NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics

Lignende værker

• Structurally- and dynamically-driven allostery of the chymotrypsin-like proteases of SARS, Dengue and Zika viruses
  af: Lim, Liangzhong, et al.
  Udgivet: (2019)
• Curcumin Allosterically Inhibits the Dengue NS2B-NS3 Protease by Disrupting Its Active Conformation
  af: Liangzhong Lim, et al.
  Udgivet: (2020-09-01)
• Curcumin Allosterically Inhibits the Dengue NS2B-NS3 Protease by Disrupting Its Active Conformation
  af: Lim, Liangzhong, et al.
  Udgivet: (2020)
• Intrinsically Unstructured Domain 3 of Hepatitis C Virus NS5A Forms a “Fuzzy Complex” with VAPB-MSP Domain Which Carries ALS-Causing Mutations
  af: Gupta, Garvita, et al.
  Udgivet: (2012)
• Structural, Stability, Dynamic and Binding Properties of the ALS-Causing T46I Mutant of the hVAPB MSP Domain as Revealed by NMR and MD Simulations
  af: Lua, Shixiong, et al.
  Udgivet: (2011)