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| Barbara A. Baird |
| Title: |
Horace White Professor of Chemistry and Chemical Biology and Chair |
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| Office: |
660 Spencer T. Olin Laboratory |
Phone:
(outside the University
preceded by 1-607-25) |
5-4095 or 5-4175 |
| Email: |
bab13@cornell.edu |
| Educational Background: |
PhD, Cornell University, 1979
BS, Knox College, 1973
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Awards:
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• Fellow of the American Academy of Arts and Sciences
• Postdoctoral Fellow of Damon Runyon-Walter Winchell Cancer Fund (at the National Institutes of Health)
• Harold Lamport Award for Biophysics and Physiology, New York Academy of Sciences
• National Science Foundation Women in Science and Engineering Faculty Award
• Fellow of the John Simon Guggenheim Memorial Foundation
• Fellow of the American Association for the Advancement of Science (Sections of Chemistry and Biology)
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Research Description:
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Mechanisms of Receptor Mediated Cell Activation
Basic molecular mechanisms of cell surface receptors that mediate transmembrane signals can be elucidated by integrating information from multiple interdisciplinary approaches.
Many of our studies focus on the receptor (FcεRI) for immunoglobulin E (IgE) that plays a central role in the allergic immune response and serves as a model for other types of immune receptors. Binding and cross-linking of IgE-FcεRI complexes by antigen initiates transmembrane signal transduction resulting in cell activation and release of chemical mediators.
We measure kinetics and thermodynamics of binding and cross-linking between cell-bound IgE and structurally defined ligands with fluorescence methods. Analysis with realistic theoretical models and correlation with biological activities enable us to determine features of ligand-receptor interactions that are critical for signaling.
Quantitative fluorescence microscopy, including imaging, fluorescence resonance energy transfer, and fluorescence correlation spectroscopy, is used to monitor changes in the distribution and dynamics of the receptor and signaling components (and genetically engineered analogs) that accompany receptor cross-linking and cellular activation.
Using biochemical and biophysical approaches we found that IgE receptor-mediated signaling involves plasma membrane domains containing cholesterol and ordered lipids (also known as "lipid rafts") that enable regulation and targeting of the signaling components. Collaborative studies apply mass spectrometry, electron spin resonance, electron microscopy, and other powerful analytical methods to investigate the composition, structure and dynamics of the participating membrane components.
Dynamic cellular structures and organization are related to stimulated cellular activities such as phosphorylation of proteins and lipids, Ca2+ mobilization, membrane trafficking, and degranulation, that are measured in parallel.
Together with these other approaches, we are developing nanofabrication technology to probe immunological systems on subcellular and molecular scales.
Detailed descriptions of individual projects can be found on our group webpage: http://www.chem.cornell.edu/bab13/index.html |
Selected Publications:
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Wu, M., D. Holowka, H.G. Craighead and B. Baird. 2004. Visualization of plasma membrane compartmentalization with patterned plasma membrane bilayers. Proc. Natl. Acad. Sci. USA 101:13798-13803.
Young, R.M., X. Zheng, D. Holowka and B. Baird. 2005. Reconstitution of Regulated phosphorylation of FcεRI by a lipid raft-excluded protein tyrosine phosphatase. J. Biol. Chem. 280:1230-1235.
Hammond, A.T., T. Baumgart, A.K Smith, D. Holowka, B. Baird and G.W. Feigenson. 2005. Crosslinking a lipid raft component triggers raft-like phases in model plasma membranes. Proc. Natl. Acad. Sci. USA 102:6320-6325.
Gosse, J.A., A. Wagenknecht-Wiesner, D. Holowka and B. Baird. 2005. Transmembrane sequences are determinants of immunoreceptor signaling. J. Immunol. 175:2123-2131.
Holowka, D., J.A. Gosse, A.T. Hammond, X. Han, P. Sengupta, N.L. Smith, A. Wagenknecht-Wiesner, M. Wu, R.M. Young and B. Baird. 2005. Lipid segretion and IgE receptor signaling: a decade of progress. Biophys. Biochim. Acta. 1746:252-259.
Larson, D.R, J.A. Gosse, D. Holowka, B. Baird and W.W. Webb. 2005. Temporally Resolved Interactions Between Antigen-Stimulated IgE Receptors and Lyn Kinase on Living Cells Revealed by Fluorescence Cross-correlation Spectroscopy. J. Cell. Biol. 171:527-536.
Senaratne, W., P. Sengupta, V. Jakubek, D. Holowka, C.K. Ober and B. Baird. 2006. Self-assembled monolayer functionalized surface arrays for investigating immune cell signaling. J. Am. Chem. Soc. 128:5594-5595.
Swamy, M.J., L. Ciani, M. Ge, D. Holowka, B. Baird and J.H. Freed. 2006. Coexisting domains in the plasma membranes of live cells characterized by spin label ESR Spectroscopy. Biophys. J. 90:4452-4465.
Burns, A., P. Sengupta, T. Zedayko, B. Baird and U. Wiesner. 2006. Core-Shell Fluorescent Silica Nanoparticles for Chemical Sensing: Towards Single Particle Laboratories. Small 2:723-726.
Sengupta, P., D. Holowka and B. Baird. 2007. Fluorescence Resonance Energy Transfer Between Lipid Probes Detects Nanoscopic Heterogeneity in the Plasma Membrane of Live Cells. Biophys. J. 92:3564-3574.
Moran-Mirabal, J.M., A.J. Torres, K.T. Samiee, B.A. Baird and H.G. Craighead. 2007. Cell investigation of nanostructures: Zero-Mode Waveguides for plasma membrane studies with single molecule resolution. Nanotechnology 18: 195101-195111.
Sil, D., J.B. Lee, D. Luo, D. Holowka and B. Baird. 2007. Trivalent ligands with rigid DNA spacers reveal structural requirements for IgE receptor signaling in RBL mast cells. ACS Chemical Biology 2:674-684.
A full list of publications can be found here http://www.chem.cornell.edu/bab13/Publications.html
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