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Barry Potter

As seen in: Nature
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Articles

Design, structure-based optimization and antiviral evaluation of potent inhibitors for the macrodomain Mac1 of SARS-CoV-2

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By Maximilian Sandmann, Simon Sander, David Carrillo, Benedikt Ganter, Celine J. Fischer, Neele Pekarek, Julia M. Berger, Toni Luise Meister, Bruno Canard, Joanna M Watt, Barry Potter, Chris Meier, Sahra Tajdar, Marina Ocenas, Stefanie Etzold, Barbara Selisko, Maria Garcia Alai, Tidow Henning, Pfefferle Susanne, Ralf Fliegert
| Nature Verified
Abstract Enzymatically active macrodomains of (+)ss-RNA viruses mediate immune evasion by countering ADP-ribosylation and are therefore promising druggable targets. Here we report testing of ADP / ADP-ribose analogues for their ability to inhibit Mac1 of SARS-CoV-2, measurement of the affinity of active compounds and characterization of their binding mode by cocrystallization, uncovering critical molecular determinants of protein-ligand interaction.
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The intracellular inositol (pyro)phosphate receptor AtSPX1 reciprocally binds to P1BS DNA - Nature Communications

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By Hayley Whitfield, Megan Gilmartin, Andrew Riley, Megan L. Shipton, Barry Potter, Andrew Hemmings, Charles A. Brearley
| Nature Verified
Abstract The response of plants to phosphate starvation engages PHR (CC-MYB-PHOSPHATE STARVATION RESPONSE) transcription factors that bind to P1BS (GNATATNC) promoter elements of phosphate-starvation induced (PSI) genes. The encoded proteins include single-domain SPX (SYG1/Pho81/XPR1) proteins. SPX proteins bind PHR proteins. Current models of SPX1: PHR interaction define only a high-phosphate role for SPX1, as an inositol (pyro)phosphate-dependent negative regulator of PHR.
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