Michael Piazza

Michael Piazza
University of Waterloo | UWaterloo · Department of Chemistry

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15
Publications
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135
Citations

Publications

Publications (15)
Article
Full-text available
Hematopoietic adaptor containing SH3 and SAM domains-1 (HACS1) is a signaling protein with two juxtaposed protein–protein interaction domains and an intrinsically unstructured region that spans half the sequence. Here, we describe the interaction between the HACS1 SH3 domain and a sequence near the third immunoreceptor tyrosine-based inhibition mot...
Article
NMR spectroscopy allows for the determination of high resolution structures, as well as being an efficient method for studying the dynamics of protein-protein and protein-peptide complexes. 15N relaxation and H/D exchange experiments allow for the analysis of these structural dynamics at a residue specific level. Calmodulin (CaM) is a small cytosol...
Article
Full-text available
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 as pacemakers of the mammalian brain and heart, lack a C-terminal IQ motif. We illustrate that T-type channels associate with C...
Article
Calmodulin (CaM) is a cytosolic Ca(2+)-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 Ca(2+), joined by a flexible central linker region. CaM is able to bind and activate its target proteins in the Ca(2+)-replete and/or Ca(2+)-deplete forms...
Article
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. CaM binding causes a conformational change in NOS to allow for the electron transfer between the reductase and oxygenase domains t...
Article
Full-text available
Calmodulin (CaM) is a ubiquitous cytosolic Ca(2+)-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 domains contains two EF hand pairs capable of binding to Ca(2+). Upon Ca(2+) binding CaM undergoes a conformational change expos...
Article
The intracellular Ca(2+) concentration is an important regulator of many cellular functions. The small acidic protein Calmodulin (CaM) serves as a Ca(2+) sensor and control element for many enzymes. Nitric oxide synthase (NOS) is one of the proteins that is activated by CaM and plays a major role in a number of key physiological and pathological pr...
Article
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 critical for drug development and for our understanding of protein regulation in general. CaM is a small acidic calcium binding pro...
Article
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 (CaM), is required to fully activate the enzyme. The exact mechanism of how CaM activates NOS is not fully understood at this...
Data
. Table of primers for constructions of the human iNOS oxyFMN S562K, C563R and R536E mutants; gel electrophoresis of the purified mutants; UV–vis spectra of the proteins; summary of the processes occurring upon CO photolysis; analysis of the FMN content by HPLC; flavin fluorescence spectra of wt iNOS oxyFMN with added EDTA.
Article
Nitric oxide synthase (NOS) plays a major role in a number of key physiological and pathological processes. Knowledge of how this is regulated is important. The small acidic calcium binding protein, calmodulin (CaM), is required to fully activate the enzyme. The exact mechanism of how CaM activates NOS is not fully understood. Studies have shown Ca...
Article
Full-text available
In the crystal structure of a calmodulin (CaM)-bound FMN domain of human inducible nitric oxide synthase (NOS), the CaM-binding region together with CaM forms a hinge, and pivots on an R536(NOS)/E47(CaM) pair (Xia et al. J Biol Chem 284:30708-30717, 2009). Notably, isoform-specific human inducible NOS S562 and C563 residues form hydrogen bonds with...
Article
Nuclear magnetic resonance (NMR) spectroscopy is an efficient method for studying the dynamics and structures of protein‐ protein and protein‐peptide complexes. Calmodulin (CaM), a ubiquitous Ca 2+ ‐sensing protein, is able to bind and regulate various intracellular proteins, including the nitric oxide synthase (NOS) enzymes. The investigation of C...

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