ArticleMolecular & cellular proteomics : MCP2013
Comprehensive identification of proteins from MALDI imaging.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Multimodal spatial omics: From data acquisition to computational integration.Patterns (New York, N.Y.) · 2026Review
- The evolving landscape of spatial proteomics technologies in the AI age.Fundamental research · 2026Review
- Enhancing mass spectrometry imaging accessibility using convolutional autoencoders for deriving hypoxia-associated peptides from tumors.NPJ systems biology and applications · 2024Article
- Spatial analysis of the osteoarthritis microenvironment: techniques, insights, and applications.Bone research · 2024Review
- Proteomic analysis of granulomas from cattle and pigs naturally infected withFrontiers in immunology · 2024Article
- Spatial and Temporal Protein Modules Signatures Associated with Alzheimer Disease in 3xTg-AD Mice Are Restored by Early Ubiquinol Supplementation.Antioxidants (Basel, Switzerland) · 2023Article
- ImShot: An Open-Source Software for Probabilistic Identification of Proteins In Situ and Visualization of Proteomics Data.Molecular & cellular proteomics : MCP · 2022Article
- Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins.Molecular biology and evolution · 2022Article
- Spatial omics: Navigating to the golden era of cancer research.Clinical and translational medicine · 2022Review
- Article
- Automated annotation and visualisation of high-resolution spatial proteomic mass spectrometry imaging data using HIT-MAP.Nature communications · 2021Article
- Implementation of MALDI Mass Spectrometry Imaging in Cancer Proteomics Research: Applications and Challenges.Journal of personalized medicine · 2020Review
- Derangements of amino acids in cachectic skeletal muscle are caused by mitochondrial dysfunction.Journal of cachexia, sarcopenia and muscle · 2020Article
- MicroLESA: Integrating Autofluorescence Microscopy, In Situ Micro-Digestions, and Liquid Extraction Surface Analysis for High Spatial Resolution Targeted Proteomic Studies.Analytical chemistry · 2019Article
- Spatially resolved metabolomics to discover tumor-associated metabolic alterations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Integrative Clustering in Mass Spectrometry Imaging for Enhanced Patient Stratification.Proteomics. Clinical applications · 2019Article
- Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Protein identification in imaging mass spectrometry through spatially targeted liquid micro-extractions.Rapid communications in mass spectrometry : RCM · 2018Article
- Anatomical-Molecular Distribution of EphrinA1 in Infarcted Mouse Heart Using MALDI Mass Spectrometry Imaging.Journal of the American Society for Mass Spectrometry · 2018Article
- Spatially-Resolved Top-down Proteomics Bridged to MALDI MS Imaging Reveals the Molecular Physiome of Brain Regions.Molecular & cellular proteomics : MCP · 2018Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) is a powerful tool for the visualization of proteins in tissues and has demonstrated considerable diagnostic and prognostic value. One main challenge is that the molecular identity of such potential biomarkers mostly remains unknown. We introduce a generic method that removes this issue by systematically identifying the proteins embedded in the MALDI matrix using a combination of bottom-up and top-down proteomics. The analyses of ten human tissues lead to the identification of 1400 abundant and soluble proteins constituting the set of proteins detectable by MALDI IMS including >90% of all IMS biomarkers reported in the literature. Top-down analysis of the matrix proteome identified 124 mostly N- and C-terminally fragmented proteins indicating considerable protein processing activity in tissues. All protein identification data from this study as well as the IMS literature has been deposited into MaTisse, a new publically available database, which we anticipate will become a valuable resource for the IMS community.
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