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A peptide dehydratase with core strength
Ribosomally synthesized and post-translationally modified peptide (RiPP) natural products typically rely on substrate recognition through remote protein–protein interaction sites. Now, an atypical dehydratase, whose activity is directed by neighboring azole modifications, has been shown to produce a highly modified peptide hybrid bearing dehydroamino acids, enabling the synthesis of members of the dehydrazole family of RiPPs.
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Chemical Biology of Microbiomes
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Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
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Molecular recording of calcium signals via calcium-dependent proximity labeling
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Bringing chemistry to medicine to redefine the undruggable
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UFL1 triggers replication fork degradation by MRE11 in BRCA1/2-deficient cells