Browsing Chemistry by Author "Taiakina, Valentina"
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Calmodulin as a universal regulator of voltage gated calcium channels
Taiakina, Valentina (University of Waterloo, 2014-05-22)Calmodulin (CaM) is a ubiquitous calcium-binding protein responsible for the binding and activation of a vast number of enzymes and signaling pathways. It contains two lobes that bind two calcium ions each, separated by a ... -
Calmodulin regulates Cav3 T-type channels at their gating brake
Chemin, Jean; Taiakina, Valentina; Monteil, Arnaud; Piazza, Michael; Guan, Wendy; Stephens, Robert F.; Kitmitto, Ashraf; Pang, Zhiping P.; Dolphin, Annette C.; Perez-Reyes, Edward; Dieckmann, Thorsten; Guillemette, J. Guy; Spafford, J. David (American Society for Biochemistry and Molecular Biology, 2017-12-08)Calcium (Cav1 and Cav2) and sodium channels possess homologous CaM-binding motifs, known as IQ motifs in their C termini, which associate with calmodulin (CaM), a universal calcium sensor. Cav3 T-type channels, which serve ... -
Solution Structure of Calmodulin Bound to the Target Peptide of Endothelial Nitric Oxide Synthase Phosphorylated at Thr495
Piazza, Michael; Taiakina, Valentina; Guillemette, Simon R.; Guillemette, J. Guy; Dieckmann, Thorsten (American Chemical Society, 2014-03-04)Nitric oxide synthase (NOS) plays a major role in a number of key physiological and pathological processes, and it is important to understand how this enzyme is regulated. The small acidic calcium binding protein, calmodulin ... -
Structural Consequences of Calmodulin EF Hand Mutations
Piazza, Michael; Taiakina, Valentina; Dieckmann, Thorsten; Guillemette, J. Guy (American Chemical Society, 2017-02-21)Calmodulin (CaM) is a cytosolic Ca2+-binding protein that serves as a control element for many enzymes. It consists of two globular domains, each containing two EF hand pairs capable of binding Ca2+, joined by a flexible ...