Anthony John O’Donoghue

The paper characterizes LOca-1, a calcium-activated arginyl-specific orthocaspase from Loki's Castle, showing its thermoactivity and structural conservation with plant metacaspases.

This study characterizes glycosyl hydrolase 18 chitinases from chloroviruses, revealing their enzymatic properties, structural features, and potential as biotechnological tools for algal control.

This study identifies aspartic proteases as active enzymes in acidified wound fluid, showing their activity is optimal between pH 3.0 and 3.8 and persists for ten days post-injury.

This paper develops a recombinant Pf20S platform for structural analysis and inhibitor design, identifying a selective inhibitor with high potency against Plasmodium falciparum proteasome.

The paper evaluates thio- and seleno-semicarbazones and their azole derivatives for treating African trypanosomiasis, finding Se derivatives more active than S analogues and highlighting the importance of combining TbrCATL inhibition with antioxidant activity.

The paper introduces mspms, an R package and graphical interface for analyzing MSP-MS data, validated using cathepsin substrate profiling.

The paper presents the cryo-EM structure of the human 20S proteasome bound to marizomib, revealing its binding mode and irreversible inhibitory mechanism.

This study identifies three new ketomemicin analogs from Salinispora pacifica, maps their biosynthetic gene cluster across Salinispora species, and reports their protease inhibitory activity.

This study characterizes RHBDL4 enzymatic properties using an in vitro platform, identifying effective inhibitors and providing insights for drug development.

This study identifies midgut proteases in Aedes aegypti mosquitoes and their role in blood meal digestion using MSP-MS, revealing shifts in proteolytic activity and substrate specificity.

The paper develops subunit-specific proteasome substrates for Schistosoma species, showing improved performance and cross-species applicability.

This study uses native metabolomics to identify a family of protease inhibitors from cyanobacteria, revealing their structure and potent biological activity.

The paper evaluates gallinamide A and its analogs against Trypanosoma cruzi, finding that intramolecular π-π stacking interactions enhance potency by improving solubility and permeability.