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This laboratory's main focus is on the molecular basis of synaptic plasticity. Current research centers on CaMKII, a calcium-regulated protein kinase and its role as a synaptic frequency detector in determining the direction of long-term changes in synaptic strength. The laboratory also studies the cellular redistribution of CaMKII in response to calcium transients and under conditions of calcium overload, processes likely to affect the availability of the enzyme for synaptic modification. A related project concerns the molecular architecture and activity-dependent modification of the postsynaptic density, a structure that anchors and organizes neurotransmitter receptors and signal transduction molecules at the receiving end of the synapse.
Adjunct Scientist Ayse Dosemeci
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Education:
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| 1985 |
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Ph.D. Biochemistry, University of London, U.K. |
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| 1979 |
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M.S. Biological Sciences, Middle East Technical, Ankara, Turkey |
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| 1976 |
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B.S. Chemistry, Middle East Technical University, Ankara, Turkey |
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Recent Publications:
Dosemeci, A., J.-H. Tao-Cheng, L. Vinade, C.A. Winters, L. Pozzo-Miller, and T.S. Reese. 2001. Glutamate-induced transient modification of the postsynaptic density. Proc. Natl. Acad. Sci. USA 98: 10,428-10,432.
Tao-Cheng, J.-H., L. Vinade, C. Smith, C.A. Winters, R. Ward, M.W. Brightman, T.S. Reese, and A. Dosemeci. 2001. Sustained elevation of calcium induces transient Ca2+/calmodulin-dependent protein kinase II clusters in neurons. Neuroscience 106: 69-78.
Vinade, L., J.D. Petersen, K. Do, A. Dosemeci, and T.S. Reese. 2001. Activation of calpain may alter the postsynaptic density structure and modulate anchoring of NMDA receptors. Synapse 40: 302-309.
Dosemeci, A. and C. Choi. 1997. Ca2+- independent autophosphorylation of Postsynaptic Density-Associated Ca2+/ calmodulin-dependent protein kinase. Neurochem. Res., 22:1151-1157.
Dosemeci, A. and R. W. Albers. 1996. A mechanism for synaptic frequency detection through autophosphorylation of CaM Kinase II. Biophys. J., 70:2493-2501. |
