Pamela J. E. Rowling

This paper describes a method to purify and characterize soluble domains of bacterial membrane receptors, demonstrating its effectiveness with the HasR receptor from Pseudomonas aeruginosa.

This study identifies chemically constrained peptides that inhibit PfUCHL3, a critical deubiquitinating enzyme in Plasmodium falciparum, by blocking substrate binding rather than active site interaction.

The paper investigates how the CMV 2b protein interacts with AGO1 and 1a protein, finding that residues 56-60 influence these interactions but no single residue is solely responsible.