The Baird laboratory employs a broad range of biophysico-chemical methods to investigate the structure and molecular mechanisms of cell surface receptors that operate in immunological and other responses. How are complex cellular responses controlled in time and space? Our biophysical characterization is carried out in conjunction with extensive measurements of cellular activities to determine the features critical for the initiation and regulation of signal transduction. A particular area of interest is the role of cellular membranes in targeting these responses. Many of our current studies focus on signaling pathways initiated by the receptor (FceRI) for immunoglobulin E (IgE) that plays a central role in allergic and inflammatory responses and serves as a model for other types of immune receptors. We apply similar methods to other receptors, currently including growth factor receptors involved in cancer. The goal of our integrated studies is to elucidate complex biological systems on a molecular level; the information obtained also has important biomedical applications in drug design and clinical therapies.
[ A complete list of publications can be found on the Baird-Holowka Group webpage]
Veatch, S., E. Chiang, P. Sengupta, D. Holowka and B. Baird. 2012. Quantitative Nano-Scale Analysis of IgE-FcεRI Clustering and Coupling to Early Signaling Proteins. J. Phys. Chem. B. 116(23): 6923-6935.
Veatch, S.L., B.B. Machta, S.A. Shelby, E.N. Chiang, D.A. Holowka and B.A. Baird. 2012. Correlation Functions Quantify Super-resolution Images and Estimate Apparent Clustering Due to Over-counting. PLoS One 7(2): e31457.
Bryant, K.L., M.A. Antonyak, R.A. Cerione, B. Baird and D. Holowka. 2013. Mutations in the Polybasic Juxtamembrane Sequence of Both Plasma Membrane- and Endoplasmic Reticulum-localized Epidermal Growth Factor Receptors Confer Ligand-independent Cell Transformation. J. Biol. Chem. 288(48): 34930-34942.
Shelby, S.A., D. Holowka, B. Baird and S.L. Veatch. 2013. Distinct Stages of Stimulated FcεRI Receptor Clustering and Immobilization Are Identified through Superresolution Imaging. Biophys. J. 105(10): 2343-2354.
Welch, M. Elizabeth, N.L. Ritzert, H. Chen, N.L. Smith, M.E. Tague, Y. Xu, B.A. Baird, H.D. Abruña and C.K. Ober. 2014. Generalized Platform for Antibody Detection using the Antibody Catalyzed Water Oxidation Pathway. J. Am. Chem. Soc. 136(5): 1879-1883.
Chylek, L.A., D.A. Holowka, B.A. Baird and W.S. Hlavacek. 2014. An interaction library for the FcεRI signaling network. Front. Immunol. 5: 172.
Wilkes, M.M., J.D. Wilson, B. Baird and D. Holowka. 2014. Activation of Cdc42 is Necessary for Sustained Oscillations of Ca2+ and PIP2 Stimulated by Antigen in RBL Mast Cells. Biology Open 3(8): 700-710.
Kelly, C.V., D.L. Wakefield, D.A. Holowka, H.G. Craighead and B.A. Baird. 2014. Near-Field Fluorescence Cross-Correlation Spectroscopy on Planar Membrane. ACS Nano 8(7): 7392-7404.
Holowka, D. and B. Baird. 2015. Nanodomains in Early and Later Phases of FcεRI Signaling. Essays in Biochemistry: Membrane Nanodomains; Vol. 57, pp. 147-163.
Singhai, A., D.L. Wakefield, K.L. Bryant, S.R. Hammes, D. Holowka and B. Baird. 2015. Spatially Defined EGF Receptor Activation Reveals an F-Actin-Dependent Phospho-Erk Signaling Complex. Biophys. J. 107(11): 2639-2651.