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Buuh ZY , Lyu Z , Wang RE
Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins
J Med Chem. 2018 Apr 26;61(8) :3239-3252
PMID: 28505447 URL: https://www.ncbi.nlm.nih.gov/pubmed/28505447
AbstractPost-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pivotal pathways related to cellular response and stability. Due to the roles these dynamic modifications assume, their dysregulation has been associated with cancer and many other important diseases such as inflammatory disorders and neurodegenerative diseases. For this reason, we present a review and perspective on important post-translational modifications on non-histone proteins, with emphasis on their roles in diseases and small molecule inhibitors developed to target PTM writers. Certain PTMs' contribution to epigenetics has been extensively expounded; yet more efforts will be needed to systematically dissect their roles on non-histone proteins, especially for their relationships with nononcological diseases. Finally, current research approaches for PTM study will be discussed and compared, including limitations and possible improvements.
Notes1520-4804 Buuh, Zakey Yusuf Lyu, Zhigang Wang, Rongsheng E Orcid: 0000-0002-5749-7447 Journal Article Research Support, Non-U.S. Gov't Review United States J Med Chem. 2018 Apr 26;61(8):3239-3252. doi: 10.1021/acs.jmedchem.6b01817. Epub 2017 May 24.