Residues on the Dimer Interface of SARS Coronavirus 3C-like Protease: Dimer Stability Characterization and Enzyme Catalytic Activity Analysis

Podobné jednotky

• Mutation of Gly-11 on the Dimer Interface Results in the Complete Crystallographic Dimer Dissociation of Severe Acute Respiratory Syndrome Coronavirus 3C-like Protease: CRYSTAL STRUCTURE WITH MOLECULAR DYNAMICS SIMULATIONS
  Autor: Chen, Shuai, a další
  Vydáno: (2008)
• Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure()
  Autor: Hu, Tiancen, a další
  Vydáno: (2009)
• Mechanism for controlling the monomer–dimer conversion of SARS coronavirus main protease
  Autor: Wu, Cheng‐Guo, a další
  Vydáno: (2013)
• Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase N Terminus Is Indispensable for Proteolytic Activity but Not for Enzyme Dimerization: BIOCHEMICAL AND THERMODYNAMIC INVESTIGATION IN CONJUNCTION WITH MOLECULAR DYNAMICS SIMULATIONS
  Autor: Chen, Shuai, a další
  Vydáno: (2005)
• Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus
  Autor: Sun, Haifang, a další
  Vydáno: (2003)