ArticleJournal of mass spectrometry : JMS2011
A mass spectrometric analysis of 4-hydroxy-2-(E)-nonenal modification of cytochrome c.
Article in Journal of mass spectrometry : JMS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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.
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.
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Who cites it
10 citing papers in PubMed.
- Lipoxidation in cardiovascular diseases.Redox biology · 2019Review
- Preferential binding of 4-hydroxynonenal to lysine residues in specific parasite proteins in plakortin-treated Plasmodium falciparum-parasitized red blood cells.Data in brief · 2015Article
- 4-Hydroxy-nonenal-A Bioactive Lipid Peroxidation Product.Biomolecules · 2015Review
- Assay of protein and peptide adducts of cholesterol ozonolysis products by hydrophobic and click enrichment methods.Chemical research in toxicology · 2014Article
- Covalent modification of cytochrome c by reactive metabolites of furan.Chemical research in toxicology · 2014Article
- Carbonylation of mitochondrial aconitase with 4-hydroxy-2-(E)-nonenal: localization and relative reactivity of addition sites.Biochimica et biophysica acta · 2013Article
- Peptidyl-prolyl cis/trans-isomerase A1 (Pin1) is a target for modification by lipid electrophiles.Chemical research in toxicology · 2013Article
- The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis.Redox biology · 2013Review
- The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.Journal of mass spectrometry : JMS · 2012Article
- Exploring the biology of lipid peroxidation-derived protein carbonylation.Chemical research in toxicology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Cytochrome c is a key mitochondrial respiratory protein that is particularly susceptible to modification during oxidative stress. The nature of this susceptibility is linked to the mitochondrial membrane being rich in esterified linoleic acid, which predisposes this organelle to the formation of lipid peroxidation products such as 4-hydroxy-2-(E)-nonenal (4-HNE). To better understand the nature of cytochrome c modification by 4-HNE, we initiated an in vitro study utilizing a combination of MALDI-TOF mass spectrometry, LC-ESI-MS/MS and isotope labeling to monitor 4-HNE modification of cytochrome c under various conditions. The overwhelming reaction observed is Michael addition by Lys side-chains in addition to the modification of His 33. While the Lys-4-HNE adducts were generally observed to be reversible, the 4-HNE-His 33 was observed to be stable with half of the formed adduct surviving the denaturation and proteolysis protocols used to generate proteolytic peptides for LC-ESI-MS/MS.
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Registered trials
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.