ArticleAnalytical chemistry2010
Radical directed dissociation for facile identification of iodotyrosine residues using electrospray ionization mass spectrometry.
Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- First in Human Evaluation and Dosimetry Calculations for PeptideMolecular imaging and biology · 2022Article
- Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules.Chemical reviews · 2020Review
- Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Development of Novel Free Radical Initiated Peptide Sequencing Reagent: Application to Identification and Characterization of Peptides by Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Exploitation of the Ornithine Effect Enhances Characterization of Stapled and Cyclic Peptides.Journal of the American Society for Mass Spectrometry · 2016Article
- Comparison of Ultraviolet Photodissociation and Collision Induced Dissociation of Adrenocorticotropic Hormone Peptides.Journal of the American Society for Mass Spectrometry · 2015Article
- Strategies for generating peptide radical cations via ion/ion reactions.Journal of mass spectrometry : JMS · 2015Article
- Photodissociation mass spectrometry: new tools for characterization of biological molecules.Chemical Society reviews · 2014Review
- New protein footprinting: fast photochemical iodination combined with top-down and bottom-up mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Shedding light on the frontier of photodissociation.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Iodination of tyrosine residues in proteins has many uses in chemistry, biology, and medicine. Site specific identification of the sites of iodination is important for many of these uses. Reported herein is a facile method employing photodissociation and mass spectrometry to localize sites of iodination in whole proteins. Absorption of ultraviolet photons by iodotyrosine results in loss of iodine via homolytic bond dissociation. The resulting protein radical fragments in the vicinity of the iodotyrosine upon collisional activation. Analysis of the fragments within the vicinity of each tyrosine residue in the protein enables quantitative evaluation of the likelihood for iodination at each site. The results are compared with both traditional bottom up and top down mass spectrometric methods. Radical directed dissociation yields results in agreement with traditional approaches but requires significantly less effort and is inherently more sensitive. One limitation occurs when multiple tyrosine residues are in close proximity, in which case the extent of iodination at each residue may be difficult to determine. This limitation is frequently problematic for traditional approaches as well.
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Registered trials
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