Recommended Readings: David Julius, Ph.D. Friday February 8, 2019

Friday Lectures

Friday, February 8, 2019  3:45 p.m

Caspary Auditorium

David Julius Ph.D.

Morris Herzstein Chair in Molecular Biology and Medicine

Professor and Chair of Physiology

University of California

Natural Products as Probes of the Pain Pathway: From Physiology to Atomic Structure

Recommended Readings:

Empirical Articles

Gao, Yuan; Cao, Erhu; Julius, David; et al. (2016). TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. NATURE. 534 (7607): 347-+

Paulsen, Candice E.; Armache, Jean-Paul; Gao, Yuan; et al. (2015). Structure of the TRPA1 ion channel suggests regulatory mechanisms. NATURE. 520 (7548): 511-+

Liao, Maofu; Cao, Erhu; Julius, David; et al. (2013). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. NATURE. 504 (7478): 107-+

Cavanaugh, Daniel J.; Chesler, Alexander T.; Jackson, Alexander C.; et al. (2011). Trpv1 Reporter Mice Reveal Highly Restricted Brain Distribution and Functional Expression in Arteriolar Smooth Muscle Cells. JOURNAL OF NEUROSCIENCE. 31 (13): 5067-5077

Cordero-Morales, Julio F.; Gracheva, Elena O.; Julius, David. (2011). Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli. PNAS. 108 (46): E1184-E1191

Cavanaugh, Daniel J.; Chesler, Alexander T.; Braz, Joao M.; et al. (2011). Restriction of Transient Receptor Potential Vanilloid-1 to the Peptidergic Subset of Primary Afferent Neurons Follows Its Developmental Downregulation in Nonpeptidergic Neurons. JOURNAL OF NEUROSCIENCE. 31 (28): 10119-10127

Review Papers

Bohlen, Christopher J.; Julius, David (2012). Receptor-targeting mechanisms of pain-causing toxins: How ow? TOXICON. 60 (3): 254-264

Basbaum, Allan I.; Bautista, Diana M.; Scherrer, Gregory; et al. (2009). Cellular and Molecular Mechanisms of Pain. CELL. 139 (2): 267-284

Book Chapter

Julius, David. (2013). TRP Channels and Pain. ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY. 29: 355-384

 

Recommended Readings: Lingyin Li, Ph.D., February 25

Special Lecture
Wednesday, February 25, 2015
4:00 p.m., Carson Family Auditorium (CRC)

Lingyin Li, Ph.D.,
Merck Fellow of the Jane Coffins Child Memorial Fund,
Department of Systems Biology,
Harvard Medical School

Chemical Biology of Anti-Cancer Innate Immunity

Recommended Readings

Kim, S., Li, L., Maliga, Z., Yin, Q., Wu, H., & Mitchison, T. J. (2013). Anticancer flavonoids are mouse-selective STING agonists. ACS Chemical Biology, 8(7), 1396–1401. doi:10.1021/cb400264n

Li, L., Yin, Q., Kuss, P., Maliga, Z., Wu, H., & Mitchison, T. J. (2014). Hydrolysis of 2′3′-cGAMP by ENPP1 and design of nonhydrolyzable analogs. Nature Chemical Biology, 10(12), 1043–1048. doi:10.1038/nchembio.1661

Recommended Readings: Andrew Kruse Ph.D. March 3

SPECIAL SEMINAR
Monday, March 3, 2014
4:00 p.m., Carson Family Auditorium

Andrew Kruse, Ph.D.
Department of Molecular and Cellular Physiology
Stanford University School of Medicine

Structural insights into G protein-coupled receptor activation and allosteric modulation

Recommended Readings:

Empirical Papers

Haga, K., Kruse, A. C., Asada, H., Yurugi-Kobayashi, T., Shiroishi, M., Zhang, C., … Kobayashi, T. (2012). Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. Nature, 482(7386), 547–551. doi:10.1038/nature10753

Kruse, A. C., Hu, J., Pan, A. C., Arlow, D. H., Rosenbaum, D. M., Rosemond, E., … Kobilka, B. K. (2012). Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature, 482(7386), 552–556. doi:10.1038/nature10867

Kruse, A. C., Ring, A. M., Manglik, A., Hu, J., Hu, K., Eitel, K., … Kobilka, B. K. (2013). Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature, 504(7478), 101–106. doi:10.1038/nature12735

Kruse, A. C., Weiss, D. R., Rossi, M., Hu, J., Hu, K., Eitel, K., … Shoichet, B. K. (2013). Muscarinic receptors as model targets and antitargets for structure-based ligand discovery. Molecular Pharmacology, 84(4), 528–540. doi:10.1124/mol.113.087551

Ring, A. M., Manglik, A., Kruse, A. C., Enos, M. D., Weis, W. I., Garcia, K. C., & Kobilka, B. K. (2013). Adrenaline-activated structure of β2-adrenoceptor stabilized by an engineered nanobody. Nature, 502(7472), 575–579. doi:10.1038/nature12572

Review Articles

Kruse, A. C., Li, J., Hu, J., Kobilka, B. K., & Wess, J. (2013). Novel insights into M3 muscarinic acetylcholine receptor physiology and structure. Journal of Molecular Neuroscience. doi:10.1007/s12031-013-0127-0

Kruse, A. C., Manglik, A., Kobilka, B. K., & Weis, W. I. (2013). Applications of molecular replacement to G protein-coupled receptors. Acta Crystallographica. Section D, Biological Crystallography, 69(11), 2287–2292. doi:10.1107/S090744491301322X

Recommended Readings: Kevan Shokat, Ph.D.

Friday Lecture Series

The William H. Stein Memorial Lecture

A New Druggable Pocket on K-Ras and a Neo-substrate for Activating the Kinase

PINK in Parkinson’s Disease

Kevan Shokat, Ph.D., professor and chair, department of cellular and molecular

pharmacology, University of California, San Francisco;

investigator, Howard Hughes Medical Institute

November 22, 2013

3:45 p.m.-5:00 p.m. (Refreshments, 3:15 p.m., Abby Lounge)

Caspary Auditorium

Recommended Readings

Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013). A neo-substrate that amplifies catalytic activity of parkinson’s-disease- related kinase PINK1. Cell, 154(4), 737-747

Larochelle, S., Amat, R., Glover-Cutter, K., Sansó, M., Zhang, C., Allen, J. J., . . . Fisher, R. P. (2012). Cyclin-dependent kinase control of the initiation-to-elongation switch of polymerase II. Nature Structural and Molecular Biology, 19(11), 1108-1115

Soskis, M. J., Ho, H. -. H., Bloodgood, B. L., Robichaux, M. A., Malik, A. N., Ataman, B., . . . Greenberg, M. E. (2012). A chemical genetic approach reveals distinct EphB signaling mechanisms during brain development. Nature Neuroscience, 15(12), 1645-1654

Statsuk, A. V., & Shokat, K. M. (2012). Covalent cross-linking of kinases with their corresponding peptide substrates. Methods in Molecular Biology 795 , pp. 179-190

Sun, Y., Miao, Y., Yamane, Y., Zhang, C., Shokat, K. M., Takematsu, H., . . . Drubin, D. G. (2012). Orm protein phosphoregulation mediates transient sphingolipid biosynthesis response to heat stress via the pkh-ypk and Cdc55-PP2A pathways. Molecular Biology of the Cell, 23(12), 2388-2398

Ultanir, S., Hertz, N., Li, G., Ge, W. -., Burlingame, A., Pleasure, S., . . . Jan, Y. -. (2012). Chemical genetic identification of NDR1/2 kinase substrates AAK1 and Rabin8 uncovers their roles in dendrite arborization and spine development. Neuron, 73(6), 1127-1142