Bottom-up and middle-down proteomics have comparable accuracies in defining histone PTM relative abundance and stoichiometry
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Summary
It is evidenced that the middle-down strategy is at least equally reliable to bottom-up in quantifying histone PTMs, and provided similar performance in defining accurate PTM stoichiometry.
- Type
- article
- Published
- 2015-03-03
- Cited by
- 62
- References
- 22
- Access
- Open access
- OpenAlex
- https://openalex.org/W17489521
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19796111
Keywords
Chemistry, Histone, Mass spectrometry, Posttranslational modification, Proteomics
References
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- Epigenetic modifications and human disease
- Middle‐down hybrid chromatography/tandem mass spectrometry workflow for characterization of combinatorial post‐translational modifications in histones
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- Chromatin replication and epigenome maintenance
- The complex language of chromatin regulation during transcription
- High Throughput Characterization of Combinatorial Histone Codes*
- Large Scale Analysis of Co-existing Post-translational Modifications in Histone Tails Reveals Global Fine Structure of Cross-talk*
- Regulation of chromatin by histone modifications
- Stable-isotope-labeled Histone Peptide Library for Histone Post-translational Modification and Variant Quantification by Mass Spectrometry *
- Analytical Chemistry
- BIOCHIMICA ET BIOPHYSICA ACTA
Cited by
- Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics
- Computational and statistical methods for high-throughput analysis of post-translational modifications of proteins.
- Dynamic changes of histone H3 marks during Caenorhabditis elegans lifecycle revealed by middle‐down proteomics
- H3K23me2 is a new heterochromatic mark in Caenorhabditis elegans
- Transgenerational Epigenetic Mechanisms of Stress Axis Programming
- Loss of HP1 causes depletion of H3K27me3 from facultative heterochromatin and gain of H3K27me2 at constitutive heterochromatin
- Unabridged Analysis of Human Histone H3 by Differential Top-Down Mass Spectrometry Reveals Hypermethylated Proteoforms from MMSET/NSD2 Overexpression*
- Profiling post-translational modifications of histones in neural differentiation of embryonic stem cells using liquid chromatography-mass spectrometry.
- Site-Specific Quantification of Surface N-Glycoproteins in Statin-Treated Liver Cells.
- Ion Activation Methods for Peptides and Proteins
- Epiproteomics: quantitative analysis of histone marks and codes by mass spectrometry
- Proteomic characterization of histone variants in the mouse testis by mass spectrometry-based top-down analysis.
- Hybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity
- Profiling Changes in Histone Post-translational Modifications by Top-Down Mass Spectrometry.
- Profiling of Histone Post-Translational Modifications in Mouse Brain with High-Resolution Top-Down Mass Spectrometry.
- Protein Fractionation and Enrichment Prior to Proteomics Sample Preparation.
- New-generation Mass Spectrometry Expands the Toolbox of Cell and Developmental Biology
- Toward an Optimized Workflow for Middle-Down Proteomics
- Middle-Down Proteomics: A Still Unexploited Resource for Chromatin Biology
- Metabolic labeling in middle-down proteomics allows for investigation of the dynamics of the histone code
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