ArticleJournal of the American Society for Mass Spectrometry2010
Electron capture dissociation mass spectrometry of tyrosine nitrated peptides.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Nitroproteomics is instrumental for stratification and targeted treatments of astrocytoma patients: expert recommendations for advanced 3PM approach with improved individual outcomes.The EPMA journal · 2023Review
- Molecular mechanism of ethanol fermentation inhibition via protein tyrosine nitration of pyruvate decarboxylase by reactive nitrogen species in yeast.Scientific reports · 2022Article
- Structural Characterization of Daunomycin-Peptide Conjugates by Various Tandem Mass Spectrometric Techniques.International journal of molecular sciences · 2021Article
- Electron transfer reduction of the diazirine ring in gas-phase peptide ions. On the peculiar loss of [NH4O] from photoleucine.Journal of the American Society for Mass Spectrometry · 2015Article
- 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
- Proteomic approaches to analyze protein tyrosine nitration.Antioxidants & redox signaling · 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
- The radical ion chemistry of S-nitrosylated peptides.Journal of the American Society for Mass Spectrometry · 2012Article
- Electron capture dissociation of hydrogen-deficient peptide radical cations.Journal of the American Society for Mass Spectrometry · 2012Article
- Relative quantitation of protein nitration by liquid chromatography-mass spectrometry using isotope-coded dimethyl labeling and chemoprecipitation.Journal of chromatography. A · 2012Article
- Accelerated high-resolution differential ion mobility separations using hydrogen.Analytical chemistry · 2011Article
- Separation of a set of peptide sequence isomers using differential ion mobility spectrometry.Analytical chemistry · 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
- Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode.Journal of the American Society for Mass Spectrometry · 2011Article
- Characterization of tyrosine nitration and cysteine nitrosylation modifications by metastable atom-activation dissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Probing the mechanisms of electron capture dissociation mass spectrometry with nitrated peptides.Physical chemistry chemical physics : PCCP · 2010Article
- Top-down mass analysis of protein tyrosine nitration: comparison of electron capture dissociation with "slow-heating" tandem mass spectrometry methods.Analytical chemistry · 2010Article
- 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
4 authors at 2 institutions in 2 countries.
Funding
Abstract
In vivo protein nitration is associated with many disease conditions that involve oxidative stress and inflammatory response. The modification involves addition of a nitro group at the position ortho to the phenol group of tyrosine to give 3-nitrotyrosine. To understand the mechanisms and consequences of protein nitration, it is necessary to develop methods for identification of nitrotyrosine-containing proteins and localization of the sites of modification. Here, we have investigated the electron capture dissociation (ECD) and collision-induced dissociation (CID) behavior of 3-nitrotyrosine-containing peptides. The presence of nitration did not affect the CID behavior of the peptides. For the doubly-charged peptides, addition of nitration severely inhibited the production of ECD sequence fragments. However, ECD of the triply-charged nitrated peptides resulted in some singly-charged sequence fragments. ECD of the nitrated peptides is characterized by multiple losses of small neutral species including hydroxyl radicals, water and ammonia. The origin of the neutral losses has been investigated by use of activated ion (AI) ECD. Loss of ammonia appears to be the result of non-covalent interactions between the nitro group and protonated lysine side-chains.
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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.