Biochemical mechanisms of aggregation in TGFBI-linked corneal dystrophies
Transforming growth factor-β-induced protein (TGFBIp), an extracellular matrix protein, is the
second most abundant protein in the corneal stroma. In this review, we summarize the …
second most abundant protein in the corneal stroma. In this review, we summarize the …
Critical influence of cosolutes and surfaces on the assembly of serpin-derived amyloid fibrils
MW Risør, DW Juhl, M Bjerring, J Mathiesen… - Biophysical journal, 2017 - cell.com
Many proteins and peptides self-associate into highly ordered and structurally similar
amyloid cross-β aggregates. This fibrillation is critically dependent on properties of the …
amyloid cross-β aggregates. This fibrillation is critically dependent on properties of the …
Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain
Numerous mutations in the corneal protein TGFBIp lead to opaque extracellular deposits
and corneal dystrophies (CDs). Here we elucidate the molecular origins underlying …
and corneal dystrophies (CDs). Here we elucidate the molecular origins underlying …
How glycosaminoglycans promote fibrillation of salmon calcitonin
Glycosaminoglycans (GAGs) bind all known amyloid plaques and help store protein
hormones in (acidic) granular vesicles, but the molecular mechanisms underlying these …
hormones in (acidic) granular vesicles, but the molecular mechanisms underlying these …
The changing face of aging: highly sulfated glycosaminoglycans induce amyloid formation in a lattice corneal dystrophy model protein
Glycosaminoglycans (GAGs) are related to multiple biological functions and diseases. There
is growing evidence that GAG concentration and sulfate content increase with age. The …
is growing evidence that GAG concentration and sulfate content increase with age. The …