M. F. Fisher

The paper solves the crystal structure of Arabidopsis thaliana HPPK/DHPS, revealing structural conservation with bacterial enzymes and exploring the herbicidal and antibacterial activity of asulam and related compounds.

The paper uses solution NMR and racemic crystallography to characterize the structure of PDP-23 and related peptides, revealing their unique folding and potential as drug scaffolds.

The paper characterizes the structural features of nine PawL-Derived Peptides (PLPs), revealing beta-turns and sequence diversity but no antibacterial or antifungal activity.

The paper describes a chameleonic macrocyclic peptide, PDP-23, which can adopt different structures and is used to create a cell-penetrating inhibitor of the P-glycoprotein drug efflux pump.

The paper rediscovered evolidine, a plant cyclic peptide, and identified its biosynthetic origin through de novo transcriptomics, revealing a diverse family of related peptides in Rutaceae.

The paper characterizes the structural features of Vicilin Buried Peptides (VBPs) using solution NMR spectroscopy, revealing a helix-loop-helix hairpin fold stabilized by disulfide bonds and inter-helix interactions.

The paper identifies ten novel cyclic peptides in Annona muricata seeds and reveals their ribosomal biosynthesis mechanism through transcriptomic and mass spectrometry analysis.

The paper shows butelase 1 retains cleavage activity despite being classified as a ligase, with structural insights into its macrocyclization efficiency.