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- W4323532396 abstract "Post-translational modifications (PTMs) of proteins not only exponentially increase the diversity of proteoforms, but also contribute to dynamically modulating the localization, stability, activity, and interaction of proteins. Understanding the biological consequences and functions of specific PTMs has been challenging for many reasons, including the dynamic nature of many PTMs and the technical limitations to access homogenously modified proteins. The genetic code expansion technology has emerged to provide unique approaches for studying PTMs. Through site-specific incorporation of unnatural amino acids (UAAs) bearing PTMs or their mimics into proteins, genetic code expansion allows the generation of homogenous proteins with site-specific modifications and atomic resolution both in vitro and in vivo. With this technology, various PTMs and mimics have been precisely introduced into proteins. In this review, we summarize the UAAs and approaches that have been recently developed to site-specifically install PTMs and their mimics into proteins for functional studies of PTMs." @default.
- W4323532396 created "2023-03-09" @default.
- W4323532396 creator A5002571324 @default.
- W4323532396 creator A5010559849 @default.
- W4323532396 creator A5074502765 @default.
- W4323532396 creator A5088099956 @default.
- W4323532396 date "2023-03-22" @default.
- W4323532396 modified "2023-10-10" @default.
- W4323532396 title "Functional analysis of protein post‐translational modifications using genetic codon expansion" @default.
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