ArticleProteomics2025
Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.
Article in Proteomics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
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Who cites it
1 citing paper in PubMed.
- Top-Down Thermal Proteome Profiling (TD-TPP) for Functional Characterization of the Intact Proteoforms in Complex Samples.Journal of mass spectrometry : JMS · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Mass spectrometry (MS)-based proteomics methods, including protein footprinting methods such as hydrogen-deuterium exchange mass spectrometry (HDX-MS) and hydroxyl radical footprinting (HRF), can give unique insight into protein structure and interactions. These methods primarily utilize bottom-up proteomics techniques that require the digestion of intact proteins into small peptides before MS analysis. This digestion can obscure structural information relevant to the function of the intact proteoforms. Here, we have developed a novel top-down footprinting method, Methionine Oxidation Footprinting in Intact Proteins (MOFIP), to probe solvent accessibility in intact proteoforms. For MOFIP, natively folded protein lysates are incubated with and without hydrogen peroxide (H
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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.