ArticleNature communications2015
Discovery of protein acetylation patterns by deconvolution of peptide isomer mass spectra.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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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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
9 citing papers in PubMed, 29 citations in OpenAlex.
- Proteomic Analysis of Histone Sequence Variants and Post-translationally Modified Forms.Advances in experimental medicine and biology · 2026Review
- Evaluation of Protein Ion Relative Ratio Quantification in Top-down Electrospray Ionization-Mass Spectrometry Using Site-Specific Acetylated Recombinant Histone H3 Proteoforms.Journal of the American Society for Mass Spectrometry · 2025Article
- Rapid degradation of histone deacetylase 1 (HDAC1) reveals essential roles in both gene repression and active transcription.Nucleic acids research · 2025Article
- Identification of Cofragmented Combinatorial Peptide Isomers by Two-Dimensional Partial Covariance Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation.Nature communications · 2019Article
- EpiProfile 2.0: A Computational Platform for Processing Epi-Proteomics Mass Spectrometry Data.Journal of proteome research · 2018Article
- Identification of absolute geometries of cis and trans molecular isomers by Coulomb Explosion Imaging.Scientific reports · 2016Article
- Epiproteomics: quantitative analysis of histone marks and codes by mass spectrometry.Current opinion in chemical biology · 2016Review
- Unraveling Posttranslational Modification Complexity: Advances in Quantitative Histone Proteoform Mass Spectrometry.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Protein post-translational modifications (PTMs) play important roles in the control of various biological processes including protein-protein interactions, epigenetics and cell cycle regulation. Mass spectrometry-based proteomics approaches enable comprehensive identification and quantitation of numerous types of PTMs. However, the analysis of PTMs is complicated by the presence of indistinguishable co-eluting isomeric peptides that result in composite spectra with overlapping features that prevent the identification of individual components. In this study, we present Iso-PeptidAce, a novel software tool that enables deconvolution of composite MS/MS spectra of isomeric peptides based on features associated with their characteristic fragment ion patterns. We benchmark Iso-PeptidAce using dilution series prepared from mixtures of known amounts of synthetic acetylated isomers. We also demonstrate its applicability to different biological problems such as the identification of site-specific acetylation patterns in histones bound to chromatin assembly factor-1 and profiling of histone acetylation in cells treated with different classes of HDAC inhibitors.
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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.