ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants
Author:
Funder
Ministry of Education - Singapore
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. Hydrotropic function of ATP in the crystalline lens;Greiner;Exp. Eye Res.,2020
2. The βγ-crystallins: native state stability and pathways to aggregation;Serebryany;Prog. Biophys. Mol. Biol.,2014
3. Crystallins and their complexes;Ghosh;Subcell. Biochem.,2019
4. Protein interactions in the calf eye lens: interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive;Tardieu;Eur. Biophys. J.,1992
5. A small-angle neutron scattering study of gamma-crystallins near their isoelectric point;Petitt;Eur. J. Biochem.,1997
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