Evidence map›Paper›PMID 40887159›Full record

ArticleMethods in enzymology2025

Purification and activity assays of N-terminal acetyltransferase D.

Yi-Hsun Ho, Emma K Seipp, Rong Huang

Abstract read
In one paragraph

Article in Methods in enzymology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Yi-Hsun HoBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN, United States.
Emma K SeippBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN, United States.
Rong HuangBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN, United States. Electronic address: huang-r@purdue.edu.

Funding

Discovery of small molecule inhibitors for protein N-terminal acetyltransferase DR01CA258887 · NCI · PURDUE UNIVERSITY · PI HUANG, RONG · 2022 to 2025
$2.1M
NCI NIH HHS R01 CA258887
6 · The paper itself

Abstract

α-N-terminal acetyltransferase D (NatD) specifically acetylates the α-amine of the N-terminal SGRGK motif on histones H4 and H2A, a modification crucial for regulating gene expression. Thus, assays for the characterization of NatD-mediated acetylation is essential to study its functions and discover inhibitors. Here we present two methods for characterizing NatD-mediated acetylation: fluorescence-based and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) assays. We describe detailed procedures to characterize enzymatic kinetics and assess inhibitor activity for NatD. Additionally, we discuss the advantages and limitations of each approach compared to other in vitro acetyltransferase assays and highlight their broader applicability for evaluating N-terminal acetylation.

Indexed as

Enzyme AssaysN-Terminal AcetyltransferasesAcetylationHistonesHumansKineticsRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationHistonesN-Terminal AcetyltransferasesRecombinant Proteinsacetylationacetyltransferasefluorescence assayMALDI-MSNα-acetylation

Identifiers

PMID40887159
PMCPMC12498240

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Registered trials

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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.