Prof. Dr. Tamara L. Kinzer-Ursem

Purdue University
Weldon School of Biomedical Engineering
Marta E. Gross Associate Professor

External Senior Fellow (Marie S. Curie FCFP)
September 2021 – December 2021

Last Update: 31.08.2022

Curriculum Vitae

Tamara Kinzer-Ursem is the Marta E. Gross Associate Professor and Associate Head of Academic Programs in the Weldon School of Biomedical Engineering at Purdue University. She received her B.S. degree in Bioengineering from the University of Toledo (USA); M.S. and Ph.D. degrees in Chemical Engineering from the University of Michigan; and Post-Doctoral training at the California Institute of Technology. Research in the Kinzer-Ursem lab employs a unique experimental-theoretical framework to quantitatively measure, analyze and describe biomolecular and cellular behavior for the improvement of human health. Dr. Kinzer-Ursem’s work falls within two areas of expertise: 1) Computational modeling of protein signaling networks; 2) Development of technologies that enable quantitative description of protein function and for characterization and quantification of disease biomarkers in environmental and patient samples.

Dr. Kinzer-Ursem’s work at Purdue University has also included advancing multidisciplinary research initiatives as part of the leadership teams of the Purdue Institute of Integrative Neuroscience (PIIN), Molecular Biophysics Training Program, and Purdue-Eli Lilly Collaborative Research: Connected Health Program. In teaching Dr. Kinzer-Ursem uses innovative methods of instruction to engage students in learning and provides personalized student mentorship to make the highest positive impact on her student’s professional development. She has held leadership roles in the American Institute of Chemical Engineers and Biomedical Engineering Society and is also a member of the Society for Neuroscience and the African International Biotechnology and Biomedical Conference.

Selected Publications

Waller A*, Sutton KL, Kinzer-Ursem TL, Absood A, Traynor JR, Linderman JJ, Omann GM, “Receptor Binding Kinetics and Cellular Responses of Six N-Formyl Peptide Agonists in Human Neutrophils,” Biochemistry (2004) 43: 8204-16, PMID: 15209517 (Tier 1)
Kinzer-Ursem TL*, Sutton KL, Absood A, Waller A, Omann GM, Linderman JJ, “Multiple Receptor States are Required to Describe Both Kinetic Binding and Activation of Neutrophils Via N-Formyl Peptide Receptor Ligand,” Cellular Signaling (2006) 18(10): 1732-47, PMID: 16530386 (Tier 2)
Kulkarni C*, Kinzer-Ursem TL*, Tirrell DA, “Selective Functionalization of the Protein N-Terminus with N-Myristoyl Transferase for Bioconjugation in Cell Lysate,” ChemBioChem (2013) 14(15):1958-62, DOI: 10.1002/cbic.201300453, PMID: 24030852 (Tier 2)
Pepke SL*, Kinzer-Ursem TL*, Mihalas S, Kennedy MB, “A Dynamic Model of Interactions of Ca²⁺, Calmodulin, and Catalytic Subunits of Ca²⁺/Calmodulin-Dependent Protein Kinase II,” Public Library of Science (PLoS) Computational Biology (2010) 6(2):e1000675, DOI: 10.1371/journal.pcbi.1000675, PMID: 20168991 (Tier 1)
Kinzer-Ursem TL*, Linderman JJ, “Ligand- and Cell-Specific Parameters Affect Ligand Efficacy in a Kinetic Model of G Protein Coupled Receptor Signaling,” Public Library of Science (PLoS) Computational Biology (2007) 3(1): e6, PMID: 17222056 (Tier 1)

FRIAS Project

Phosphatase-Dependent Regulation of CaMKII Kinase Activity in Heart Failure

Heart failure affects 26 million people worldwide. A key molecular pathology is disruption of calcium ion (Ca²⁺) homeostasis in cardiac myocytes. Ca2+/calmodulin-dependent kinase II (CaMKII)‐dependent hyperphosphorylation of ryanodine receptors (RyRs) causes depletion of internal Ca²⁺ stores. Both CaMKII and RyRs are regulated by the protein phosphatase PP1. In this multi-disciplinary project, we propose to develop a theoretical-experimental framework to quantify the relative effect of disruptions in the temporal and spatial regulation of CaMKII and PP1 on Ca²⁺ homeostasis in cardiac myocytes. Taking advantage of our complementary expertise in computational biology and kinase/phosphatase regulation, these studies are expected to contribute to development of novel therapeutic strategies that target key molecular mechanisms in heart disease.