ArticleRapid communications in mass spectrometry : RCM2018
Protein identification in imaging mass spectrometry through spatially targeted liquid micro-extractions.
Article in Rapid communications in mass spectrometry : RCM, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- MALDI spatial proteomics: a mini review of approaches and techniques.Analytical methods : advancing methods and applications · 2026Review
- High-Throughput Proteoform Imaging for Revealing Spatial-Resolved Changes in Brain Tissues Associated with Alzheimer's Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- SPOT: spatial proteomics through on-site tissue-protein-labeling.Clinical proteomics · 2024Article
- Thermal Denaturation of Fresh Frozen Tissue Enhances Mass Spectrometry Detection of Peptides.Analytical chemistry · 2024Article
- Spatially resolved proteomics via tissue expansion.Nature communications · 2022Article
- Mass Spectrometry-Based Analysis of Lipid Involvement in Alzheimer's Disease Pathology-A Review.Metabolites · 2022Review
- ADVANCES IN HIGH-RESOLUTION MALDI MASS SPECTROMETRY FOR NEUROBIOLOGY.Mass spectrometry reviews · 2022Review
- Applications of spatially resolved omics in the field of endocrine tumors.Frontiers in endocrinology · 2022Review
- Deep-ultraviolet laser ablation sampling for proteomic analysis of tissue.Analytica chimica acta · 2021Article
- Multimodal Imaging Mass Spectrometry: Next Generation Molecular Mapping in Biology and Medicine.Journal of the American Society for Mass Spectrometry · 2020Review
- Article
- LESA Cyclic Ion Mobility Mass Spectrometry of Intact Proteins from Thin Tissue Sections.Analytical chemistry · 2020Article
- Localization of sterols and oxysterols in mouse brain reveals distinct spatial cholesterol metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- In situ mass spectrometry analysis of intact proteins and protein complexes from biological substrates.Biochemical Society transactions · 2020Review
- Probing the Fundamentals of Native Liquid Extraction Surface Analysis Mass Spectrometry of Proteins: Can Proteins Refold during Extraction?Analytical chemistry · 2019Article
- Benchtop-compatible sample processing workflow for proteome profiling of < 100 mammalian cells.Analytical and bioanalytical chemistry · 2019Article
- MicroLESA: Integrating Autofluorescence Microscopy, In Situ Micro-Digestions, and Liquid Extraction Surface Analysis for High Spatial Resolution Targeted Proteomic Studies.Analytical chemistry · 2019Article
- Protein identification strategies in MALDI imaging mass spectrometry: a brief review.Current opinion in chemical biology · 2019Review
- Correlated Materials Characterization via Multimodal Chemical and Functional Imaging.ACS nano · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
rationaleLiquid extraction surface analysis (LESA) can be used to generate spatially directed protein identifications in an imaging mass spectrometry (IMS) workflow. This approach involves the use of robotic micro-extractions coupled to online liquid chromatography (LC). We have characterized the extraction efficiency of this method as well as its ability to identify proteins from a matrix assisted laser/desorption ionization (MALDI) IMS experiment.
methodsProteins and peptides were extracted from transverse sections of a rat brain and sagittal sections of a mouse pup using liquid surface extractions. Extracts were either analyzed by online LC coupled to a high mass resolution Fourier transform ion cyclotron resonance (FTICR) mass spectrometer or collected offline and analyzed by traditional LC/MS methods. Identifications were made using both top-down and bottom-up methodologies. MALDI images were acquired on a 15T FTICR mass spectrometer at 125 μm spatial resolution.
resultsRobotic liquid surface extractions are reproducible across various tissue types, providing significantly improved spatial resolution, with respect to extractions, while still allowing for a robust number of protein identifications. A single 2-μL extract can provide identification of over 14,000 peptides with little sample preparation, increasing throughput for spatially targeted workflows. Surface extractions from tissue were coupled directly to LC to gather spatially relevant proteomics data.
conclusionsRobotic liquid surface extractions can be used to interrogate discrete regions of tissue to provide protein identifications with high throughput, accuracy, and robustness. The direct coupling of tissue surface extractions and LC offers a new and effective approach to provide spatial proteomics data in an imaging experiment.
Identifiers
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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.