Formation of Amyloid Fibrils in Vitro by Human yd-crystallin and its Isolated Domains
Amyloid fibrils are associated with a variety of human protein misfolding and protein deposition diseases. Previous studies have shown that bovine crystallins form amyloid fibers under denaturing conditions and amyloid fibers accumulate in the lens of mice carrying mutations in crystallin genes. Within differentiating lens fiber cells, crystallins may be exposed to low pH lysosome compartments. We have investigated whether human γD-crystallin forms amyloid fibrils in vitro, when exposed to low pH partially denaturing conditions.
Papanikolopoulou, K., I. Mills-Henry, S. L. Thol, Y. Wang, et al. 2008. "Formation of Amyloid Fibrils in Vitro by Human yd-crystallin and its Isolated Domains." Molecular Vision 14: 81-89.
Chemistry and Biochemistry