Barbara A. Baird



Above: Legend for baird_Picture2
Left: Legend for baird_Picture3
Current Position
Professor of Chemistry, Cornell University

Graduate Education
Ph.D. in Chemistry, Cornell University

Postdoctoral Experience
Walter Winchell Postdoctoral Fellowship at the National Institutes of Health

Honors and Awards
Professor Baird has been a visiting scientist at Stanford University, Los Alamos National Laboratory, Becton Dickinson Monoclonal Center, and Immunex Research and Development Corporation. She received the Harold Lamport Award for Biophysics and Physiology from the New York Academy of Sciences, a Faculty Award for Women in Science and Engineering from the National Science Foundation, and a Fellowship from the John Simon Guggenheim Memorial Foundation.



Selected Publications
Holowka, D. and B. Baird: Antigen Binding, Crosslinking, and IgE Receptor Aggregation: A Window on Cell Surface Dynamics. Annual Reviews of Biophysics and Biomolecular Structure Invited (manuscript in preparation), 1996.

Field, K.A., D. Holowka and B. Baird: IgE receptor-mediated recruitment of p53/56lyn to detergent-resistent membrane domains accompanies cellular signaling. Submitted for publication.

Hashemi, B.B., J.P. Slattery, D. Holowka and B. Baird: T Cell Recptor-Mediated Ca2+ Responses are Governed by Dynamic Aggregation of Receptors. Submitted for publication.

Posner, R.G., K. Subramanian, J. Thomas, T. Feder, D. Holowka, B. Baird and B. Goldstein: Simultaneous crosslinking by two non-triggering bivalent ligands causes synergistic signaling of IgE-FceRI complexes. Submitted for publication.

Chang, E.-Y., S.-Y. Mao, H. Metzger, D. Holowka and B. Baird: Effects of subunit mutation on the rotational dynamics of FceRI, the high affinity receptor for IgE, in transfected cells. Biochemistry In press.

Chang, E.-Y., Y. Zheng, D. Holowka and B. Baird: Alteration of lipid composition modulates FceRI signaling in RBL-2H3 Cells. Biochemistry, 34: 4376-4384, 1995.

Thomas, J.L., D. Holowka, B. Baird and W.W. Webb: Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J. Cell Biol. 125: 795-802, 1994.

Baird, B., Y. Zheng and D. Holowka: Structural mapping of IgE-FceRI, an immuno-receptor complex. Accts Chem. Res. 26: 428-434, 1993.

Weetall, M., D. Holowka, and B. Baird: Heterologous desensitization of FceRI on RBL Cells. J. Immunol. 150: 4072-4083, 1993.

Marano, N., M. Liotta, J.P. Slattery, D. Holowka, and B. Baird: FceRI and the T cell receptor for antigen activate similar signaling pathways in T cell - RBL cell hybrids. Cellular Signalling 5: 155-167, 1993.

Posner, R.G., B. Lee, D.H. Conrad, D. Holowka, B. Baird, and B. Goldstein: Aggregation of IgE-receptor complexes on rat basophilic leukemia cells does not change the intrinsic affinity but can alter the kinetics of the ligand-IgE interaction, Biochemistry. 31: 5350-5356, 1992.

Zheng, Y., B. Shopes, D. Holowka, and B. Baird: Dynamic conformations compared for IgE and IgG1 in solution and bound to receptors, Biochemistry. 31: 7446-7456, 1992.

Holowka, D. and B. Baird: Recent evidence for common signalling mechanisms among immunoreceptors that recognize foreign antigens, Cellular Signalling 4: 339-349, 1992.

Myers, J., D. Holowka, and B. Baird: Rotational motion of monomeric and dimeric immunoglobulin E-receptor complexes, Biochemistry 31: 567-575, 1992.

Zheng, Y., B. Shopes, D. Holowka, and B. Baird: Conformation of IgE bound to receptor and in solution, Biochemistry 30: 9125-9131, 1991.

Labrecque, G., D. Holowka, and B. Baird: Characterization of increased K+ permeability associated with the stimulation of receptors for immunoglobulin E on rat basophilic cells, J. Biol. Chem. 266: 14912-14917, 1991.

Keegan, A., C. Fratazzi, B. Shopes, B. Baird, and D. Conrad: Characterization of monoclonal rat anti-mouse IgE antibodies and their use to map the site on mouse IgE that interacts with FceRI and FceRII, Molec. Immunol., 28: 1149-1154, 1991.

Erickson, J., R.G. Posner, B. Goldstein, D. Holowka, and B. Baird: Bivalent ligand dissociation kinetics from receptor-bound immunoglobulin E: Evidence for a time dependent increase in ligand rebinding at the cell surface, Biochemistry 30: 2357-2363, 1991.

Posner, R., J. Erickson, D. Holowka, B. Baird, and B. Goldstein: Dissociation kinetics of bivalent hapten - immunoglobulin E aggregates in solution, Biochemistry 30: 2348-2356, 1991.

Erickson, J., R. Posner, B. Goldstein, D. Holowka and B. Baird: Analysis of ligand binding and crosslinking of receptor in solution and on cell surfaces: immunoglobulin E as a model system. In Biophysical and Biochemical Aspects of Fluorescence Spectroscopy (Ed. T.G. Dewey) Plenum Press, New York. 169-195, 1991.

Weetall, M. B. Shopes, D. Holowka, and B. Baird: Mapping the site of interaction between murine IgE and its high affinity receptor with chimeric immunoglobulins, J. Immunol. 145: 3849-3854, 1990.

Shopes, B., M. Weetall, D. Holowka, and B. Baird: Recombinant human IgG1-murine IgE chimeric immunoglobulins: Construction, expression, and binding to human FcgRI and FcgRII, J. Immunol. 145: 3842-3848, 1990.

Narasimhan, V., D. Holowka, and B. Baird: Microfilaments regulate the rate of exocytosis in rat basophilic leukemia cells, Biochem. Biophys. Res. Comm. 171: 222-229, 1990.

Holowka, D. and B. Baird: Structure and function of the high affinity receptor for immunoglobulin E. In Cellular and Molecular Mechanisms of Inflammation: Receptors of Inflammatory Cells, C.C. Cochrane and M. Gimbrone, eds., Academic Press, Inc., Orlando, FL. 173-197, 1990.

Holowka, D., T. Wensel, and B. Baird: A nanosecond fluorescence depolarization study on the segmental flexibility of receptor-bound IgE. Biochemistry 29: 4607-4612, 1990.

Narasimhan, V., D. Holowka, and B. Baird: A guanine nucleotide-binding protein participates in IgE receptor-mediated activation of endogenous and reconstituted phospholipase A2 in a permeabilized cell system. J. Biol. Chem. 264: 1459-1464, 1990.

Kane, P., D. Holowka and B. Baird: Characterization of model antigens composed of biotinylated haptens bound to avidin. Immunol. Invest. 19: 1-25, 1990.

Goldstein, B., R. Posner, D. Torney, J. Erickson, D. Holowka and B. Baird: Competition between solution and cell surface receptors for ligand: the dissociation of hapten bound to surface antibody in the presence of solution antibody. Biophys. J. 56: 955-966, 1989.

Hammes, S., D. Holowka and B. Baird: Proteolytic digestion of the ß and g subunits of the receptor for immunoglobulin E at the cytoplasmic face of the plasma membrane. J. Receptor Res. 9: 235-238, 1989.

Marano, N., D. Holowka and B. Baird: Bivalent binding of an anti-CD3 antibody to Jurkat cells induces association of the T cell receptor complex with the cytoskeleton. J. Immunol. 143: 931-938, 1989.

Baird, B., R.J. Shopes, V.T. Oi, J. Erickson, P. Kane and D. Holowka: Structural interactions of IgE and its high affinity receptor on the cell surface. Int. Arch. Allergy Appl. Immunol. 88: 23-28, 1989.

Labrecque, G., D. Holowka and B. Baird: Antigen-triggered membrane potential changes in IgE-sensitized rat basophilic leukemia cells: evidence for a repolarization response that is important in the stimulation of cellular degranulation. J. Immunol. 142: 236-243, 1989.

Narasimhan, V., D. Holowka, C. Fewtrell and B. Baird: Cholera toxin increases the rate of antigen-stimulated calcium influx in rat basophilic leukemia cells. J. Biol. Chem. 263: 19626-19632, 1988.

Kane, P., D. Holowka and B. Baird: Crosslinking of IgE-receptor complexes by rigid bivalent antigens >200 Å in length triggers cellular degranulation. J. Cell Biol. 107: 969-980, 1988.

Baird, B., J. Erickson, B. Goldstein, P. Kane, A. Menon, D. Robertson and D. Holowka: Progress toward understanding the molecular details and consequences of IgE-receptor crosslinking. In Theoretical Immunology (Ed. A. Perelson) Addison-Wesley, Reading, MA., 1988. Part 1, pp. 41-59.

Ryan, T., J. Myers, D. Holowka, B. Baird and W.W. Webb: Molecular Crowding on the Cell Surface. Science 239: 61-64, 1988.

Baird, B. and D. Holowka: Structural mapping of membrane-associated complexes by resonance energy transfer: a case study of the IgE-receptor complex. In Spectroscopic Membrane Probes (Ed. L. Loew) CRC Press Inc., Boca Raton, 1988, pp. 93-116.

Erickson, J., B. Goldstein, D. Holowka and B. Baird: The Effect of Receptor Density on the Forward Rate Constant for Binding of Ligands to Cell Surface Receptors. Biophys. J. 52: 657-662, 1987.

Estes K, L. Monfalcone, S. Hammes, D. Holowka and B. Baird: Membrane-bound IgE receptor complexes fused with RBL cells mediate degranulation. J. Cell Biol. 105: 747-755, 1987.

Erickson, J., P. Kane, B. Goldstein, D. Holowka and B. Baird: Crosslinking of IgE-receptor complexes at the cell surface: a fluorescence method for studying the binding of monovalent and bivalent haptens to IgE. Molec. Immunol., 23: 769-780, 1986.

Kane, P., J. Erickson, C. Fewtrell, B. Baird and D. Holowka: Crosslinking of IgE-receptor complexes at the cell surface: structural requirements of bivalent haptens for the triggering of mast cells and tumor basophils. Molec. Immunol., 23: 783-790, 1986.

Robertson, D., D. Holowka and B. Baird: Crosslinking of immunoglobulin E - receptor complexes induces their interaction with the cytoskeleton of rat basophilic leukemia cells. J. Immunol. 136: 4565-4572, 1986.

Menon, A. K., D. Holowka, W. W. Webb, and B. Baird: Crosslinking of receptor-bound immunoglobulin E to aggregates larger than dimers leads to rapid immobilization. J. Cell Biol., 102: 541-550, 1986.

Menon, A. K., D. Holowka, W. W. Webb, and B. Baird: Clustering, mobility, and triggering activity of small oligomers of IgE on rat basophilic leukemia cells. J. Cell Biol., 102: 534-540, 1986.

Slattery, J., D. Holowka, and B. Baird: Segmental flexibility of receptor-bound immunoglobulin E. Biochemistry, 24: 7810-7820, 1985.

Holowka, D., D. A. Conrad, and B. Baird: Structural mapping of membrane-bound immunoglobulin E-receptor complexes: use of monoclonal anti-IgE antibodies to probe the conformation of receptor-bound IgE. Biochemistry 24: 6260-6267, 1985.

Baird, B. and D. Holowka: Structural mapping of Fc-receptor-bound immunoglobulin E: proximity to the membrane surface of the antibody combining site and another site in the Fab segments. Biochemistry 24: 6252-6259, 1985.

Holowka, D. and B. Baird: Lactoperoxidase-catalyzed iodination of the receptor for immunoglobulin E at the cytoplasmic side of the plasma membrane. J. Biol. Chem. 259: 3720-3728, 1984.

Menon, A. K., D. Holowka, and B. Baird: Small oligomers of immunoglobulin E (IgE) cause large scale clustering of IgE receptors on the surface of rat basophilic leukemia cells. J. Cell Biol. 98: 577-583, 1984.

Baird, B., D. Sajewski, and S. Mazlin: A microtiter plate assay using cellulose acetate filters for measuring cellular 3H-serotonin release. J. Immunol. Meth. 64: 365-375, 1983.

Holowka, D. and B. Baird: Structural studies on the membrane-bound immunoglobulin E (IgE)-receptor complex. 2. Mapping of distances between sites on IgE and the membrane surface. Biochemistry 22: 3475-3484, 1983.

Holowka, D. and B. Baird: Structural studies on the membrane-bound immunoglobulin E-receptor complex. 1. Characterization of large plasma membrane vesicles from rat basophilic leukemia cells and insertion of amphipathic fluorescent probes. Biochemistry 22: 3466-3474, 1983.




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