Person Dr Sheena McGowan Monash University Viewed: [[ro.stat.viewed]] Click to explore relationships graph Help Related Data $relation_to_title = []; $dupes = 0;?> Owner of A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Enriches Synthesis of new (-)-Bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase. Owner of X-ray crystal structure and specificity of the Plasmodium falciparum malaria aminopeptidase PfM18AAP Owner of X-ray crystal structure of the streptococcal specific phage lysin PlyC User Contributed Tags Login to tag this record with meaningful keywords to make it easier to discover Identifiers Local : MON:0000042593 Saved to MyRDA Save to MyRDA Contact Information Sheena.McGowan@monash.eduhttp://www.monash.edu.au/research/profiles/profile.html?sid=3301&pid=3399
Click to explore relationships graph Help Related Data $relation_to_title = []; $dupes = 0;?> Owner of A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Enriches Synthesis of new (-)-Bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase. Owner of X-ray crystal structure and specificity of the Plasmodium falciparum malaria aminopeptidase PfM18AAP Owner of X-ray crystal structure of the streptococcal specific phage lysin PlyC User Contributed Tags Login to tag this record with meaningful keywords to make it easier to discover Identifiers Local : MON:0000042593