Selective Regulation of Neurite Extension and Synapse Formation by the β but not the α Isoform of CaMKII
By Charles C Fink, K. Bayer, J. Myers, J. Ferrell, H. Schulman, T. Meyer. 2003
311 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/41d23e9a0a56c3974068cfc0adbecfc1de02396f
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In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- Calmodulin-Kinases: Modulators of Neuronal Development and Plasticity (2008, unknown): “…(Okamoto et al., 2007) or blocked by transfection of the full-length CaMKIIN (Wayman et al., 2004) or treatment with membrane-permeable peptides (Fink et al., 2003; Sanhueza et al., 2007; Yang et al., 2004) derived from either CaMKIIN (Chang et al., 1998) or the autoinhibitory domain of CaMKII…”
- NF-κB functions in synaptic signaling and behavior (2003, background): “In contrast, inhibiting Ca 2+ -calmodulin dependent kinases (CaMKs) with KN-62, a general CaMK inhibitor, or a potent and specific peptide inhibitor of CaMKI”
- Control of Dendritic Arborization by the Phosphoinositide-3′-Kinase–Akt–Mammalian Target of Rapamycin Pathway (2005, background): “…dendritic shape are protein kinases, such as calcium calmodulin-dependent protein (CaM) kinases II and IV (Wu and Cline, 1998; Redmond et al., 2002; Fink et al., 2003), mitogen-activated protein (MAP) kinases (Fukuda et al., 1995), Rho-associated coiled-coil-forming protein kinase (Nakayama et…”