ArticleJournal of chromatography. A2012
Relative quantitation of protein nitration by liquid chromatography-mass spectrometry using isotope-coded dimethyl labeling and chemoprecipitation.
Article in Journal of chromatography. A, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Stable isotope dimethyl labelling for quantitative proteomics and beyond.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Review
- ANSID: A Solid-Phase Proteomic Approach for Identification and Relative Quantification of Aromatic Nitration Sites.Frontiers in chemistry · 2015Article
- Review of methods to assign the nuclear magnetic resonance peaks of reductively methylated proteins.Analytical biochemistry · 2014Review
- Evaluation of a method for nitrotyrosine site identification and relative quantitation using a stable isotope-labeled nitrated spike-in standard and high resolution fourier transform MS and MS/MS analysis.International journal of molecular sciences · 2014Article
- Selective chemoprecipitation to enrich nitropeptides from complex proteomes for mass-spectrometric analysis.Nature protocols · 2014Article
- Proteomic approaches to analyze protein tyrosine nitration.Antioxidants & redox signaling · 2013Review
- Relative quantification of biomarkers using mixed-isotope labeling coupled with MS.Bioanalysis · 2012Review
- Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Protein nitration has been recognized as an important biomarker for nitroxidative stress associated with various diseases. While identification of protein targets for nitration is important, its quantitative profiling also is necessary to understand the biological impact of this low-abundance posttranslational modification. We have previously reported an efficient and straightforward enrichment method for nitropeptides to reduce sample complexity and permit unambiguous site-specific identifications by LC-MS analyses. This approach relies on two chemical derivatization steps: specifically reductive methylation of aliphatic amines and, then, conversion of nitrotyrosines to the corresponding aminotyrosines before their selective capture by a solid-phase reagent we introduced previously. Hence, the method inherently offers the opportunity for relative quantitation of nitropeptides by using isotopic variants of formaldehyde for reductive methylation. This simple method was tested via LC-MS analyses of differently N-methylated nitropeptides and nitroubiquitin as a model nitroprotein enriched from human serum albumin digest and from human plasma, respectively.
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Registered trials
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