Results 191 to 200 of about 4,073 (218)
Mitochondrial fatty acid synthesis is an emergent central regulator of mammalian oxidative metabolism. [PDF]
Wedan RJ, Longenecker JZ, Nowinski SM.
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Cuproptosis: A potential therapeutic target in clear cell renal cell carcinoma. [PDF]
Zhao Y +6 more
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Emerging regulated cell death mechanisms in bone remodeling: decoding ferroptosis, cuproptosis, disulfidptosis, and PANoptosis as therapeutic targets for skeletal disorders. [PDF]
Hu HT +14 more
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ABHD11 mediated deglutarylation regulates the TCA cycle and T cell metabolism
Grice GL +7 more
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Chemical Tagging of Protein Lipoylation
Angewandte Chemie, 2020AbstractProtein lipoylation is a post‐translational modification of emerging importance in both prokaryotes and eukaryotes. However, labeling and large‐scale profiling of protein lipoylation remain challenging. Here, we report the development of iLCL (iodoacetamide‐assisted lipoate‐cyclooctyne ligation), a chemoselective reaction that enables chemical ...
Qi Tang +3 more
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A colorimetric method for the assay of lipoyl dehydrogenase [PDF]
A colorimetric method for the direct assay of lipoyl dehydrogenase is described. Enzyme reaction is stopped by ethanol precipitation. This is followed by the displacement of 1,3-bis(2′-pyridyl)-1,2-diaza-prop-2-ene (PAPHY) from a Pd(II)-PAPHY complex by reduced lipoic acid.
Kum Tatt Lee, Ai Mee Seet
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N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase
Archives of Biochemistry and Biophysics, 1969Abstract N - dl -Lipoyl- d -glucosamine and N - dl -lipoyl- d -glucosaminitol were prepared and tested as substrates for lipoyl dehydrogenase (reduced nicotinamide adenine dinucleotide: Lipoamide oxidoreductase, EC 1.6.4.3). It was anticipated that such lipoateamino carbohydrate derivatives would be superior substrates for the enzyme, having ...
Bruce P. Gaber +2 more
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Molecular Microbiology, 1990
SummaryThe overexpression of a subgene encoding a hybrid lipoyl domain of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli has previously bee shown to result in the formation of lipoylated an unlipoylated products.
P. R. Ashton +4 more
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SummaryThe overexpression of a subgene encoding a hybrid lipoyl domain of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli has previously bee shown to result in the formation of lipoylated an unlipoylated products.
P. R. Ashton +4 more
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