Results 191 to 200 of about 4,073 (218)

Cuproptosis: A potential therapeutic target in clear cell renal cell carcinoma. [PDF]

open access: yesChin Med J (Engl)
Zhao Y   +6 more
europepmc   +1 more source

Emerging regulated cell death mechanisms in bone remodeling: decoding ferroptosis, cuproptosis, disulfidptosis, and PANoptosis as therapeutic targets for skeletal disorders. [PDF]

open access: yesCell Death Discov
Hu HT   +14 more
europepmc   +1 more source

ABHD11 mediated deglutarylation regulates the TCA cycle and T cell metabolism

open access: yes
Grice GL   +7 more
europepmc   +1 more source
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Chemical Tagging of Protein Lipoylation

Angewandte Chemie, 2020
AbstractProtein 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
openaire   +3 more sources

A colorimetric method for the assay of lipoyl dehydrogenase [PDF]

open access: possibleMikrochimica Acta, 1975
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
openaire   +2 more sources

N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase

Archives of Biochemistry and Biophysics, 1969
Abstract 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
openaire   +3 more sources

Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyl‐deficient strain of Escherichia coli

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
openaire   +3 more sources

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