ArticleJournal of the American Society for Mass Spectrometry2015
MALDI FTICR IMS of Intact Proteins: Using Mass Accuracy to Link Protein Images with Proteomics Data.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it, 138 citations in OpenAlex.
- Mass spectrometry-based human spatial omics: fundamentals, innovations, and applications.Journal of biomedical science · 2026Pooled it
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- The evolving landscape of spatial proteomics technologies in the AI age.Fundamental research · 2026Review
- MALDI mass spectrometry imaging of extracellular matrix proteins.The Analyst · 2025Review
- Cell-Instructive Biomaterials with Native-Like Biochemical Complexity.Annual review of biomedical engineering · 2025Review
- Spatial top-down proteomics for the functional characterization of human kidney.Clinical proteomics · 2025Article
- On-Tissue Chemical Derivatization for Mass Spectrometry Imaging of Fatty Acids with Enhanced Detection Sensitivity.Biomolecules · 2025Article
- Evaluation of combined workflows for multimodal mass spectrometry imaging of elements and lipids from the same tissue section.Analytical and bioanalytical chemistry · 2025Article
- Decellularization and Enzymatic Digestion Methods to Enhance ECM Protein Detection via MALDI-MS Imaging.Analytical chemistry · 2025Article
- Recent Applications of Artificial Intelligence and Related Technical Challenges in MALDI MS and MALDI-MSI: A Mini Review.Mass spectrometry (Tokyo, Japan) · 2025Review
- Uncovering lipid dynamics in Staphylococcus aureus osteomyelitis using multimodal imaging mass spectrometry.Cell chemical biology · 2024Article
- Spatial top-down proteomics for the functional characterization of human kidney.bioRxiv : the preprint server for biology · 2024Article
- Enhancing mass spectrometry imaging accessibility using convolutional autoencoders for deriving hypoxia-associated peptides from tumors.NPJ systems biology and applications · 2024Article
- Imaging Mass Spectrometry of Isotopically Resolved Intact Proteins on a Trapped Ion-Mobility Quadrupole Time-of-Flight Mass Spectrometer.Analytical chemistry · 2024Article
- Review
- Article
- Article
- Post-translational modifications on the metal-sequestering protein calprotectin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- MALDI IMS-Derived Molecular Contour Maps: Augmenting Histology Whole-Slide Images.Journal of the American Society for Mass Spectrometry · 2023Article
- On-Tissue Chemical Derivatization for Comprehensive Mapping of Brain Carboxyl and Aldehyde Metabolites by MALDI-MS Imaging.Journal of the American Society for Mass Spectrometry · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MALDI imaging mass spectrometry is a highly sensitive and selective tool used to visualize biomolecules in tissue. However, identification of detected proteins remains a difficult task. Indirect identification strategies have been limited by insufficient mass accuracy to confidently link ion images to proteomics data. Here, we demonstrate the capabilities of MALDI FTICR MS for imaging intact proteins. MALDI FTICR IMS provides an unprecedented combination of mass resolving power (~75,000 at m/z 5000) and accuracy (<5ppm) for proteins up to ~12kDa, enabling identification based on correlation with LC-MS/MS proteomics data. Analysis of rat brain tissue was performed as a proof-of-concept highlighting the capabilities of this approach by imaging and identifying a number of proteins including N-terminally acetylated thymosin β(4) (m/z 4,963.502, 0.6ppm) and ATP synthase subunit ε (m/z 5,636.074, -2.3ppm). MALDI FTICR IMS was also used to differentiate a series of oxidation products of S100A8 (m/z 10,164.03, -2.1ppm), a subunit of the heterodimer calprotectin, in kidney tissue from mice infected with Staphylococcus aureus. S100A8 - M37O/C42O(3) (m/z 10228.00, -2.6ppm) was found to co-localize with bacterial microcolonies at the center of infectious foci. The ability of MALDI FTICR IMS to distinguish S100A8 modifications is critical to understanding calprotectin's roll in nutritional immunity.
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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.