ArticleAnalytical and bioanalytical chemistry2015
Data-independent-acquisition mass spectrometry for identification of targeted-peptide site-specific modifications.
Article in Analytical and bioanalytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Multi-adductomics: Advancing mass spectrometry techniques for comprehensive exposome characterization.Trends in analytical chemistry : TRAC · 2024Article
- Biomonitoring of Ambient Outdoor Air Pollutant Exposure in Humans Using Targeted Serum Albumin Adductomics.Chemical research in toxicology · 2021Article
- Applications of Chromatography-Ultra High-Resolution MS for Stable Isotope-Resolved Metabolomics (SIRM) Reconstruction of Metabolic Networks.Trends in analytical chemistry : TRAC · 2020Article
- Review
- Mass Spectrometry-Based Methodologies for Targeted and Untargeted Identification of Protein Covalent Adducts (Adductomics): Current Status and Challenges.High-throughput · 2019Review
- A Metabolomics-Inspired Strategy for the Identification of Protein Covalent Modifications.Frontiers in chemistry · 2019Article
- Refinement of a Methodology for Untargeted Detection of Serum Albumin Adducts in Human Populations.Chemical research in toxicology · 2017Article
- Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry.Analytical chemistry · 2017Article
- Inference and quantification of peptidoforms in large sample cohorts by SWATH-MS.Nature biotechnology · 2017Article
- Biomonitoring Human Albumin Adducts: The Past, the Present, and the Future.Chemical research in toxicology · 2017Article
- Methemoglobin Formation and Characterization of Hemoglobin Adducts of Carcinogenic Aromatic Amines and Heterocyclic Aromatic Amines.Chemical research in toxicology · 2016Article
- Low Resolution Data-Independent Acquisition in an LTQ-Orbitrap Allows for Simplified and Fully Untargeted Analysis of Histone Modifications.Analytical chemistry · 2015Article
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2 authors.
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Abstract
We present a novel strategy based on data-independent acquisition coupled to targeted data extraction for the detection and identification of site-specific modifications of targeted peptides in a completely unbiased manner. This method requires prior knowledge of the site of the modification along the peptide backbone from the protein of interest, but not the mass of the modification. The procedure, named multiplex adduct peptide profiling (MAPP), consists of three steps: 1) A fragment-ion tag is extracted from the data, consisting of the b-type and y-type ion series from the N and C-terminus, respectively, up to the amino-acid position that is believed to be modified; 2) MS1 features are matched to the fragment-ion tag in retention-time space, using the isolation window as a pre-filter to enable calculation of the mass of the modification; and 3) modified fragment ions are overlaid with the unmodified fragment ions to verify the mass calculated in step 2. We discuss the development, applications, and limitations of this new method for detection of unknown peptide modifications. We present an application of the method in profiling adducted peptides derived from abundant proteins in biological fluids with the ultimate objective of detecting biomarkers of exposure to reactive species.
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