ArticleCurrent chemical genomics2011
Quantitative proteomic approaches to studying histone modifications.
Article in Current chemical genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
8 citing papers in PubMed.
- Chemical biology tools for studying histone post-translational modifications.Cell chemical biology · 2026Review
- Chromatin Structure and Dynamics: Focus on Neuronal Differentiation and Pathological Implication.Genes · 2022Review
- Quantification of histone modifications by parallel-reaction monitoring: a method validation.Analytical chemistry · 2015Article
- Regulation of histone modifying enzymes by the ubiquitin-proteasome system.Biochimica et biophysica acta · 2014Review
- Histone modifications and a choice of variant: a language that helps the genome express itself.F1000prime reports · 2014Review
- Identification and interrogation of combinatorial histone modifications.Frontiers in genetics · 2013Review
- Mass spectrometry-based proteomics for the analysis of chromatin structure and dynamics.International journal of molecular sciences · 2013Article
- Inhibitor of apoptosis protein-like protein-2 as a novel serological biomarker for breast cancer.International journal of molecular sciences · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Histone post-translational modifications (PTMs) positively and negatively regulate gene expression, and are consequently a vital influence on the genomic profile of all eukaryotic species. The study of histone PTMs using classical methods in molecular biology, such as immunofluorescence and Western blotting, is challenging given the technical issues of the approaches, and chemical diversity and combinatorial patterns of the modifications. In light of these many technical limitations, mass spectrometry (MS) is emerging as the most unbiased and rigorous experimental platform to identify and quantify histone PTMs in a high-throughput manner. This review covers the latest developments in mass spectrometry for the analysis of histone PTMs, with the hope of inspiring the continued integration of proteomic, genomic and epigenetic research.
Indexed as
Identifiers
What OpenQuestion holds
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.