Associated Papers
A hyper-activatable CAMK2A variant associated with intellectual disability causes exaggerated long-term potentiation and learning impairments.
Pan M et al.
Translational Psychiatry, 2025
Molecular basis of interactions between CaMKII and α-actinin-2 that underlie dendritic spine enlargement.
Curtis AJ et al.
Elife, 2023
Förster resonance energy transfer-based kinase mutation phenotyping reveals an aberrant facilitation of Ca2+/calmodulin-dependent CaMKIIα activity in de novo mutations related to intellectual disability.
Fujii H et al.
Frontiers in Molecular Neuroscience, 2022
The intellectual disability-associated CAMK2G p.Arg292Pro mutation acts as a pathogenic gain-of-function.
Proietti Onori M et al.
Human Mutation, 2018
Activated CaMKIIα Binds to the mGlu5 Metabotropic Glutamate Receptor and Modulates Calcium Mobilization.
Marks CR et al.
Molecular Pharmacology, 2018
Differential stimulus-dependent synaptic recruitment of CaMKIIα by intracellular determinants of GluN2B.
She K et al.
Molecular and Cellular Neurosciences, 2012
Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation.
Rellos P et al.
Plos Biology, 2010
Select a paper to view details