@article{db0969e2f8ff4e99b27c9f0e581ae9bc,
title = "Chapter 12: Molecular and cellular studies on brain calcium/calmodulin-dependent protein kinase II",
abstract = "This chapter discusses brain CaM-kinase II with a particular focus on its unique regulatory properties, its regulation in cultured brain cells, and its physiological functions. CaM-kinase II has widespread tissue distribution as oligomeric isozyme forms and is particularly abundant in the brain. In certain regions of the brain, such as hippocampus, it constitutes up to 2\% of total protein, which probably makes it the most abundant enzyme in these tissues. CaM-kinase II is localized presynaptically where it is involved in Ca2+-dependent regulation of neurotransmitter biosynthesis and exocytosis. At excitatory synapses in forebrain, there is a thickening of the postsynaptic membrane called the postsynaptic density (PSD), and CaM-kinase II constitutes about 30–50\% of the protein in the PSD. These excitatory synapses are subject to a usage-dependent enhancement of synaptic transmission called long-term potentiation (LTP)—a popular model for learning and memory.",
author = "Soderling, \{T. R.\} and K. Fukunaga and Brickey, \{D. A.\} and Fong, \{Y. L.\} and Rich, \{D. P.\} and K. Smith and Colbran, \{R. J.\}",
year = "1991",
month = jan,
day = "1",
doi = "10.1016/S0079-6123(08)61722-7",
language = "English (US)",
volume = "89",
pages = "169--183",
journal = "Progress in Brain Research",
issn = "0079-6123",
publisher = "Elsevier B.V.",
number = "C",
}