Evidence map›Paper›PMID 37373206›Full record

ArticleInternational journal of molecular sciences2023

Affi-BAMS™: A Robust Targeted Proteomics Microarray Platform to Measure Histone Post-Translational Modifications.

Ghaith M Hamza, Eric Miele, Don M Wojchowski, Paul Toran, Camilla R Worsfold, Tamil S Anthonymuthu, Vladislav B Bergo, Andrew X Zhang, Jeffrey C Silva

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Ghaith M HamzaDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, USA.ORCID 0000-0001-7235-4826
Eric MieleDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, USA.
Don M WojchowskiMolecular, Cellular and Biomedical Sciences, University of New Hampshire, Durham, NH 03824, USA.
Paul ToranMolecular, Cellular and Biomedical Sciences, University of New Hampshire, Durham, NH 03824, USA.
Camilla R WorsfoldAdeptrix Corporation, Beverly, MA 01915, USA.
Tamil S AnthonymuthuAdeptrix Corporation, Beverly, MA 01915, USA.
Vladislav B BergoAdeptrix Corporation, Beverly, MA 01915, USA.
Andrew X ZhangDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, USA.
Jeffrey C SilvaAdeptrix Corporation, Beverly, MA 01915, USA.

Funding

HistoneScan™: a multiplex immunoassay for histone epigenetic profilingR44CA272029 · NCI · ADEPTRIX CORPORATION · PI BERGO, VLADISLAV · 2022 to 2023
$1.3M
NCI NIH HHS R44 CA272029
6 · The paper itself

Abstract

For targeted protein panels, the ability to specifically assay post-translational modifications (PTMs) in a quantitative, sensitive, and straightforward manner would substantially advance biological and pharmacological studies. The present study highlights the effectiveness of the Affi-BAMS™ epitope-directed affinity bead capture/MALDI MS platform for quantitatively defining complex PTM marks of H3 and H4 histones. Using H3 and H4 histone peptides and isotopically labelled derivatives, this affinity bead and MALDI MS platform achieves a range of >3 orders of magnitude with a technical precision CV of <5%. Using nuclear cellular lysates, Affi-BAMS PTM-peptide capture resolves heterogeneous histone N-terminal PTMs with as little as 100 µg of starting material. In an HDAC inhibitor and MCF7 cell line model, the ability to monitor dynamic histone H3 acetylation and methylation events is further demonstrated (including SILAC quantification). Affi-BAMS (and its capacity for the multiplexing of samples and target PTM-proteins) thus provides a uniquely efficient and effective approach for analyzing dynamic epigenetic histone marks, which is critical for the regulation of chromatin structure and gene expression.

Indexed as

HistonesProteomicsAcetylationHistone CodePeptidesProtein Processing, Post-TranslationalTandem Mass SpectrometryHistonesPeptidesBAMShistonesimmunoaffinity peptide captureMALDI MSproteomicsPTMs

Identifiers

PMID37373206
PMCPMC10298961

What OpenQuestion holds

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Registered trials

None linked

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.