein adductions by electrophilic lipoxidation products. We then provide an overview of tandem mass spectrometry approaches that have been developed in recent years for the interrogation of protein modifications by electrophilic oxylipid species.

Indexed as

Lipid PeroxidationOxidation-ReductionProtein Processing, Post-TranslationalProteinsTandem Mass SpectrometryProteins

Identifiers

PMID24818247
PMCPMC4138024
OpenAlexW1554963318

What OpenQuestion holds

Textmetadata
LicenceTDM
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.