ArticleMethods in molecular biology (Clifton, N.J.)2023
Mass Spectrometry-Based Analysis of Histone Posttranslational Modifications from Laser Microdissected Samples.
Article in Methods in molecular biology (Clifton, N.J.), 2023. 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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Who cites it
3 citing papers in PubMed.
- Protein lactylation in Alzheimer's disease: bridging metabolism, pathology, and therapeutic opportunity.Frontiers in aging neuroscience · 2026Review
- Lactate-induced lactylation: from basic research to clinical perspectives.Frontiers in pharmacology · 2025Review
- Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases.Signal transduction and targeted therapy · 2024Review
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The analysis of histone posttranslational modifications (PTMs) in clinical samples has gained considerable interest due to the increasing knowledge about the implication of epigenetics in a multitude of physiological and pathological processes. Mass spectrometry (MS) has emerged as the most accurate and versatile tool to detect and quantify histone PTMs and has also been applied to clinical specimens, thanks to protocols developed during the past years. However, the requirement for relatively large amounts of material has so far impaired the application of these approaches to samples available in limited amounts. To address this issue, we have recently streamlined the protein extraction procedure from low-amount clinical samples and optimized the digestion step, obtaining a protocol suitable for the analysis of the most common histone PTMs from laser microdissected tissue areas containing down to 1000 cells, which we will describe in this chapter.
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Registered trials
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