Articles with "lipoylation" as a keyword



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Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation.

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Published in 2022 at "Journal of the American Chemical Society"

DOI: 10.1021/jacs.2c01528

Abstract: Protein lipoylation is an evolutionarily conserved post-translational modification from prokaryotes to eukaryotes. Lipoylation is implicated with several human diseases, including metabolic disorders, cancer, and Alzheimer's disease. While individual lipoylated proteins have been biochemically studied, a… read more here.

Keywords: site specific; quantitative site; lipoylation; protein lipoylation ... See more keywords

Chemical Probes Reveal Sirt2's New Function as a Robust "Eraser" of Lysine Lipoylation.

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Published in 2019 at "Journal of the American Chemical Society"

DOI: 10.1021/jacs.9b06913

Abstract: Lysine lipoylation, a highly conserved lysine PTM, plays a critical role in regulating cell metabolism. The catalytic activity of a number of vital metabolic proteins, such as pyruvate dehydrogenase (PDH), depends on lysine lipoylation. Despite… read more here.

Keywords: lipoylation; sirt2; lysine lipoylation; chemical probes ... See more keywords