Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin binding domains of utrophin and dystrophin()

Eitemau Tebyg

• Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-β aggregates
  gan: Singh, Surinder M., et al.
  Cyhoeddwyd: (2010)
• Tissue-Specificity of Dystrophin–Actin Interactions: Isoform-Specific Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains
  gan: Upadhyay, Vaibhav, et al.
  Cyhoeddwyd: (2020)
• Missense Mutation Lys18Asn in Dystrophin that Triggers X-Linked Dilated Cardiomyopathy Decreases Protein Stability, Increases Protein Unfolding, and Perturbs Protein Structure, but Does Not Affect Protein Function
  gan: Singh, Surinder M., et al.
  Cyhoeddwyd: (2014)
• 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
  gan: Singh, Surinder M., et al.
  Cyhoeddwyd: (2012)
• Role of partial protein unfolding in alcohol-induced protein aggregation
  gan: Singh, Surinder M., et al.
  Cyhoeddwyd: (2010)