Evidence map›Paper›PMID 21812433›Full record

ReviewChemical research in toxicology2011

Exploring the biology of lipid peroxidation-derived protein carbonylation.

Kristofer S Fritz, Dennis R Petersen

Open access · greenAbstract readReview
In one paragraph

Review in Chemical research in toxicology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 1 synthesis or guideline pooled it, 124 citations in OpenAlex.

  1. Pooled it
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  6. Review
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  14. Review
  15. FAF1 blocks ferroptosis by inhibiting peroxidation of polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Profiling of Protein Carbonylations in Ferroptosis by Chemical Proteomics.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  18. Article
  19. Review
  20. Article

4 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Kristofer S FritzDepartment of Pharmaceutical Sciences, School of Pharmacy, University of Colorado Denver, Anschutz Medical Campus, Aurora, Colorado 80045, USA.
Dennis R Petersen
University of Colorado Denver · US

Funding

Lipid Aldehyde and Ethanol Induced Liver DamageR37AA009300 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2008 to 2017
$4.4M
Proteomic profiling of NASH: disease mechanisms and novel treatmentR01DK074487 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2007 to 2011
$1.5M
NIAAA NIH HHS 5R37AA009300NIAAA NIH HHS R37 AA009300NIDDK NIH HHS 5R01DK074487NIDDK NIH HHS R01 DK074487
6 · The paper itself

Abstract

The sustained overproduction of reactive oxygen and nitrogen species results in an imbalance of cellular prooxidant-antioxidant systems and is implicated in numerous disease states, including alcoholic liver disease, cancer, neurological disorders, inflammation, and cardiovascular disease. The accumulation of reactive aldehydes resulting from sustained oxidative stress and lipid peroxidation is an underlying factor in the development of these pathologies. Determining the biochemical factors that elicit cellular responses resulting from protein carbonylation remains a key element to developing therapeutic approaches and ameliorating disease pathologies. This review details our current understanding of the generation of reactive aldehydes via lipid peroxidation resulting in protein carbonylation, focusing on pathophysiologic factors associated with 4-hydroxynonenal-protein modification. Additionally, an overview of in vitro and in vivo model systems used to study the physiologic impact of protein carbonylation is presented. Finally, an update of the methods commonly used in characterizing protein modification by reactive aldehydes provides an overview of isolation techniques, mass spectrometry, and computational biology. It is apparent that research in this area employing state-of-the-art proteomics, mass spectrometry, and computational biology is rapidly evolving, yielding foundational knowledge concerning the molecular mechanisms of protein carbonylation and its relation to a spectrum of diseases associated with oxidative stress.

Indexed as

Lipid PeroxidationProtein CarbonylationAldehydesAnimalsComputational BiologyHumansMass SpectrometryProteins4-hydroxy-2-nonenalAldehydesProteins

Identifiers

PMID21812433
PMCPMC3178011
OpenAlexW2080280910

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.