• Publications
  • Influence
Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice.
  • J. Pak, F. Huang, +5 authors K. Huang
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 10 October 2000
A central role of Ng in the regulation of CaMKII activity with decisive influences on synaptic plasticity and spatial learning is indicated. Expand
Feedback regulation of phospholipase C-beta by protein kinase C.
  • S. Ryu, U. Kim, +4 authors S. Rhee
  • Medicine, Biology
  • The Journal of biological chemistry
  • 15 October 1990
It is proposed that rather than having a direct effect on enzyme activity, the phosphorylation of PLC-beta by PKC may alter its interaction with a putative guanine nucleotide-binding regulatory protein and thereby prevent its activation. Expand
Phosphorylation of CCAAT-enhancer binding protein by protein kinase C attenuates site-selective DNA binding.
Four DNA-recombinant proteins, corresponding to the DNA-binding domain of CCAAT/enhancer binding protein (C/EBP), were phosphorylated in vitro by protein kinase C (PKC). High-performance liquidExpand
Differential distribution of protein kinase C isozymes in the various regions of brain.
The results indicate that protein kinase C isozymes are differentially distributed in various regions of rat and monkey brains and suggest a unique role for each isozyme in controlling the different neuronal functions in the brain. Expand
Immunocytochemical localization of protein kinase C isozymes in rat brain
The distinct cellular and subcellular distribution of PKC isozymes suggests that each isozyme plays a unique role in the various neural functions. Expand
Calcium/phospholipid-dependent kinase recognizes sites in microtubule-associated protein 2 which are phosphorylated in living brain and are not accessible to other kinases.
3 kinases were chosen because of their abundance in brain and/or proximity to microtubules, and all 3 recognized more sites in the bovine than in the rat MAP-2, suggesting that 20 of these had been inadvertently released by phosphatase during assembly cycles. Expand
Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain.
A 7.5-kDa heat- and acid-stable rat brain protein kinase C (PKC) substrate was purified to near homogeneity by a two-step procedure using DEAE-cellulose and hydroxylapatite column chromatography.Expand
Calcium-sensitive interaction between calmodulin and modified forms of rat brain neurogranin/RC3.
Results indicate that modification of NG to form intramolecular disulfides outside the IQ domain provides an alternative mechanism for regulation of its binding affinity to CaM. Expand
Protein kinase C as a component of a nerve growth factor-sensitive phosphorylation system in PC12 cells.
It is suggested that the binding of nerve growth factor to its receptor on PC12 cells causes an increase in the activity of protein kinase C in the cytosol and phosphorylation of Nsp100 kinase, which in turn lowers its ability to phosphorylate Nsp 100. Expand
Autophosphorylation of rat brain Ca2+-activated and phospholipid-dependent protein kinase.
Findings suggest that autophosphorylation of protein kinase C may be important in the regulation of the enzymic activity subsequent to signal transduction. Expand