Article
Abnormal assemblies and subunit exchange of alphaB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure.
Biochemistry - 20 Jan 2009
Michiel Magalie, Skouri-Panet Fériel, Duprat Elodie, Simon Stéphanie, Férard Céline, Tardieu Annette, Finet Stéphanie
Abstract excerpt
Mutation of the Arg120 residue in the human alphaB-crystallin sequence has been shown to be associated with a significant ability to aggregate in cultured cells and have an increased oligomeric size coupled to a partial loss of the chaperone-like activity in vitro. In the present study, static and dynamic light scattering, small-angle X-ray scattering, and size exclusion chromatography were used to follow the...
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