ArticleProteomics2015
Engineered bromodomains to explore the acetylproteome.
Article in Proteomics, 2015. 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
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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
8 citing papers in PubMed.
- Proteomics in Antitumor Drug Target Discovery, Toxicity, Resistance, and Precision Oncology.Drug design, development and therapy · 2026Review
- Engineered Reader Proteins for Enhanced Detection of Methylated Lysine on Histones.ACS chemical biology · 2020Article
- Proteins and Proteoforms: New Separation Challenges.Analytical chemistry · 2018Review
- Building a KATalogue of acetyllysine targeting and function.Briefings in functional genomics · 2016Review
- Emerging Proteomic Technologies Provide Enormous and Underutilized Potential for Brain Cancer Research.Molecular & cellular proteomics : MCP · 2016Review
- SPOTing Acetyl-Lysine Dependent Interactions.Microarrays (Basel, Switzerland) · 2015Article
- Towards the computational design of protein post-translational regulation.Bioorganic & medicinal chemistry · 2015Review
- Bromodomains shake the hegemony of pan-acetyl antibodies.Proteomics · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
MS-based analysis of the acetylproteome has highlighted a role for acetylation in a wide array of biological processes including gene regulation, metabolism, and cellular signaling. To date, anti-acetyllysine antibodies have been used as the predominant affinity reagent for enrichment of acetyllysine-containing peptides and proteins; however, these reagents suffer from high nonspecific binding and lot-to-lot variability. Bromodomains represent potential affinity reagents for acetylated proteins and peptides, given their natural role in recognition of acetylated sequence motifs in vivo. To evaluate their efficacy, we generated recombinant proteins representing all known yeast bromodomains. Bromodomain specificity for acetylated peptides was determined using degenerate peptide arrays, leading to the observation that different bromodomains display a wide array of binding specificities. Despite their relatively weak affinity, we demonstrate the ability of selected bromodomains to enrich acetylated peptides from a complex biological mixture prior to mass spectrometric analysis. Finally, we demonstrate a method for improving the utility of bromodomain enrichment for MS through engineering novel affinity reagents using combinatorial tandem bromodomain pairs.
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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.