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Glucose feeds the tricarboxylic acid cycle via excreted ethanol in fermenting yeast

Chemical genomics with pyrvinium identifies <i>C1orf115</i> as a regulator of drug efflux

Glucose feeds the tricarboxylic acid cycle via excreted ethanol in fermenting yeast

Nature Chemical Biology, Published online: 15 August 2022; doi:10.1038/s41589-022-01091-7Metabolic labeling experiments on fermenting yeast revealed that ethanol is oxidized to acetaldehyde and acetyl-CoA and is also a major source of NADH and NADPH, demonstrating that ethanol can be consumed as a TCA cycle and redox fuel.

Chemical genomics with pyrvinium identifies <i>C1orf115</i> as a regulator of drug efflux

Nature Chemical Biology, Published online: 15 August 2022; doi:10.1038/s41589-022-01109-0A chemical genomics approach was used to identify regulators of drug sensitivity for pyrvinium, a cytotoxic agent with anti-cancer potential, revealing mitochondrial complex I sensitivities and a role for C1orf115 in regulating ABCB1 activity.

Identifying cell receptors for the nanoparticle protein corona using genome screens

Unbiased matchmaking

Bicyclostreptins are radical SAM enzyme-modified peptides with unique cyclization motifs

Artificial intelligence uncovers carcinogenic human metabolites

Unbiased matchmaking

Nature Chemical Biology, Published online: 11 August 2022; doi:10.1038/s41589-022-01108-1Elucidating the interactions between serum protein-bound nanoparticles and cell-surface receptors typically operates on a per protein–receptor interaction basis. Integration of omic approaches for testing thousands of interactions unbiasedly reveals important interactions...

Bicyclostreptins are radical SAM enzyme-modified peptides with unique cyclization motifs

Nature Chemical Biology, Published online: 11 August 2022; doi:10.1038/s41589-022-01090-8Bicyclostreptins are peptide natural products in which a macrocyclic β-ether and a heterocyclic sp3–sp3 linkage between a backbone amide nitrogen and an adjacent α-carbon are installed by two radical S-adenosylmethionine metalloenzymes.

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