Person Dr Ashley Buckle Monash University Viewed: [[ro.stat.viewed]] Click to explore relationships graph Help Related Data $relation_to_title = []; $dupes = 0;?> Manages A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Manages A common fold mediates vertebrate defense and bacterial attack Manages Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site. Manages Crystal structure of scabies mite inactivated protease paralogue S-D1 (SMIPP-S-D1) Manages Crystal structures of the substrate free-enzyme, and reaction intermediate of the HAD superfamily member, haloacid dehalogenase DehIVa from Burkholderia cepacia MBA4. View all 32 related data User Contributed Tags Login to tag this record with meaningful keywords to make it easier to discover Identifiers Local : MON:0000039742 Saved to MyRDA Save to MyRDA Contact Information Ashley.Buckle@monash.eduhttp://www.monash.edu.au/research/profiles/profile.html?sid=5224&pid=3721
Click to explore relationships graph Help Related Data $relation_to_title = []; $dupes = 0;?> Manages A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Manages A common fold mediates vertebrate defense and bacterial attack Manages Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site. Manages Crystal structure of scabies mite inactivated protease paralogue S-D1 (SMIPP-S-D1) Manages Crystal structures of the substrate free-enzyme, and reaction intermediate of the HAD superfamily member, haloacid dehalogenase DehIVa from Burkholderia cepacia MBA4. View all 32 related data User Contributed Tags Login to tag this record with meaningful keywords to make it easier to discover Identifiers Local : MON:0000039742