Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-d-aspartate receptor

Lignende værker

• The Serine Protease Plasmin Cleaves the Amino-terminal Domain of the NR2A Subunit to Relieve Zinc Inhibition of the N-Methyl-d-aspartate Receptors
  af: Yuan, Hongjie, et al.
  Udgivet: (2009)
• Control of NMDA Receptor Function by the NR2 Subunit Amino-Terminal Domain
  af: Yuan, Hongjie, et al.
  Udgivet: (2009)
• Cleavage of the NR2B Subunit Amino Terminus of N-Methyl-d-aspartate (NMDA) Receptor by Tissue Plasminogen Activator: IDENTIFICATION OF THE CLEAVAGE SITE AND CHARACTERIZATION OF IFENPRODIL AND GLYCINE AFFINITIES ON TRUNCATED NMDA RECEPTOR
  af: Ng, Kay-Siong, et al.
  Udgivet: (2012)
• Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies
  af: Ng, Fui-Mee, et al.
  Udgivet: (2008)
• Molecular determinants of coordinated proton and zinc inhibition of N-methyl-d-aspartate NR1/NR2A receptors
  af: Low, Chian-Ming, et al.
  Udgivet: (2000)