{"result":[{"lastName":"Boxer","clinicalFocus":[],"appointments":[{"appointment":"Member,Bio-X"}],"primaryAppointment":"Member,Bio-X","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=8050&type=small&showNoImage","displayName":"Steven Boxer","firstName":"Steven","href":"http://med.stanford.edu/profiles/cancer/researcher/Steven_Boxer","researchInterest":""},{"lastName":"Doniach","clinicalFocus":[],"appointments":[{"appointment":"Member,Bio-X"}],"primaryAppointment":"Member,Bio-X","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=8062&type=small&showNoImage","displayName":"Sebastian Doniach","firstName":"Sebastian","href":"http://med.stanford.edu/profiles/cancer/researcher/Sebastian_Doniach","researchInterest":""},{"lastName":"McKay","clinicalFocus":[],"appointments":[{"appointment":"Emeritus Faculty, Acad Council,Structural Biology"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Emeritus Faculty, Acad Council,Structural Biology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4099&type=small&showNoImage","displayName":"David B. McKay","firstName":"David","href":"http://med.stanford.edu/profiles/cancer/researcher/David_McKay","researchInterest":"Three-dimensional structure determination and biophysical studies of macromolecules."},{"lastName":"Levitt","clinicalFocus":[],"appointments":[{"appointment":"Professor,Structural Biology"},{"appointment":"Member,Bio-X"},{"appointment":"Professor (By courtesy),Computer Science"}],"primaryAppointment":"Professor,Structural Biology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4494&type=small&showNoImage","displayName":"Michael Levitt","firstName":"Michael","href":"http://med.stanford.edu/profiles/cancer/researcher/Michael_Levitt","researchInterest":"having pioneered, we (a) predict folding of a polypeptide and RNA chains into a unique native-structure, we (b) model protein structure using the well-established paradigms that similar protein sequences imply similar three-dimensional structures, and (c) we are focusing on mesoscale modeling of large macromolecular complexes such as RNA polymerase and the mammalian chaperonin."},{"lastName":"Saggu","clinicalFocus":[],"appointments":[{"appointment":"Postdoctoral Research fellow, Natural Sciences Cluster"}],"primaryAppointment":"Postdoctoral Research fellow, Natural Sciences Cluster","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=16850&type=small&showNoImage","displayName":"Miguel Saggu","firstName":"Miguel","href":"http://med.stanford.edu/profiles/postdocs/researcher/Miguel_Saggu","researchInterest":""},{"lastName":"Snyder","clinicalFocus":[],"appointments":[{"appointment":"Professor,Genetics"},{"appointment":"Member,Stanford Cancer Institute"},{"appointment":"Member,Child Health Research Institute"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor,Genetics","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=13465&type=small&showNoImage","displayName":"Michael Snyder","firstName":"Michael","href":"http://med.stanford.edu/profiles/cancer/researcher/Michael_Snyder","researchInterest":"We are presently in an omics revolution in which genomes and other omes can be readily characterized. Our laboratory uses a variety of approaches to analyze genomes and regulatory networks. Our research focuses on yeast, an ideal model organism ideally suited to genetic analysis, and humans.\r\n\r\n1) Transcriptomes\r\nTo annotate genomes, we developed RNA sequencing for annotation the yeast and human transcriptomes. We discovered that the eukaryotic transcriptome is much more complex than previously"},{"lastName":"Jardetzky","clinicalFocus":[],"appointments":[{"appointment":"Emeritus Faculty, Acad Council,Chemical and Systems Biology"}],"primaryAppointment":"Emeritus Faculty, Acad Council,Chemical and Systems Biology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4190&type=small&showNoImage","displayName":"Oleg Jardetzky","firstName":"Oleg","href":"http://med.stanford.edu/profiles/cancer/researcher/Oleg_Jardetzky","researchInterest":"Structure, dynamics and function of proteins involved in transport and regulatory processes; high resolution nuclear magnetic resonance studies of conformational transitions and protein folding; study of the mechanism of action of the trp-repressor, ankyrin-domain proteins and the development of programs to calculate protein solution structure"},{"lastName":"Berg","clinicalFocus":[],"appointments":[{"appointment":"Emeritus Faculty, Acad Council,Biochemistry"},{"appointment":"Professor Emeritus,SoM Dean's Office Administrative Units - Dean's Office Operations"},{"appointment":"Professor Emeritus,Biochemistry"}],"primaryAppointment":"Emeritus Faculty, Acad Council,Biochemistry","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=6263&type=small&showNoImage","displayName":"Paul Berg","firstName":"Paul","href":"http://med.stanford.edu/profiles/cancer/researcher/Paul_Berg","researchInterest":"For about 10 years until 2000, my lab's research activities were focused on the mechanism of recombinational repair of double-strand breaks in DNA. We focused our efforts on two model systems:  one involved the repair of restriction enzyme cleavages at specific mammalian chromosomal loci and the second explored the biochemical properties of purified yeast Rad51 protein, an essential catalyst for synapsing the broken ends of DNA with an intact homologue of that sequence.  We also explored the ro"},{"lastName":"Puglisi","clinicalFocus":[],"appointments":[{"appointment":"Professor,Structural Biology"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor,Structural Biology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4431&type=small&showNoImage","displayName":"Joseph (Jody) Puglisi","firstName":"Joseph","href":"http://med.stanford.edu/profiles/cancer/researcher/Joseph_Puglisi","researchInterest":"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."},{"lastName":"Cherry","clinicalFocus":[],"appointments":[{"appointment":"Professor (Research),Genetics"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor (Research),Genetics","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4249&type=small&showNoImage","displayName":"Mike Cherry","firstName":"J. Michael","href":"http://med.stanford.edu/profiles/cancer/researcher/J. Michael_Cherry","researchInterest":"My research involves identifying, validating and integrating scientific facts into encyclopedic databases essential for research and scientific education.  Published results of scientific experimentation are a foundation of our understanding of the natural world and provide motivation for new experiments.  The combination of in-depth understanding reported in the literature with computational analyses is an essential ingredient of modern biological research."},{"lastName":"Solomon","clinicalFocus":[],"appointments":[{"appointment":"Professor,Natural Sciences Cluster - Chemistry"},{"appointment":"Member,Bio-X"},{"appointment":"Professor,Photon Science Directorate"}],"primaryAppointment":"Professor,Natural Sciences Cluster - Chemistry","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=8081&type=small&showNoImage","displayName":"Edward I. Solomon","firstName":"Edward","href":"http://med.stanford.edu/profiles/cancer/researcher/Edward_Solomon","researchInterest":"Professor Solomon\u0092s research is in the fields of Physical-Inorganic, Bioinorganic, and Theoretical-Inorganic Chemistry. His focus is on spectroscopic elucidation of the electronic structure of transition metal complexes and its contribution to reactivity.  He has made significant contributions to our understanding of metal sites involved in electron transfer, copper sites involved in O2 binding, activation and reduction to water, and in structure/function correlations over non-heme iron enzymes."},{"lastName":"Block","clinicalFocus":[],"appointments":[{"appointment":"Professor,Natural Sciences Cluster - Applied Physics"},{"appointment":"Professor,Biology (School of Humanities and Sciences)"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor,Natural Sciences Cluster - Applied Physics","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=6209&type=small&showNoImage","displayName":"Steven M. Block","firstName":"Steven","href":"http://med.stanford.edu/profiles/cancer/researcher/Steven_Block","researchInterest":""},{"lastName":"Yanofsky","clinicalFocus":[],"appointments":[{"appointment":"Professor Emeritus,Biology (School of Humanities and Sciences)"}],"primaryAppointment":"Professor Emeritus,Biology (School of Humanities and Sciences)","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=6252&type=small&showNoImage","displayName":"Charles Yanofsky","firstName":"Charles","href":"http://med.stanford.edu/profiles/cancer/researcher/Charles_Yanofsky","researchInterest":""},{"lastName":"Gherardini","clinicalFocus":[],"appointments":[{"appointment":"Postdoctoral Research fellow, Microbiology & Immunology"}],"primaryAppointment":"Postdoctoral Research fellow, Microbiology & Immunology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=35679&type=small&showNoImage","displayName":"Pier Federico Gherardini","firstName":"Pier Federico","href":"http://med.stanford.edu/profiles/postdocs/researcher/Pier Federico_Gherardini","researchInterest":""},{"lastName":"Baldwin","clinicalFocus":[],"appointments":[{"appointment":"Emeritus Faculty, Acad Council,Biochemistry"}],"primaryAppointment":"Emeritus Faculty, Acad Council,Biochemistry","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=6816&type=small&showNoImage","displayName":"Robert Baldwin","firstName":"Robert","href":"http://med.stanford.edu/profiles/cancer/researcher/Robert_Baldwin","researchInterest":"I closed my laboratory when I retired in 1998.  I continue to do research, chiefly in collaboration with Franc Avbelj, on problems of protein folding energetics, especially peptide backbone solvation,  and to write reviews."},{"lastName":"Zaugg","clinicalFocus":[],"appointments":[{"appointment":"Postdoctoral Research fellow, Biochemistry"}],"primaryAppointment":"Postdoctoral Research fellow, Biochemistry","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=33764&type=small&showNoImage","displayName":"Judith Zaugg","firstName":"Judith","href":"http://med.stanford.edu/profiles/postdocs/researcher/Judith_Zaugg","researchInterest":""},{"lastName":"Spudich","clinicalFocus":[],"appointments":[{"appointment":"Professor,Biochemistry"},{"appointment":"Member,Bio-X"},{"appointment":"Member,Stanford Cancer Institute"}],"primaryAppointment":"Professor,Biochemistry","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4609&type=small&showNoImage","displayName":"James Spudich","firstName":"James","href":"http://med.stanford.edu/profiles/cancer/researcher/James_Spudich","researchInterest":"The general research interest of this laboratory is the molecular basis of cell motility. We have three specific research interests, the molecular basis of energy transduction that leads to ATP-driven myosin movement on actin, the biochemical basis of the regulation of actin and myosin interaction and their assembly states, and the roles these proteins play in vivo, in cell movement and changes in cell shape."},{"lastName":"Feng","clinicalFocus":[],"appointments":[{"appointment":"Assistant Professor,Molecular & Cellular Physiology"}],"primaryAppointment":"Assistant Professor,Molecular & Cellular Physiology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=35054&type=small&showNoImage","displayName":"Liang Feng","firstName":"Liang","href":"http://med.stanford.edu/profiles/cancer/researcher/Liang_Feng","researchInterest":"We are interested in the structure, dynamics and function of eukaryotic transport proteins mediating ions and major nutrients crossing the membrane, the kinetics and regulation of transport processes, the catalytic mechanism of membrane embedded enzymes and the development of small molecule modulators based on the structure and function of membrane proteins."},{"lastName":"Pringle","clinicalFocus":[],"appointments":[{"appointment":"Professor,Genetics"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor,Genetics","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=7022&type=small&showNoImage","displayName":"John R. Pringle","firstName":"John","href":"http://med.stanford.edu/profiles/cancer/researcher/John_Pringle","researchInterest":"Much of our research exploits the power of yeast as an experimentally tractable model eukaryote to investigate fundamental problems in cell and developmental biology such as the mechanisms of cell polarization and cytokinesis.  In another project, we are developing the small sea anemone Aiptasia as a model system for study of the molecular and cellular biology of dinoflagellate-cnidarian symbiosis, which is critical for the survival of most corals but still very poorly understood."},{"lastName":"Greenleaf","clinicalFocus":[],"appointments":[{"appointment":"Assistant Professor,Genetics"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Assistant Professor,Genetics","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=24604&type=small&showNoImage","displayName":"William Greenleaf","firstName":"William","href":"http://med.stanford.edu/profiles/cancer/researcher/William_Greenleaf","researchInterest":"Our lab focuses on developing methods to probe the genome and epigenome at the single-cell and single-molecule levels. Our efforts are split between building new tools to leverage the power of high-throughput sequencing and cutting-edge microscopies, and bringing these new technologies to bear against basic biological questions of genomic and epigenomic variation."},{"lastName":"Kornberg","clinicalFocus":[],"appointments":[{"appointment":"Professor,Structural Biology"},{"appointment":"Member,Bio-X"}],"primaryAppointment":"Professor,Structural Biology","imageUrl":"http://cancer.stanford.edu/profiles/viewImage?facultyId=4308&type=small&showNoImage","displayName":"Roger Kornberg","firstName":"Roger","href":"http://med.stanford.edu/profiles/cancer/researcher/Roger_Kornberg","researchInterest":"We study the regulation of transcription, the first step in gene expression. The main lines of our work are 1) reconstitution of the process with more than 50 pure proteins and mechanistic analysis, 2) structure determination of the 50 protein complex at atomic resolution, and 3) studies of chromatin remodelling, required for transcription of the DNA template in living cells"}]}