Above: Legend for baird_Picture2 Left: Legend for baird_Picture3 |
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.