Calmodulin Mouse mAb (clone CaM85) - Citations

Calmodulin Mouse mAb (clone CaM85) - Citations

View additional product information for Calmodulin Mouse mAb (clone CaM85) - Citations (136900)

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Citations & References
Abstract
Calmodulin activation of polo-like kinase 1 is required during mitotic entry.
AuthorsDai G, Qian Y, Chen J, Meng FL, Pan FY, Shen WG, Zhang SZ, Xue B, Li CJ,
Journal
PubMed ID24032677
'Polo-like kinase 1 (Plk1) is a conserved key regulator of the G2/M transition, but its upstream spatiotemporal regulators remain unknown. With the help of immunofluorescence, co-immunoprecipitation, and glutathione S-transferase (GST) pull-down assay, we found that calmodulin (CaM) is one such regulatory molecule that associates with Plk1 from G2 to metaphase. ... More
Trans-activation Response (TAR) RNA-binding Protein 2 Is a Novel Modulator of Transient Receptor Potential Canonical 4 (TRPC4) Protein.
AuthorsZimmermann J, Latta L, Beck A, Leidinger P, Fecher-Trost C, Schlenstedt G, Meese E, Wissenbach U, Flockerzi V,
Journal
PubMed ID24563462
TRPC4 proteins function as Ca(2+) conducting, non-selective cation channels in endothelial, smooth muscle, and neuronal cells. To further characterize the roles of TRPC4 in vivo, detailed information about the molecular composition of native channel complexes and their association with cellular signaling networks is needed. Therefore, a mouse brain cDNA library ... More
Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin.
AuthorsLeonard AS, Bayer KU, Merrill MA, Lim IA, Shea MA, Schulman H, Hell JW,
JournalJ Biol Chem
PubMed ID12379661
Ca(2+) influx through the N-methyl-d-aspartate (NMDA)-type glutamate receptor leads to activation and postsynaptic accumulation of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) and ultimately to long term potentiation, which is thought to be the physiological correlate of learning and memory. The NMDA receptor also serves as a CaMKII docking site in dendritic ... More