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Barry Sleno on Muck Rack

Barry Sleno

As seen in: Nature, PLOS ONE
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Articles

Crystal structure of the fungal mannosyltransferase Och1 reveals active site primed for N-glycan binding

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By Dmitry A. Rodionov, Barry Sleno, Albert M. Berghuis, Pedro A. Romero
| PLOS ONE
Loading metrics Open Access Peer-reviewed Research Article Citation: Kelly ETR, Rodionov D, Sleno B, Romero PA, Berghuis AM (2025) Crystal structure of the fungal mannosyltransferase Och1 reveals active site primed for N-glycan binding. PLoS One 20(7): e0329259.
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Structural and functional insights into esterase-mediated macrolide resistance

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By Jaeok Park, Albert M. Berghuis, St John’s, Barry Sleno
| Nature Verified
Abstract Macrolides are a class of antibiotics widely used in both medicine and agriculture. Unsurprisingly, as a consequence of their exensive usage a plethora of resistance mechanisms have been encountered in pathogenic bacteria. One of these resistance mechanisms entails the enzymatic cleavage of the macrolides’ macrolactone ring by erythromycin esterases (Eres). The most frequently identified Ere enzyme is EreA, which confers resistance to the majority of clinically used macrolides.
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