ArticleMethods in enzymology2016
Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray.
Article in Methods in enzymology, 2016. 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.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Histone modification crosstalk between host and pathogen.bioRxiv : the preprint server for biology · 2026Article
- Epigenetic regulation of TDP-43: potential implications for amyotrophic lateral sclerosis.Frontiers in molecular medicine · 2025Review
- Determining the Substrate Specificity of Lysine Methyltransferases.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Chemical Biology Approaches to Identify and Profile Interactors of Chromatin Modifications.ACS chemical biology · 2023Review
- Modified Histone Peptides Linked to Magnetic Beads Reduce Binding Specificity.International journal of molecular sciences · 2022Article
- Exploring the Ligand Preferences of the PHD1 Domain of Histone Demethylase KDM5A Reveals Tolerance for Modifications of the Q5 Residue of Histone 3.ACS chemical biology · 2021Article
- Article
- Epigenetics and vascular diseases.Journal of molecular and cellular cardiology · 2019Review
- Improved methods for the detection of histone interactions with peptide microarrays.Scientific reports · 2019Article
- Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance.Nucleic acids research · 2018Article
- Analysis of Histone Antibody Specificity with Peptide Microarrays.Journal of visualized experiments : JoVE · 2017Article
- ArrayNinja: An Open Source Platform for Unified Planning and Analysis of Microarray Experiments.Methods in enzymology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The dynamic addition and removal of covalent posttranslational modifications (PTMs) on histone proteins serves as a major mechanism regulating chromatin-templated biological processes in eukaryotic genomes. Histone PTMs and their combinations function by directly altering the physical structure of chromatin and as rheostats for effector protein interactions. In this chapter, we detail microarray-based methods for analyzing the substrate specificity of lysine methyltransferase and demethylase enzymes on immobilized synthetic histone peptides. Consistent with the "histone code" hypothesis, we reveal a strong influence of adjacent and, surprisingly, distant histone PTMs on the ability of histone-modifying enzymes to methylate or demethylate their substrates. This platform will greatly facilitate future investigations into histone substrate specificity and mechanisms of PTM signaling that regulate the catalytic properties of histone-modifying enzymes.
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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.