H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation

Our findings identify H2A.X as a novel bona fide substrate of NAA40. Moreover, the responsiveness of H2A.X N-terminal acetylation to UV-induced DNA damage indicates that this is a dynamic modification with potential biological functions.

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Publication Details

Journal
Epigenetics & Chromatin
Published
2025-07-16
DOI
https://doi.org/10.1186/s13072-025-00608-3
Citations
2
Primary Topic
Peptidase Inhibition and Analysis
Type
article
Field-Weighted Citation Impact
2.09
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article

H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation

Costas Koufaris, Christina Demetriadou, Ariel Klavaris, Antonis Kirmizis et al.
2 citations
Epigenetics & Chromatin
Peptidase Inhibition and Analysis
2.09
article

H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation

Costas Koufaris, Christina Demetriadou, Ariel Klavaris, Antonis Kirmizis, Tiziana Bonaldi, Nikolas Dietis, Roberta Noberini, Maria Kouma, Alessandro Ghiringhelli
article en
2 citations

Abstract

Our findings identify H2A.X as a novel bona fide substrate of NAA40. Moreover, the responsiveness of H2A.X N-terminal acetylation to UV-induced DNA damage indicates that this is a dynamic modification with potential biological functions.

Epigenetics & ChromatinVol. 18(1)
Cyprus Institute (CY), University of Nicosia (CY), University of Milan (IT), University of Cyprus (CY), Cyprus Institute of Neurology and Genetics (CY), European Institute of Oncology (IT)
Openalex Percentile: Top 11%
Peptidase Inhibition and Analysis
2.09
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