Browsing Chemistry by Author "Piazza, Michael"
Now showing items 1-9 of 9
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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 ... -
Chemical shift assignments of calmodulin constructs with EF hand mutations
Piazza, Michael; Guillemette, J. Guy; Dieckmann, Thorsten (Springer, 2016-04-01)Calmodulin (CaM) is a ubiquitous cytosolic Ca2+-binding protein able to bind and regulate hundreds of different proteins. It consists of two globular domains joined by a flexible central linker region. Each one of these ... -
Chemical shift perturbations induced by residue specific mutations of CaM interacting with NOS peptides
Piazza, Michael; Guillemette, J. Guy; Dieckmann, Thorsten (Springer, 2015-10-01)The regulation of nitric oxide synthase (NOS) by calmodulin (CaM) plays a major role in a number of key physiological and pathological processes. A detailed molecular level picture of how this regulation is achieved is ... -
Dynamics of Nitric Oxide Synthase–Calmodulin Interactions at Physiological Calcium Concentrations
Piazza, Michael; Guillemette, J. Guy; Dieckmann, Thorsten (American Chemical Society, 2015-03-24)The intracellular Ca2+ concentration is an important regulator of many cellular functions. The small acidic protein calmodulin (CaM) serves as a Ca2+ sensor and control element for many enzymes. Nitric oxide synthase (NOS) ... -
NMR Studies of Protein and Peptide Structure and Dynamics
Piazza, Michael (University of Waterloo, 2016-04-18)Calmodulin (CaM) is a small, acidic cytosolic calcium binding protein that responds to increases in intracellular Ca2+ concentrations. It is proposed to be involved in binding to and regulating over 300 functionally and ... -
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 ... -
Structural Studies of a Complex Between Endothelial Nitric Oxide Synthase and Calmodulin at Physiological Calcium Concentration
Piazza, Michael; Dieckmann, Thorsten; Guillemette, J. Guy (American Chemical Society, 2016-10-25)The small acidic protein calmodulin (CaM) serves as a Ca2+ sensor and control element for many enzymes including nitric oxide synthase (NOS) enzymes that play major roles in key physiological and pathological processes. ... -
Structure/Function of Calmodulin Mutants bound to target peptides from Nitric Oxide Synthase
Piazza, Michael (University of Waterloo, 2012-01-18)Calmodulin (CaM) is a ubiquitous calcium binding protein that responds to intracellular Ca2+ and is proposed to be involved in the binding of over 300 functionally and structurally diverse proteins. It is a highly conserved ...