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Putative alternative functions of human stefin B (cystatin B): binding to amyloid‐beta, membranes, and copper
Author(s) -
Žerovnik Eva
Publication year - 2017
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2562
Subject(s) - cystatin , cystatin c , amyloid (mycology) , biology , protein folding , amyloid fibril , cytosol , biochemistry , chemistry , computational biology , disease , amyloid β , pathology , medicine , enzyme , botany , renal function
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.