Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers

Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins

(2009) Victoria A. Higman et al.   JOURNAL OF BIOMOLECULAR NMR

Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20

(2009) C. Bagnéris et al.   JOURNAL OF MOLECULAR BIOLOGY

Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)

(2009) Greg L Hura et al.   NATURE METHODS

The eye lens chaperone  -crystallin forms defined globular assemblies

(2009) J. Peschek et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Crystallin proteins and amyloid fibrils

(2008) H. Ecroyd et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

αB-Crystallin: A Hybrid Solid-State/Solution-State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer

(2008) Stefan Jehle et al.   JOURNAL OF MOLECULAR BIOLOGY

Influence of different assignment conditions on the determination of symmetric homodimeric structures with ARIA

(2008) Benjamin Bardiaux et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core

(2008) C. Wasmer et al.   SCIENCE

Ser-59 is the major phosphorylation site in αB-crystallin accumulated in the brains of patients with Alexander's disease

(2003) Kanefusa Kato et al.   JOURNAL OF NEUROCHEMISTRY