ArticleJournal of mass spectrometry : JMS2010
Identification of carbonylation sites in apomyoglobin after exposure to 4-hydroxy-2-nonenal by solid-phase enrichment and liquid chromatography-electrospray ionization tandem mass spectrometry.
Article in Journal of mass spectrometry : JMS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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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
14 citing papers in PubMed, 31 citations in OpenAlex.
- Solid-phase synthesis of peptides containing aminoadipic semialdehyde moiety and their cyclisations.Scientific reports · 2018Article
- Oxidative stress and its significant roles in neurodegenerative diseases and cancer.International journal of molecular sciences · 2014Review
- Selective chemoprecipitation to enrich nitropeptides from complex proteomes for mass-spectrometric analysis.Nature protocols · 2014Article
- Carbonylation of mitochondrial aconitase with 4-hydroxy-2-(E)-nonenal: localization and relative reactivity of addition sites.Biochimica et biophysica acta · 2013Article
- The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis.Redox biology · 2013Review
- Conversion of 3-nitrotyrosine to 3-aminotyrosine residues facilitates mapping of tyrosine nitration in proteins by electrospray ionization-tandem mass spectrometry using electron capture dissociation.Journal of mass spectrometry : JMS · 2012Article
- Comparing the efficiencies of hydrazide labels in the study of protein carbonylation in human serum albumin.Analytical and bioanalytical chemistry · 2012Article
- Relative quantitation of protein nitration by liquid chromatography-mass spectrometry using isotope-coded dimethyl labeling and chemoprecipitation.Journal of chromatography. A · 2012Article
- The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.Journal of mass spectrometry : JMS · 2012Article
- To tag or not to tag: a comparative evaluation of immunoaffinity-labeling and tandem mass spectrometry for the identification and localization of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation.Journal of proteomics · 2011Article
- Protein targets for carbonylation by 4-hydroxy-2-nonenal in rat liver mitochondria.Journal of proteomics · 2011Article
- Isotope-coded dimethyl tagging for differential quantification of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation.Journal of mass spectrometry : JMS · 2011Article
- Selective chemoprecipitation and subsequent release of tagged species for the analysis of nitropeptides by liquid chromatography-tandem mass spectrometry.Molecular & cellular proteomics : MCP · 2011Article
- Mechanisms of 4-hydroxy-2-nonenal induced pro- and anti-apoptotic signaling.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Identification of protein carbonylation because of covalent attachment of a lipid peroxidation end-product was performed by combining proteolytic digestion followed by solid-phase hydrazide enrichment and liquid chromatography (LC)-electrospray ionization (ESI) tandem mass spectrometry (MS/MS) using both collision-induced dissociation (CID) and electron capture dissociation (ECD). To evaluate this approach, we selected apomyoglobin and 4-hydroxy-2-nonenal (4-HNE) as a model protein and a representative end-product of lipid peroxidation, respectively. Although the characteristic elimination of 4-HNE (156 Da) in CID was found to serve as a signature tag for the modified peptides, generation of nearly complete fragment ion series because of efficient peptide backbone cleavage (in most cases over 75%) and the capability to retain the labile 4-HNE moiety of the tryptic peptides significantly aided the elucidation of primary structural information and assignment of exact carbonylation sites in the protein, when ECD was employed. We have concluded that solid-phase enrichment with both CID- and ECD-MS/MS are advantageous during an in-depth interrogation and unequivocal localization of 4-HNE-induced carbonylation of apomyoglobin that occurs via Michael addition to its histidine residues.
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What OpenQuestion holds
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.