Binding of the Inward Rectifier K+ Channel Kir 2.3 to PSD-95 Is Regulated by Protein Kinase A Phosphorylation

This publication has 60 references indexed in Scilit:

• Cloning and Characterization of Postsynaptic Density 93, a Nitric Oxide Synthase Interacting Protein
  Journal of Neuroscience, 1996
• Crystal Structures of a Complexed and Peptide-Free Membrane Protein–Binding Domain: Molecular Basis of Peptide Recognition by PDZ
  Cell, 1996
• Interaction of Nitric Oxide Synthase with the Postsynaptic Density Protein PSD-95 and α1-Syntrophin Mediated by PDZ Domains
  Published by Elsevier ,1996
• Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
  Cell, 1995
• Cloning and expression of two brain-specific inwardly rectifying potassium channels.
  Proceedings of the National Academy of Sciences, 1995
• Kir2.1 inward rectifier K+ channels are regulated independently by protein kinases and ATP hydrolysis
  Neuron, 1994
• Nomenclature for mammalian potassium channel genes
  Trends in Pharmacological Sciences, 1993
• Atrial G protein-activated K+ channel: expression cloning and molecular properties.
  Proceedings of the National Academy of Sciences, 1993
• Nitric oxide synthase in the visual cortex of monocular monkeys as revealed by light and electron microscopic immunocytochemistry
  Brain Research, 1993
• The rat brain postsynaptic density fraction contains a homolog of the drosophila discs-large tumor suppressor protein
  Neuron, 1992