agard@msg.ucsf.edu
(415) 476-2521 (voice)
(415) 476-1902 (fax)

Box 2240, UCSF; San Francisco, CA 94143-2240

Yale University, New Haven, B.S., 1975, Molec. Biol. and Biophysics
California Institute of Technology, Pasadena, Ph.D., 1980, Biological Chemistry
University of California, San Francisco, Postdoctoral, 1980
MRC Laboratory, Cambridge, England, Postdoctoral, 1981-82

Marshall, W.F., Straight, A., Marko, J.F., Swedlow, J., Dernburg, A., Belmont, A., Murray, A.W., Agard, D.A., Sedat, J.W. (1997). Dynamics of nuclear architecture: interphase chromosomes undergo large-scale diffusional motion in living cells. Current Biology. 7:930-939.

Han, K.F., Sedat, J.W., and Agard, D.A. (1997). Practical image restoration of thick biological specimens using multiple focus levels in transmission electron microscopy. J. Struct. Biol. 120:237-244.

Fung, J.C., Marshall, W.F., Dernburg, A., Agard, D.A., Sedat, J.W. (1998). Homologous Chromosome Pairing in Drosophila Melanogaster Proceeds through Multiple Independent Initiations. J. Cell Biol. 141:5-20.

Gustafsson, M.G.L., Agard, D.A., Sedat, J.W. (1998). I5M:3D widefield light microscopy with better than 100nnm axial resolution. Journal of Microscopy 195:10-16.

Shiau, A., Barstad,D., Loria,P.M., Cheng,L., Kushner,P.J., Agard,D.A., and Greene, G.L. (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by taxoxifen. Cell 95(7):927-37.

Jinnai, H., Nishikawa, Y., Spontak, R.J., Smith, S.D., Agard, D.A., and Hashimoto, T. (1999). Direct Measurement of Interfacial Curvature Distributions in a Bicontinuous Block Copolymer. Phys. Rev. Lett. 84(3):518-21.

Gustafsson, M.G.L., Agard, D.A., Sedat, J.W. (2000). Doubling the Lateral Resolution of Wide-field Fluorescence Microscopy using Structured Illumination. Proc. SPIE 3919:141-150.

Marshall, W.F., Marko, J.F., Agard, D.A., Sedat, J.W. (2001). Chromosome Elasticity and Mitotic Polar Ejection Force Measured in Living Drosophila Embryos by Four-Dimensional Microscopy-Based Motion Analysis. Current Biology 11:569-578.

Moritz, M., Braunfeld, M.B., Guenebaut, V., Heuser, J., and Agard, D.A. (2000). Structure of the γ-tubulin ring complex: a template for microtubule nucleation. Nature Cell Biology 2:365-370

Moritz, M., Braunfeld, M.B., Alberts, B.M., Agard, D.A. (2001). Reconstitution of Centrosome Microtubule Nucleation in Drosophila. In Methods in Cell Biology 67:141-148.

Moritz, M. and D.A. Agard. 2001. γ-Tubulin Complexes and Microtubule Nucleation. Current Opinion in Structural Biology 11(2):174-81.

Kam, Z., Hanser, B., Gustafsson, M.G.L., Agard, D.A., and Sedat, J.W. (2001). Computational Adaptive Optics for Live Three-Dimensional Imaging. Proc. of the Natl Academy of Sciences 28:3790-3795.

Ota, N. and Agard, D.A. (2001). Binding Mode Prediction for a Flexible Ligand in a Flexible Pocket using Multi-Conformation Simulated Annealing Pseudo Crystallographic Refinement. Journal of Molecular Biology 314(3):617-627.

Kushner, P.J., Agard, D.A., Greene, G.L., Scanlan, T.S., Shiau, A.K., Uht, R.M., and Webb, P. (2000). Estrogen Receptor Pathways to AP-1. J. Steriod Biochem Mol. Biol. 74(5):311-7.

Shiau, A.K., Barstad, D., Radek, J.T., Meyers, M.J., Katzenellenbogen, B.S., Katzenellenbogen, J.A., Agard, D.A., and Greene, G.L. (2002). Structural Characterization of a Subtype-Selective Ligand Reveals a Novel Mode of Estrogen Receptor Antagonism. Nature Structural Biology 9(5):359-364.

Wille, H., Michelitsch, M.M., Guenebaut, V., Supattapone, S., Serban, A., Cohen, F.E., Agard, D.A., Prusiner, S.B. (2001). Structural Studies of the Scrapie Prion Protein by Electron Crystallography. Proc. Natl. Acad. Sci. 6:3563-3568.

Rice, L.M. and Agard, D.A. (2002). Centriole duplication: centrin in on answers? Current Biology 12(18):R618-9

Hanser, B.M., Gustafsson, M.G.L., Agard, D.A., and Sedat, J.W. (2003). Phase retrieval for high-numerical-aperture optical systems. Optics Letters Vol. 28, No. 10, 801-803.

Zheng, Q.S., Braunfeld, M.B., Sedat, J.W., and Agard, D.A. (2004). An improved stategy for automated electron microscopic tomography. J. Struct. Biol., 147(2):91-101.

Harris, S.F., Shiau, A.K., and Agard, D.A. (2004). The Crystal Structure of the Carboxy-Terminal Dimerization Domain of htpG, the Escherichia coli Hsp90, Reveals a Potential Substrate Binding Site. Structure 12(6):1087-1097.

Hanser, B.M., Gustafsson, M.G., Agard, D.A., Sedat, J.W. (2004). Phase-retrieved pupil functions in wide-field fluorescence microscopy. J. Microsc. Oct;216(Part 1):32-48

Fuhrmann, C.N., Waddling, C., Ota, N., Shipley, K.M., Agard, D.A. (2003). Sub-angstrom resolution crystal structure of lpha-lytic protease provide novel insight into the mechanisms of protein stability and proteolytic catalysis. Accepted with revisions, Journal of Molecular Biology

Fuhrmann, C.N., Kelch, B.A., Ota, N., Agard, D.A. (2004). The 0.83 resolution crystal structure of lpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain. J. Mo. Biol., 338(5):999-1013.

Zheng, Q.S., Braunfeld, M.B., Sedat, J.W., Agard, D.A. (2004). An improved strategy for automated electron microscopic tomography. J. Struct. Biol., 147(2):91-101.

Harris, S.F., Shiau, A.K., Agard, D.A. (2004). The Crystal Structure of the Carboxy-Terminal Dimerization Domain of htpG, the Escherichia coli Hsp90, Reveals a Potential Substrate Binding Site. Structure, 12(6):1087-1097.

3/15/05