Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom