The role of protein post-translational modifications in prostate cancer

Involving addition of chemical groups or protein units to specific residues of the target protein, post-translational modifications (PTMs) alter the charge, hydrophobicity, and conformation of a protein, which in turn influences protein function, protein-protein interaction, and protein aggregation....

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Published inPeerJ (San Francisco, CA) Vol. 12; p. e17768
Main Authors Hao, Yinghui, Gu, Chenqiong, Luo, Wenfeng, Shen, Jian, Xie, Fangmei, Zhao, Ying, Song, Xiaoyu, Han, Zeping, He, Jinhua
Format Journal Article
LanguageEnglish
Published United States PeerJ. Ltd 12.08.2024
PeerJ Inc
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Summary:Involving addition of chemical groups or protein units to specific residues of the target protein, post-translational modifications (PTMs) alter the charge, hydrophobicity, and conformation of a protein, which in turn influences protein function, protein-protein interaction, and protein aggregation. These alterations, which include phosphorylation, glycosylation, ubiquitination, methylation, acetylation, lipidation, and lactylation, are significant biological events in the development of cancer, and play vital roles in numerous biological processes. The processes behind essential functions, the screening of clinical illness signs, and the identification of therapeutic targets all depend heavily on further research into the PTMs. This review outlines the influence of several PTM types on prostate cancer (PCa) diagnosis, therapy, and prognosis in an effort to shed fresh light on the molecular causes and progression of the disease.
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ISSN:2167-8359
2167-8359
DOI:10.7717/peerj.17768