Associated Papers
Human dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation.
Streeter O et al.
Acta Crystallographica. Section D, Structural Biology, 2025
The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.
Singh SM et al.
Biophysical Journal, 2012
Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.
Singh SM et al.
Proteins, 2012
Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.
Singh SM et al.
Proceedings of the National Academy of Sciences of the United States of America, 2010
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