Ubiquitination of Neuronal Nitric-oxide Synthase in the Calmodulin-binding Site Triggers Proteasomal Degradation of the Protein

Documenti analoghi

• Dynamic Cycling with Hsp90 Stabilizes Neuronal Nitric Oxide Synthase Through Calmodulin-dependent Inhibition of Ubiquitination
  di: Peng, Hwei-Ming, et al.
  Pubblicazione: (2009)
• C331A Mutant of Neuronal Nitric-oxide Synthase Is Labilized for Hsp70/CHIP (C Terminus of HSC70-interacting Protein)-dependent Ubiquitination
  di: Clapp, Kelly M., et al.
  Pubblicazione: (2010)
• Modulation of Heme/Substrate Binding Cleft of Neuronal Nitric-oxide Synthase (nNOS) Regulates Binding of Hsp90 and Hsp70 Proteins and nNOS Ubiquitination
  di: Peng, Hwei-Ming, et al.
  Pubblicazione: (2012)
• Architecture of the Nitric-oxide Synthase Holoenzyme Reveals Large Conformational Changes and a Calmodulin-driven Release of the FMN Domain
  di: Yokom, Adam L., et al.
  Pubblicazione: (2014)
• Hsp70:CHIP Ubiquitinates Dysfunctional but Not Native Neuronal NO Synthase
  di: Davis, Amanda K., et al.
  Pubblicazione: (2020)