Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain
Ennes A. Auerswald(LMU Klinikum), Hans Fritz(Novartis (Switzerland)), Dorit K. Nägler(Klinikum Ludwigshafen), Werner Machleidt(Ludwig-Maximilians-Universität München), Irmgard Assfalg‐Machleidt(Ludwig-Maximilians-Universität München), Milton T. Stubbs(University Hospital in Halle)
Cited by 41
Related Papers
Proteomic Identification of Protease Cleavage Sites Characterizes Prime and Non-prime Specificity of Cysteine Cathepsins B, L, and S
|Journal of Proteome Research|2011|190
Major Increase in Endopeptidase Activity of Human Cathepsin B upon Removal of Occluding Loop Contacts
|Biochemistry|1997|165
The contact system—a novel branch of innate immunity generating antibacterial peptides
|The EMBO Journal|2006|150
Human Cathepsin X: A Cysteine Protease with Unique Carboxypeptidase Activity
|Biochemistry|1999|135
RGD-dependent Binding of Procathepsin X to Integrin αvβ3 Mediates Cell-adhesive Properties
|Journal of Biological Chemistry|2006|103