Area of research
Cancer Research · Oncology
Research interest
Research focused on Matrix metalloproteinase and Computational biology, with related work in Cancer, Matrix metalloproteinase inhibitor, Serine protease. Notable publications include 'Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution', 'Long-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme Activation', and 'Converting a broad matrix metalloproteinase family inhibitor into a specific inhibitor of MMP ‐9 and MMP ‐14'.
Engineered TIMP2 with narrow MMP-9 specificity is an effective inhibitor of invasion and proliferation of triple-negative breast cancer cells
Improving Circulation Half-Life of Therapeutic Candidate N-TIMP2 by Unfolded Peptide Extension
Abstract 1331 Engineering Tissue Inhibitor of Metalloproteinases-1 (TIMP-1) Variants with Improved Binding Selectivity toward Matrix Metalloproteinase-9 (MMP-9) as potential protein therapeutics
The roles of proteases in prostate cancer
Designed Loop Extension Followed by Combinatorial Screening Confers High Specificity to a Broad Matrix MetalloproteinaseInhibitor
Climbing Up and Down Binding Landscapes through Deep Mutational Scanning of Three Homologous Protein–Protein Complexes
Converting a broad matrix metalloproteinase family inhibitor into a specific inhibitor of <scp>MMP</scp> ‐9 and <scp>MMP</scp> ‐14
A potent, proteolysis-resistant inhibitor of kallikrein-related peptidase 6 (KLK6) for cancer therapy, developed by combinatorial engineering
Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution
Serine protease inhibitor Kazal type 1 (SPINK1) drives proliferation and anoikis resistance in a subset of ovarian cancers
Zymogen Activation Confers Thermodynamic Stability on a Key Peptide Bond and Protects Human Cationic Trypsin from Degradation
Long-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme Activation