Evidence Source

Description	Imported from Merops: Merops-evidence: experimental \| Merops-type: physiological \| Merops-range: 135-304
Method
Experimental system	unknown
Perturbation	none
Protease inhibitor(s) used
Directness	unknown
Physiological relevance	yes
Evidence Code(s)	inferred from experiment
Database / Laboratory	- Lab: Kalbacher H - DB: MEROPS
Raw data repository

Evidence for:

Publication(s)	Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro. Beck H, Schwarz G, Schroter CJ, Deeg M, Baier D, Stevanovic S, Weber E, Driessen C, Kalbacher H Eur J Immunol. 2001 Dec;31(12):3726-36. PMID: 11745393

Publication(s)

Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro.

Beck H, Schwarz G, Schroter CJ, Deeg M, Baier D, Stevanovic S, Weber E, Driessen C, Kalbacher H