ReviewFrontiers in molecular biosciences2025
The role of USP36 in ribosome biogenesis and other pathophysiological processes.
Review in Frontiers in molecular biosciences, 2025. 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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1 citing paper in PubMed.
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6 authors.
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Abstract
Ubiquitination and deubiquitination are common forms of protein post-translational modifications that play crucial roles in the regulation of intracellular homeostasis. As a member of deubiquitination enzyme USP family, USP36 maintains the stability of substrate proteins by mediating their deubiquitination, thereby playing a significant role in various pathophysiological processes. Here we focus on discussing how USP36 participates in regulating ribosome biosynthesis and responds to ribotoxic stress response. Furthermore, this review has elucidated the role of USP36 in regulating DNA replication stress, hypoxia adaptation, oxidative stress, and selective autophagy, as well as the related molecular mechanisms. This review is very helpful for understanding the role of USP36 in pathophysiological process and exploring the possibility of USP36 as a target for disease treatment.
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