Razvan L.
Cornea
Research Associate Professor
Biochemistry Molecular Biology and Biophysics
Our goal is to understand the structure, function, and dynamics of protein complexes involved in the regulation of intracellular calcium homeostasis, particularly (not exclusively) in striated muscle. Our focus is primarily on the SERCA pump (and its regulator in the heart, phospholamban) and the ryanodine receptor (RyR, and its regulatory partners, FKBP, calmodulin, S100A1).
Research statement
Our goal is to understand the structure, function, and dynamics of protein complexes involved in the regulation of intracellular calcium homeostasis, particularly (not exclusively) in striated muscle. Our focus is primarily on the SERCA pump (and its regulator in the heart, phospholamban) and the ryanodine receptor (RyR, and its regulatory partners, FKBP, calmodulin, S100A1).
We translate our understanding of the structure-function correlations within the SERCA and RyR complexes into a program for therapeutic discovery to address a variety of diseases characterized by dysregulated intracellular calcium (sarcopenia, muscular dystrophy, heart failure, diabetes, Alzheimer's, and Parkinson's).
Selected publications
- Rebbeck R.T., Essawy, M.M., Nitu F.R., Grant, B.D., Gillispie, G.D., Thomas D.D., Bers D.M., Cornea R.L. (2016) High-Throughput Screens to Discover Small-Molecule Modulators of Ryanodine Receptor Calcium Release Channels. J Biomol Screen. DOI: 10.1177/1087057116674312.
- Uchinoumi, H., Yang, Y., Oda, T., Li, N., Alsina, K.M., Puglisi, J.L., Chen-Izu, Y., Cornea, R.L., Wehrens, X.H.T., Bers, D.M. (2016) CaMKII-dependent phosphorylation of RyR2 promotes targetable pathological RyR2 conformational shift. J Mol Cel Cardiol. 98, 62-72.
- Rebbeck R.T., Nitu F.R., Rohde D., Most P., Bers D.M., Thomas D.D., Cornea R.L. (2016). FRET-Based Selective Detection Of RyR-binding Reveals CaM Binding to RyRs Independent of S100A1. J. Biol. Chem., 291, 15896-907.
- Yuchi, Z., Wong. S.M., Lau, K., Underhill, A., Cornea, R.L., Fessenden, J.D., and Van Petegem, F., (2015) Crystal structures of Ryanodine Receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant. Nat Commun. 6, 7947.
- Svensson, B., Oda, T., Nitu, F.R., Yang, Y., Cornea, I., Chen-Izu, Y., Fessenden, J.D., Bers, D.M., Thomas, D.D., and Cornea, R.L. (2014). FRET-Based Trilateration of Probes Bound within Functional Ryanodine Receptors. Biophys.J. 107(9), 2037-48.
- Cornea, R.L., Gruber, S.J., Lockamy, E.L., Muretta, J.M., Jin, D., Chen, J., Dahl, R., Bartfai, T., Zsebo, K.M., Gillispie, G.D., and Thomas, D.D. (2013) High-Throughput FRET Assay Yields Allosteric SERCA Activators. J Biomol Screen. 18, 96-106.