M6A Demethylase ALKBH5 in Human Diseases: From Structure to Mechanisms.

Bibliographic Details
Title: M6A Demethylase ALKBH5 in Human Diseases: From Structure to Mechanisms.
Authors: Fang, Miaochun, Ye, Liwen, Zhu, Yue, Huang, Linying, Xu, Shun
Source: Biomolecules (2218-273X); Feb2025, Vol. 15 Issue 2, p157, 23p
Subject Terms: RNA modification & restriction, RNA metabolism, GENE expression, ADENOSINES, GENETIC translation
Abstract: N6-methyladenosine (m6A) is the most abundant, dynamically reversible, and evolutionarily conserved internal chemical modification in eukaryotic RNA. It is emerging as critical for regulating gene expression at the post-transcriptional level by affecting RNA metabolism through, for example, pre-mRNA processing, mRNA decay, and translation. ALKBH5 has recently been identified as an endogenous m6A demethylase implicated in a multitude of biological processes. This review provides an overview of the structural and functional characteristics of ALKBH5 and the involvement of ALKBH5 in diverse human diseases, including metabolic, immune, reproductive, and nervous system disorders, as well as the development of inhibitors. In summation, this review highlights the current understanding of the structure, functions, and detailed mechanisms of ALKBH5 in various physiological and pathological processes and provides valuable insights for clinical applications and foundational research within related fields. [ABSTRACT FROM AUTHOR]
Copyright of Biomolecules (2218-273X) is the property of MDPI and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Complementary Index
Full text is not displayed to guests.
More Details
ISSN:2218273X
DOI:10.3390/biom15020157
Published in:Biomolecules (2218-273X)
Language:English