Michael Stowell
Associate Professor of Molecular, Cellular and Developmental Biology
303-735-2983
michael.stowell@colorado.edu
Personal Website
Education
- Ph.D., Chemical Engineering, California Institute of Technology, 1997
Research Interests
- Ion channel structure and mechanism
- Synaptic architecture, dynamics, and plasticity
- Alzheimer's Disease
- Formation and mechanisms of supramolecular assemblies
Our research is focused on molecular and supramolecular structures that facilitate communication between neurons at the chemical synapse and how such structures are perturbed in neurological disease. We are particularly interested in the architectural arrangement of signaling molecules and enzymes, and characterizing the ways in which such molecular assemblies are formed and undergo changes during synaptic transmission and modulation. Our approach is to investigate individual proteins using x-ray and electron crystallographic methods and to combine this information with EM images obtained via 3-D reconstruction of supramolecular assemblies and tomographic analysis of the intact chemical synapse. Our long-term goal is to construct a dynamic molecular and architectural map for the chemical synapse that will help to understand synaptic formation, transmission and plasticity.
Selected Publications
- GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Marks, B, Stowell, MH, Vallis, Y, Mills, IG, Gibson, A, Hopkins, CR, and McMahon, HT Nature, 410(6825):231-5. 2001
- Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Stowell, MH, Marks, B, Wigge, P, and McMahon, HT Nat Cell Biol, 1(1):27-32. 1999
- Macromolecular structure determination by electron microscopy: new advances and recent results. Stowell, MH, Miyazawa, A, and Unwin, N Curr Opin Struct Biol, 8(5):595-600. 1998
- Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Stowell, MH, McPhillips, TM, Rees, DC, Soltis, SM, Abresch, E, and Feher, G Science, 276(5313):812-6. 1997
- Uncompetitive substrate inhibition and noncompetitive inhibition by 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-nonyl-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo3 complex: implications for a Q(H2)-loop proton translocation mechanism. Musser, SM, Stowell, MH, Lee, HK, Rumbley, JN, and Chan, SI Biochemistry, 36(4):894-902. 1997