Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery

Documenti analoghi

• An optimized luciferin formulation for NanoLuc-based in vivo bioluminescence imaging.
  di: Gao, Chao, et al.
  Pubblicazione: (2025)
• O‐GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co‐chaperone
  di: Afraah Javed, et al.
  Pubblicazione: (2024)
• Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP ‐43 low‐complexity domain
  di: Thomas B. Walker, et al.
  Pubblicazione: (2026)
• Ordered ATP hydrolysis in the Hsp90 chaperone is regulated by Aha1 and a conserved post‐translational modification
  di: Desmond Prah Amoah, et al.
  Pubblicazione: (2024)
• Computational Elucidation of Possible Contributors to Formation and Stabilization of ATP ‐Lid Down‐Conformation in the N‐Terminal Domain of Hsp90
  di: Keigo Gohda
  Pubblicazione: (2025)