Anthony P. Timerman
Professor of Chemistry
Ph.D., Biochemistry, The Ohio State University
B.S., Chemistry, Boise State University
Research and Professional Activities
The general area of my research interest is cellular communication, or cell signalling. That is, my studies deal with the mechanisms by which a cell responds to an applied stimulus. My specific focus in this area is excitation-contraction coupling in muscle . . . the molecular mechanisms by which muscle contraction and relaxation are regulated. Although the basic questions in my research are specifically addressed towards the model of muscle contraction and relaxation, these questions are applicable to other systems. For example, there are numerous health related concerns in which cell signalling mechanisms must be more completely understood. One example that readily comes to mind is the normal growth of a tissue during development vs. the abnormal growth associated with malignant tumors.
The last 2-3 years of my five year postdoctoral research appointment at Vanderbilt University were unusually exciting. In this time period, I made substantial progress in characterizing a poorly understood interaction between two proteins involved in excitation-contraction coupling in skeletal muscle. When I applied the same methodologies to study the analogous function in heart, I discovered a previously uncharacterized protein from heart which appears to be involved in regulating excitation-contraction coupling specifically in heart muscle.
FK506 Binding Protein is Associated with the Calcium Release Channel (Ryanodine Receptor). T. Jayaraman, A-M. Brillantes, A.P. Timerman, S. Fleischer, H. Erdjument-Bromage, P. Tempst, and A.R. Marks. J. Biol. Chem. 267, 9474-9477 (1992). 363 Citations.
The Calcium Release Channel of Sarcoplasmic Reticulum is Modulated by FK-506 Binding Protein: Dissociation and Reconstitution of FKBP-12 to the Calcium Release Channel of Skeletal Muscle Sarcoplasmic Reticulum. A.P. Timerman, E. Ogunbumni, E. Freund, G. Wiederrecht, A.R. Marks, and S. Fleischer. J. Biol. Chem. 268, 22992-22999 (1993). 248 Citations.
Cryo-Electron Microscopy and Three-Dimensional Reconstruction of the Calcium Release Channel/Ryanodine Receptor from Skeletal Muscle. M. Radermacher, V. Rao, R. Grassucci, J. Frank, A.P. Timerman, S. Fleischer, and T. Wagenknecht. J. Cell. Biol. 127, 411-423 (1994). 161 Citations.
Deficiency of Alveolar Fluid Glutathione in Patients with Sepsis and Adult Respiratory Distress Syndrome (ARDS). E.R. Pacht, A.P. Timerman, M.G. Lykens, and A.J. Merola. Chest 100, 1397-1403 (1991). 141 Citations.
Selective Binding of FKBP12.6 by the Cardiac Ryanodine Receptor. Timerman, A.P., Onoue, H., Chen, H-B., Barg, S., Wiederrecht, G., and Fleischer, S. J. Biol. Chem., 271, 20385-20391 (1996). 125 Citations.
Structural and Functional Interaction of FK506 Binding Proteins with the Calcium Release Channels of Heart and Skeletal Muscle Sarcoplasmic Reticulum. A.P. Timerman. Biology Department, Lawrence University. December 6, 1996.
The Role of Immunophilins in Signal Response Coupling. A.P. Timerman. Department of Chemistry, University of Wisconsin-Stevens Point. February, 1996.
Purification and Characterization of an Inositol Polyphosphate Receptor which is similar to Clathrin Assembly Protein AP-2 and Forms K+ Selective Ion Channels in Planar Lipid Bilayers. A.P. Timerman. Chemistry Department Symposium, Boise State University. September, 1992.
American Chemical Society (ACS