ArticleJournal of the American Society for Mass Spectrometry2024
Localizing Isomerized Residue Sites in Peptides with Tandem Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Spatially Mapping Neuropeptide Isomers via MALDI Trapped Ion Mobility MS Imaging.Analytical chemistry · 2025Article
- Untargeted Discovery and Localization of Isomerized Residues in Neuropeptides.Analytical chemistry · 2025Article
- Recent Advancements in the Characterization of D-Amino Acid and Isoaspartate Post-Translational Modifications.Mass spectrometry reviewsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Isomerized amino acid residues have been identified in many peptides extracted from tissues or excretions of humans and animals. These isomerized residues can play key roles by affecting biological activity or by exerting an influence on the process of aging. Isomerization occurs spontaneously and does not result in a mass shift. Thus, identifying and localizing isomerized residues in biological samples is challenging. Herein, we introduce a fast and efficient method using tandem mass spectrometry (MS) to locate isomerized residues in peptides. Although MS
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Registered trials
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