ArticleJournal of the American Society for Mass Spectrometry2011
Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 40 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
- Characterization of Phosphorylated Peptides by Electron-Activated and Ultraviolet Dissociation Mass Spectrometry: A Comparative Study with Collision-Induced Dissociation.Journal of the American Society for Mass Spectrometry · 2024Article
- The Omnitrap Platform: A Versatile Segmented Linear Ion Trap for Multidimensional Multiple-Stage Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Structural Characterization of Sulfated Glycosaminoglycans Using Charge-Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2020Article
- Top or Middle? Up or Down? Toward a Standard Lexicon for Protein Top-Down and Allied Mass Spectrometry Approaches.Journal of the American Society for Mass Spectrometry · 2019Article
- Free Radical Initiated Peptide Sequencing for Direct Site Localization of Sulfation and Phosphorylation with Negative Ion Mode Mass Spectrometry.Analytical chemistry · 2018Article
- Ultraviolet, Infrared, and High-Low Energy Photodissociation of Post-Translationally Modified Peptides.Journal of the American Society for Mass Spectrometry · 2018Article
- Top-Down Charge Transfer Dissociation (CTD) of Gas-Phase Insulin: Evidence of a One-Step, Two-Electron Oxidation Mechanism.Journal of the American Society for Mass Spectrometry · 2018Article
- Sulfur Pentafluoride is a Preferred Reagent Cation for Negative Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2017Article
- Charge Transfer Dissociation (CTD) Mass Spectrometry of Peptide Cations: Study of Charge State Effects and Side-Chain Losses.Journal of the American Society for Mass Spectrometry · 2017Article
- Multistage Mass Spectrometry of Phospholipids using Collision-Induced Dissociation (CID) and Metastable Atom-Activated Dissociation (MAD).International journal of mass spectrometry · 2016Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2016Review
- RADICAL-INDUCED FRAGMENTATION OF PHOSPHOLIPID CATIONS USING METASTABLE ATOM-ACTIVATED DISSOCIATION MASS SPECTROMETRY (MAD-MS).International journal of mass spectrometry · 2015Article
- Ion mobility spectrometry-hydrogen deuterium exchange mass spectrometry of anions: part 1. Peptides to proteins.Journal of the American Society for Mass Spectrometry · 2015Article
- Charge transfer dissociation (CTD) mass spectrometry of peptide cations using kiloelectronvolt helium cations.Journal of the American Society for Mass Spectrometry · 2014Article
- Direct identification of tyrosine sulfation by using ultraviolet photodissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Systematic comparison of ultraviolet photodissociation and electron transfer dissociation for peptide anion characterization.Journal of the American Society for Mass Spectrometry · 2012Article
- Tyrosine sulfation in a Gram-negative bacterium.Nature communications · 2012Article
- Simultaneous identification of tyrosine phosphorylation and sulfation sites utilizing tyrosine-specific bromination.Journal of the American Society for Mass Spectrometry · 2011Article
- 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
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dissociation behavior of phosphorylated and sulfonated peptide anions was explored using metastable atom-activated dissociation mass spectrometry (MAD-MS) and collision-induced dissociation (CID). A beam of high kinetic energy helium (He) metastable atoms was exposed to isolated phosphorylated and sulfonated peptides in the 3- and 2- charge states. Unlike CID, where phosphate losses are dominant, the major dissociation channels observed using MAD were C(α) - C peptide backbone cleavages and neutral losses of CO(2), H(2)O, and [CO(2) + H(2)O] from the charge reduced (oxidized) product ion, consistent with an electron detachment dissociation (EDD) mechanism such as Penning ionization. Regardless of charge state or modification, MAD provides ample backbone cleavages with little modification loss, which allows for unambiguous PTM site determination. The relative abundance of certain fragment ions in MAD is also demonstrated to be somewhat sensitive to the number and location of deprotonation sites, with backbone cleavage somewhat favored adjacent to deprotonated sites like aspartic acid residues. MAD provides a complementary dissociation technique to CID, ECD, ETD, and EDD for peptide sequencing and modification identification. MAD offers the unique ability to analyze highly acidic peptides that contain few to no basic amino acids in either negative or positive ion mode.
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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.