ArticleJournal of the American Society for Mass Spectrometry2011
Discrimination between peptide O-sulfo- and O-phosphotyrosine residues by negative ion mode electrospray tandem mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Electron Capture vs Transfer Dissociation for Site Determination of Tryptic Peptide Tyrosine Sulfation: Direct Detection of Fibrinogen Sulfation Sites and Identification of Novel Isobaric Interferences.Journal of proteome research · 2024Article
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.Journal of proteome research · 2023Article
- Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond.Chemical communications (Cambridge, England) · 2023Review
- Analysis of Peptide Hormone Maturation and Processing Specificity Using Isotope-Labeled Peptides.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The Key Role of Metal Adducts in the Differentiation of Phosphopeptide from Sulfopeptide Sequences by High-Resolution Mass Spectrometry.Analytical chemistry · 2022Article
- Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product.Communications biology · 2021Article
- Negative Ion Mode Collision-Induced Dissociation for Analysis of Protein Arginine Methylation.Journal of the American Society for Mass Spectrometry · 2019Article
- Distinguishing Sulfotyrosine Containing Peptides from their Phosphotyrosine Counterparts Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Ultraviolet, Infrared, and High-Low Energy Photodissociation of Post-Translationally Modified Peptides.Journal of the American Society for Mass Spectrometry · 2018Article
- Direct identification of tyrosine sulfation by using ultraviolet photodissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Gas phase chemistry of Li+ with amides: the observation of LiOH loss in mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unambiguous differentiation between isobaric sulfated and phosphorylated tyrosine residues (sTyr and pTyr) of proteins by mass spectrometry is challenging, even using high resolution mass spectrometers. Here we show that upon negative ion mode collision-induced dissociation (CID), pTyr- and sTyr-containing peptides exhibit entirely different modification-specific fragmentation patterns leading to a rapid discrimination between the isobaric covalent modifications using the tandem mass spectral data. This study reveals that the ratio between the relative abundances of [M-H-80](-) and [M-H-98](-) fragment ions in ion-trap CID and higher energy collision dissociation (HCD) spectra of singly deprotonated +80 Da Tyr-peptides can be used as a reliable indication of the Tyr modification group nature. For multiply deprotonated +80 Da Tyr-peptides, CID spectra of sTyr- and pTyr-containing sequences can be readily distinguished based on the presence/absence of the [M-nH-79]((n-1)-) and [M-nH-79-NL]((n-1)-) (n=2, 3) fragment ions (NL=neutral loss).
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