ReviewCritical reviews in biochemistry and molecular biology2011
Revealing histone variant induced changes via quantitative proteomics.
Review in Critical reviews in biochemistry and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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.
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Who cites it
13 citing papers in PubMed.
- Histone variants: key regulators of inflammation in cell dedifferentiation and transdifferentiation.Frontiers in immunology · 2025Review
- Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023Review
- Investigating pathological epigenetic aberrations by epi-proteomics.Clinical epigenetics · 2022Review
- Mass spectrometry-based characterization of histones in clinical samples: applications, progress, and challenges.The FEBS journal · 2022Review
- Current Analytical Strategies in Studying Chromatin-Associated-Proteome (Chromatome).Molecules (Basel, Switzerland) · 2021Review
- Integrating Proteomics and Targeted Metabolomics to Understand Global Changes in Histone Modifications.Proteomics · 2018Review
- Bioorthogonal Chemistry for the Isolation and Study of Newly Synthesized Histones and Their Modifications.ACS chemical biology · 2016Article
- Analyses of Histone Proteoforms Using Front-end Electron Transfer Dissociation-enabled Orbitrap Instruments.Molecular & cellular proteomics : MCP · 2016Article
- Current Proteomic Methods to Investigate the Dynamics of Histone Turnover in the Central Nervous System.Methods in enzymology · 2016Article
- EpiProfile Quantifies Histone Peptides With Modifications by Extracting Retention Time and Intensity in High-resolution Mass Spectra.Molecular & cellular proteomics : MCP · 2015Article
- Quantitative proteomic analysis of histone modifications.Chemical reviews · 2015Review
- Mass spectrometric analysis of histone proteoforms.Annual review of analytical chemistry (Palo Alto, Calif.) · 2014Review
- Quantification of histone modifications using ¹⁵N metabolic labeling.Methods (San Diego, Calif.) · 2013Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Histone variants are isoforms of linker and core histone proteins that differ in their amino acid sequences. These variants have distinct genomic locations and posttranslational modifications, thus increasing the complexity of the chromatin architecture. Biological studies of histone variants indicate that they play a role in many processes including transcription, DNA damage response, and the cell cycle. The small differences in amino acid sequence and the diverse posttranslational modification states that exist between histone variants make traditional analysis using immunoassay methods challenging. In recent years, a number of mass spectrometric techniques have been developed to identify and quantify histones at the whole protein or peptide levels. In this review, we discuss the biology of histone variants and methods to characterize them using mass spectrometry-based proteomics.
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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.