Cataract-Causing Defect of a Mutant γ-Crystallin Proceeds through an Aggregation Pathway Which Bypasses Recognition by the α-Crystallin Chaperone

Increased Hydrophobicity and Decreased Backbone Flexibility Explain the Lower Solubility of a Cataract-Linked Mutant of ?D-Crystallin

(2011) Priya R. Banerjee et al.   JOURNAL OF MOLECULAR BIOLOGY

The Congenital Cataract-Linked G61C Mutation Destabilizes γD-Crystallin and Promotes Non-Native Aggregation

(2011) Wang Zhang et al.   PLoS One

Increase in Surface Hydrophobicity of the Cataract-Associated P23T Mutant of Human γD-Crystallin Is Responsible for Its Dramatically Lower, Retrograde Solubility

(2010) Ajay Pande et al.   BIOCHEMISTRY

Aggregation of deamidated human βB2-crystallin and incomplete rescue by α-crystallin chaperone

(2010) Magalie Michiel et al.   EXPERIMENTAL EYE RESEARCH

Partially Folded Aggregation Intermediates of Human γD-, γC-, and γS-Crystallin Are Recognized and Bound by Human αB-Crystallin Chaperone

(2010) Ligia Acosta-Sampson et al.   JOURNAL OF MOLECULAR BIOLOGY

A Single Mutation Promotes Amyloidogenicity through a Highly Promiscuous Dimer Interface

(2010) Francis C. Peterson et al.   STRUCTURE

Conformational Pathology of the Serpins: Themes, Variations, and Therapeutic Strategies

(2009) Bibek Gooptu et al.   Annual Review of Biochemistry

The G18V CRYGS Mutation Associated with Human Cataracts Increases γS-Crystallin Sensitivity to Thermal and Chemical Stress

(2009) Zhiwei Ma et al.   BIOCHEMISTRY

Hydrophobic Core Mutations Associated with Cataract Development in Mice Destabilize Human γD-Crystallin

(2009) Kate L. Moreau et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein

(2008) Elizabeth M. Baden et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Deamidation destabilizes and triggers aggregation of a lens protein, βA3-crystallin

(2008) Takumi Takata et al.   PROTEIN SCIENCE