Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.

Gelijkaardige items

• Influenza Polymerase Activity Correlates with the Strength of Interaction between Nucleoprotein and PB2 through the Host-Specific Residue K/E627
  door: Ng, Andy Ka-Leung, et al.
  Gepubliceerd in: (2012)
• Functional Analysis of the Influenza Virus H5N1 Nucleoprotein Tail Loop Reveals Amino Acids That Are Crucial for Oligomerization and Ribonucleoprotein Activities
  door: Chan, Wai-Hon, et al.
  Gepubliceerd in: (2010)
• Structural Basis for RNA Binding and Homo-Oligomer Formation by Influenza B Virus Nucleoprotein
  door: Ng, Andy Ka-Leung, et al.
  Gepubliceerd in: (2012)
• Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein
  door: Hsia, Ho-Pan, et al.
  Gepubliceerd in: (2018)
• Stabilization of Influenza Virus Replication Intermediates Is Dependent on the RNA-Binding but Not the Homo-Oligomerization Activity of the Viral Nucleoprotein
  door: Vreede, Frank T., et al.
  Gepubliceerd in: (2011)