Pages that link to "Q69961157"

The following pages link to Folding-unfolding and aggregation-dissociation of bovine alpha-crystallin subunits; evidence for unfolding intermediates of the alpha A subunits (Q69961157):

Displaying 12 items.

• Unfolding of human lens recombinant betaB2- and gammaC-crystallins (Q28216321) (← links)
• Importance of eye lens α‐crystallin heteropolymer with 3:1 αA to αB ratio: Stability, aggregation, and modifications (Q36738905) (← links)
• Conformational stability of bovine alpha-crystallin. Evidence for a destabilizing effect of ascorbate (Q42161461) (← links)
• Calcium-induced decrease of the thermal stability and chaperone activity of alpha-crystallin (Q44214872) (← links)
• NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins (Q47897027) (← links)
• Unfolding and refolding of bovine alpha-crystallin in urea and its chaperone activity. (Q53913822) (← links)
• Dissociation of human alphaB-crystallin aggregates by thiocyanate is structurally and functionally reversible (Q59262071) (← links)
• Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity (Q71763382) (← links)
• The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐Crystallin (Q71814271) (← links)
• Thermodynamic stability of human lens recombinant alphaA- and alphaB-crystallins (Q73195844) (← links)
• The hydrophobic probe 4,4'-bis(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of alpha B-crystallin (Q73450829) (← links)
• Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides (Q73718014) (← links)