ArticleJournal of molecular cell biology2026
African swine fever virus DEAD-box helicase D1133L promotes OGG1-driven incision of genomic 8-oxoG via HDAC5 deacetylation.
Article in Journal of molecular cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- Host-pathogen interactions in African swine fever: From viral entry to systemic disease progression.Cell insight · 2026Review
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Authors and funding
11 authors.
Funding
Abstract
African swine fever virus (ASFV) infection induces oxidative stress and produces oxidative DNA damage bases, leading to oxidative DNA base damage, including the formation of 8-oxoguanine (8-oxoG). Prompt repair of these lesions is essential to maintain genome stability. The enzyme 8-oxoguanine DNA glycosylase 1 (OGG1) initiates the base excision repair (BER) pathway by recognizing and incising 8-oxoG, while also regulating multiple biological processes through interactions with host and viral proteins. In this study, we identified a specific interaction between the N-terminal region of ASFV DEAD-box helicase D1133L and OGG1, establishing a unique role for ASFV D1133L in DNA BER. Furthermore, we demonstrated for the first time that ASFV D1133L is a substrate for the histone acetyltransferases CBP/p300 in the nucleus. Conversely, deacetylation of D1133L by HDAC5, which predominantly occurs in the cytoplasm through its interaction with OGG1, markedly enhances OGG1 incision activity on 8-oxoG. Taken together, our findings reveal a previously unrecognized function of ASFV D1133L in promoting 8-oxoG repair by binding to OGG1 to safeguard genome integrity.
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