Petra Mlčochová

TL;DR: Investigation of the activity and expression of GCPII in various compartments of the human brain using a radiolabeled substrate of the enzyme and the novel monoclonal antibody GCP-04 shows that this antibody is more sensitive in immunoblots than the widely used antibody 7E11.

TL;DR: In this paper, crystal structures of the human GCPII complexed with three glutamate mimetics/derivatives, 2-(phosphonomethyl)pentanedioic acid (2-PMPA), quisqualic acid, and L-serine O-sulfate (L-SOS), at 1.72, 1.62, and 2.10 A resolution were reported.

TL;DR: This work reports the cloning, expression, and characterization of recombinant human GCPIII, a GCPII homolog with 67% amino acid identity that has lower N‐acetyl‐l‐aspartyl‐glutamate‐hydrolyzing activity, different pH and salt concentration dependence, and distinct substrate specificity, indicating that these homologs might play different biological roles.

TL;DR: A mutant of human GCPII [GCPII(E424A)], in which Glu424, a putative proton shuttle residue, is substituted with alanine, provides a detailed and consistent picture of the reaction mechanism of this highly interesting enzyme at the atomic level.

TL;DR: A pseudopeptide inhibitor, QF34, is designed that efficiently inhibits a wide variety of PR variants and suggests a promising route for the design of second-generation PIs that are active against a variety of resistant PR variants.