title: Putative alternative functions of human stefin B (cystatin B): binding to amyloid-beta, membranes, and copper.
abstract: We describe studies performed thus far on stefin B from the family of cystatins as a model protein for folding and amyloid fibril formation studies. We also briefly mention our studies on aggregation of some of the missense EPM1 mutants of stefin B in cells, which mimic additional pathological traits (gain in toxic function) in selected patients with EPM1 disease. We collected data on the reported interactors of stefin B and discuss several hypotheses of possible cytosolic alternative functions.
authors: Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Ljubljana, Slovenia.|CipKeBip-Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Ljubljana, Slovenia.
authors: Eva
authors: E
authors: Žerovnik
mesh_terms: D016229:Amyloid beta-Peptides / Q000378:metabolism*; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D055313:Cystatin B / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D020125:Mutation, Missense; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D016229:Amyloid beta-Peptides; C524994:CSTB protein, human; D003300:Copper; D055313:Cystatin B
keywords: amyloid; chaperone; cystatins; membrane binding; oligomers; oxidative stress; protein aggregation; protein folding