School of Medicine
Showing 11-16 of 16 Results
David B. McKay
Professor of Structural Biology, Emeritus
Current Research and Scholarly Interests Three-dimensional structure determination and biophysical studies of macromolecules.
Professor of Structural Biology and of Microbiology and Immunology
Current Research and Scholarly Interests The Parham laboratory investigates the biology, genetics, and evolution of MHC class I molecules and NK cell receptors.
Joseph (Jody) Puglisi
Jauch Professor and Professor of Structural Biology
Current Research and Scholarly Interests The Puglisi group investigates the role of RNA in cellular processes and disease. We investigate dynamics using single-molecule approaches. Our goal is a unified picture of structure, dynamics and function. We are currently focused on the mechanism and regulation of translation, and the role of RNA in viral infections. A long-term goal is to target processes involving RNA with novel therapeutic strategies.
Professor of Molecular and Cellular Physiology, of Structural Biology and of Photon Science
Bio The Skiniotis laboratory seeks to resolve structural and mechanistic questions underlying biological processes that are central to cellular physiology. Our investigations employ primarily cryo-electron microscopy (cryoEM) and 3D reconstruction techniques complemented by biochemistry, biophysics and simulation methods to obtain a dynamic view into the macromolecular complexes carrying out these processes. The main theme in the lab is the structural biology of cell surface receptors that mediate intracellular signaling and communication. Our current main focus is the exploration of the mechanisms responsible for transmembrane signal instigation in cytokine receptors and G protein coupled receptor (GPCR) complexes.
Professor of Photon Science and of Structural Biology
Bio Soichi Wakatsuki is a Professor of Photon Science at the SLAC National Accelerator Laboratory where he recently initiated the Biociences Division, and Professor of Structural Biology, Stanford School of Medicine. He received his B.S and M.S. degrees in Chemical Engineering from University of Tokyo, and his Ph.D. degree in Chemistry from Stanford University in 1991. After postdoctoral studies on time-resolved x-ray crystallography of enzyme reactions in Oxford (1990 to 1994), he moved to Grenoble, France in 1994 to work at the European Synchrotron Radiation Facility (ESRF) where he led Joint Structural Biology Group to develop high-brilliance x-ray crystallography beamlines and instruments, as well as several structural biology projects on protein transport. In 2000, Soichi moved back to Japan to start a new Structural Biology Research Center at KEK (High Energy Accelerator Research Organization), Tsukuba, Japan, and later served as Director of Photon Factory (national synchrotron radiation facility) from 2006 to 2012. There he further developed x-ray beamlines and a large scale protein crystallization system, led initiatives to start three national projects on structural proteomics. Fascinated by new research opportunities in integrative bioimaging at Stanford and the world’s first hard x-ray free electron laser (XFEL) at SLAC, Soichi returned to Stanford in 2013. Soichi’s research interests include structural biology of post-translational modification and vesicle transport, structural biology of polyubiquitin recognition, synchrotron radiation and XFEL instrumentation, protein crystallography and small angle X-ray scattering, integrative multi-scale bioimaging.
William M. Hume Professor in the School of Medicine, Professor of Structural Biology, of Molecular and Cellular Physiology and of Photon Science
Current Research and Scholarly Interests Our laboratory studies molecular interactions that underlie the establishment and maintenance of cell and tissue structure. Our specific areas of interest are the architecture and dynamics of intercellular adhesion junctions, the molecular basis of cell polarity, and the Wnt signaling pathway. We also have a long-standing interest in carbohydrate-based cellular recognition and adhesion.