Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Karagöz, G. Elif, Duarte, Afonso M.S., Akoury, Elias, Ippel, Hans, Biernat, Jacek, Morán Luengo, Tania, Radli, Martina, Didenko, Tatiana +8 more·2014·Cell

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  5. Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome
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  8. Using β-strand and β-hairpin peptidomimetics induced by constrained amino acids to modulate the aggregation of the microtubule associated protein Tau : design, synthesis and evaluation
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  9. Inducing β-hairpin and α-helix folding in peptides : design, synthesis and evaluation of α-synuclein and tau aggregation inhibitors
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  10. The Role of Molecular Chaperones in Tau Proteostasis: Potential Therapeutic Opportunities in Tauopathies
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  13. Cerebrovascular Single-Nucleus RNA-Seq Reveals Heat Shock Activation and Vascular Remodeling in Alzheimer’s Disease and Primary Tauopathies
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  15. The N-terminal domain of the endoplasmic reticulum-resident chaperone Grp94 functions in aggregation prevention
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  16. AHA1 Regulates Aβ Production via Modulation of APP Abundance and γ‐Secretase Assembly
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  18. BindingDB Entry 50009799: Development of Heat Shock Protein (Hsp90) Inhibitors To Combat Resistance to Tyrosine Kinase Inhibitors through Hsp90-Kinase Interactions.
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  20. BindingDB Entry 50009378: Allosteric Modulator Discovery: From Serendipity to Structure-Based Design.
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  21. BindingDB Entry 50006236: Progress in the discovery and development of heat shock protein 90 (Hsp90) inhibitors.
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