ArticleJournal of proteome research2009
One-pot shotgun quantitative mass spectrometry characterization of histones.
Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
88 citing papers in PubMed, 130 citations in OpenAlex.
- ACSF2 Functions as a regulatory switch for PARP inhibitor sensitivity in platinum-sensitive and homologous recombination-proficient high-grade serous ovarian cancer.Cancer cell international · 2026Article
- Review
- High-Throughput Post-Translational Modification Analyses by Reverse Phase Protein Array.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Automated Sample Preparation for the Unbiased Analysis of Histone Posttranslational Modifications Via Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC-MS/MS.Journal of proteome research · 2024Article
- Expression Proteomics and Histone Analysis Reveal Extensive Chromatin Network Changes and a Role for Histone Tail Trimming during Cellular Differentiation.Biomolecules · 2024Article
- An optimized and robust workflow for quantifying the canonical histone ubiquitination marks H2AK119ub and H2BK120ub by LC-MS/MS.bioRxiv : the preprint server for biology · 2024Article
- A global view of the human post-translational modification landscape.The Biochemical journal · 2023Review
- Cataloging Posttranslational Modifications in Plant Histones.Advances in experimental medicine and biology · 2021Article
- Investigation of Neutral Losses and the Citrulline Effect for Modified H4 N-Terminal Pentapeptides.Journal of the American Society for Mass Spectrometry · 2020Article
- Article
- One-Pot Quantitative Top- and Middle-Down Analysis of GluC-Digested Histone H4.Journal of the American Society for Mass Spectrometry · 2019Article
- Comparison of data-acquisition methods for the identification and quantification of histone post-translational modifications on a Q Exactive HF hybrid quadrupole Orbitrap mass spectrometer.Rapid communications in mass spectrometry : RCM · 2019Article
- Interaction of positive coactivator 4 with histone 3.3 protein is essential for transcriptional activation of the luteinizing hormone receptor gene.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Article
- Extensive Characterization of Heavily Modified Histone Tails by 193 nm Ultraviolet Photodissociation Mass Spectrometry via a Middle-Down Strategy.Analytical chemistry · 2018Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- The histone H4 proteoform dynamics in response to SUV4-20 inhibition reveals single molecule mechanisms of inhibitor resistance.Epigenetics & chromatin · 2018Article
- Systematic quantitative analysis of H2A and H2B variants by targeted proteomics.Epigenetics & chromatin · 2018Article
- Early butyrate induced acetylation of histone H4 is proteoform specific and linked to methylation state.Epigenetics · 2018Article
- Filter-Aided Sample Preparation Procedure for Mass Spectrometric Analysis of Plant Histones.Frontiers in plant science · 2018Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Despite increasing applications of mass spectrometry (MS) to characterize post-translational modifications (PTMs) on histone proteins, most existing protocols are not properly suited to robustly measure them in a high-throughput quantitative manner. In this work, we expand on current protocols and describe improved methods for quantitative Bottom Up characterization of histones and their PTMs with comparable sensitivity but much higher throughput than standard MS approaches. This is accomplished by first bypassing off-line fractionation of histone proteins and working directly with total histones from a typical nuclei acid extraction. Next, using a chemical derivatization procedure that is combined with stable-isotope labeling in a two-step process, we can quantitatively compare samples using nanoLC-MS/MS. We show that our method can successfully detect 17 combined H2A/H2B variants and over 25 combined histone H3 and H4 PTMs in a single MS experiment. We test our method by quantifying differentially expressed histone PTMs from wild-type yeast and a methyltransferase knockout strain. This improved methodology establishes that time and sample consuming off-line HPLC or SDS-PAGE purification of individual histone variants prior to MS interrogation as commonly performed is not strictly required. Our protocol significantly streamlines the analysis of histone PTMs and will allow for studies of differentially expressed PTMs between multiple samples during biologically relevant processes in a rapid and quantitative fashion.
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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.