Charles S. Craik

The paper uses biased Fab phage-display libraries and computational methods to identify potent serine protease inhibitors and validate their binding interactions.

This paper designs a targeted autoantibody degrader to treat neurologic diseases by specifically clearing pathogenic autoantibodies while preserving the immune system.

The paper links protease sequence variation to biochemical parameters and viral fitness using high-throughput enzymology and replication assays.

The paper identifies a conserved loop in herpesvirus proteases that controls dimerization and enzyme activity, presenting a new target for antiviral inhibitors.

This study determines the structures of CHIP stabilized by Fab antibodies, revealing conformational switches that regulate its E3 ligase and chaperone functions.

This paper describes the discovery of new coronavirus MPro inhibitors with improved pharmacokinetics, broad-spectrum antiviral activity, and superior in vivo efficacy compared to existing drugs.

The paper identifies LyLAP as a key enzyme for lysosomal degradation of transmembrane proteins, showing its role in maintaining endocytic activity and lysosomal stability in pancreatic cancer.

The paper shows that opaque cells in C. albicans up-regulate proteases and transporters to efficiently use proteins as nitrogen sources, enabling white cells to proliferate in mixed cultures.

This paper introduces ITCell, a method that predicts CD4 T-cell epitopes by integrating antigen cleavage, MHCII presentation, and TCR recognition, achieving higher accuracy than single-stage methods.