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Thomas C. Squier, Ph.D.

Expertise

Tom Squier
Tom Squier

Dr. Squier's research centers on aging and cardiac muscles and is sponsored by the National Institutes of Health. In a current 4-year study, Dr. Squier is working to identify the structural changes involving calmodulin during aging. These changes modify the ability to activate target proteins and alter turnover and repair mechanisms. He also conducts research on single-protein dynamics of target binding by calmodulin, regulatory mechanisms of secretory phospholipases A2, and structural analogs of s-adenosylmethionine. Dr. Squier has held a variety of academic appointments and currently serves at Washington State University as an adjunct professor of biology.

Education

Awards and Honors

Selected Publications

Chen B, MU Mayer, and TC Squier. 2005. "Structural uncoupling between opposing domains of oxidized calmodulin underlies enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase." Biochemistry 44, 4737-4747.

Mayer MU, L Shi, and TC Squier. 2005. "One-step, non-denaturing isolation of an RNA Polymerase core enzyme complex using an improved multi-affinity probe resin." Molecular Biosystems, DOI: 10.1039/b500950b (published online April 14, 2005).

Bigelow DJ and TC Squier. 2005. "Redox Modulation of Cellular Signaling and Metabolism Through Reversible Oxidation of Methionine Sensors in Calcium Regulatory Proteins." Biochim.et. Biophys. Acta. 1703(2):121-134.

Chen, B, MU Mayer, LM Markille, DL Stenoien, and TC Squier. 2005. "Calcium activation induces dynamic stabilization of amino-terminal domain elements of calmodulin." Biochemistry 44(3):905-914.

Nauser T, ME Jacoby, WH Koppenol, TC Squier, and C Schoneich. 2005. "Calmodulin Methionine Residues are Targets For One-Electron Oxidation by Hydroxyl Radicals: Formation of SN bonded Radical Complexes." Chemical Communications 5:587-589.

Contact Information

Thomas.Squier@pnl.gov