Corneal Dystrophy Mutations Drive Pathogenesis by Targeting TGFBIp Stability and Solubility in a Latent Amyloid-forming Domain.
Stenvang M, Schafer NP, Malmos KG, Pérez AW, Niembro O, Sormanni P, Basaiawmoit RV, Christiansen G, Andreasen M, Otzen DE.
Stenvang M, et al.
J Mol Biol. 2018 Apr 13;430(8):1116-1140. doi: 10.1016/j.jmb.2018.03.001. Epub 2018 Mar 7.
J Mol Biol. 2018.
PMID: 29524512
Thus, TGFBIp aggregation is driven by mutations that despite their physico-chemical diversity target either the stability or solubility of Fas1-4 in predictable ways, suggesting straightforward general therapeutic strategies....
Thus, TGFBIp aggregation is driven by mutations that despite their physico-chemical diversity target either the stability or solubility of F …