Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation.
Sign Up to like & getrecommendations! 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
Pathogenic variants in GCSH encoding the moonlighting H-protein cause combined nonketotic hyperglycinemia and lipoate deficiency
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DOI: 10.1093/hmg/ddac246
Abstract: Abstract Maintaining protein lipoylation is vital for cell metabolism. The H-protein encoded by GCSH has a dual role in protein lipoylation required for bioenergetic enzymes including pyruvate dehydrogenase and 2-ketoglutarate dehydrogenase, and in the one-carbon… read more here.
Keywords: pathogenic variants; gcsh encoding; protein lipoylation; protein ... See more keywords
Protein lipoylation in mitochondria requires Fe-S cluster assembly factors NFU4 and NFU5.
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DOI: 10.1093/plphys/kiab501
Abstract: Plants have evolutionarily conserved NifU-like (NFU)-domain proteins that are targeted to plastids or mitochondria. 'Plastid-type' NFU1, NFU2 and NFU3 in Arabidopsis (Arabidopsis thaliana) play a role in iron-sulfur (Fe-S) cluster assembly in this organelle, whereas… read more here.
Keywords: mitochondria; nfu4 nfu5; protein lipoylation; nfu5 ... See more keywords