Robert M. Stroud, PhD

Robert M. Stroud, PhD

Professor, Departments of Biochemistry/Biophysics and Pharmaceutical Chemistry, UCSF

Phone: (415) 476-4224 (office), 514-4179 (asst)
Box 2240, UCSF
San Francisco, CA 94158-2517

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Cancer Center Membership

Program Member ยป Non-aligned


Clare College, U. of Cambridge, U.K., B.A., 1964, Natural Sciences
Clare College, U. of Cambridge, U.K., M.A., 1968, Natural Sciences
Birkbeck College, London University, U.K., Ph.D., 1968, Biological Crystallography

Professional Experience

  • 1973-1975
    Assistant Professor of Chemistry, Cal Tech
  • 1975-1977
    Associate Professor of Chemistry, Cal Tech
  • 1977-1979
    Associate Professor of Biophysics, Department of Biochemistry & Biophysics, UCSF
  • 1977-1979
    Associate Professor, Dept. of Pharmaceutical Chemistry, UCSF
  • 1979-present
    Professor, Department of Biochemistry & Biophysics, UCSF

Honors & Awards

  • 1961-1964
    State Scholar, University of Cambridge, England
  • 1965-1968
    Moulton Trust Fellow, University of London
  • 1972-1977
    National Institutes of Health Career Development Award
  • 1975-1977
    Alfred P. Sloan Foundation Fellow
  • 1984
    DeWitt Stetton Jr. Lecturer of the National Institutes of Health
  • 1988-1989
    President, Biophysical Society of the United States
  • 1988
    Fellow of the Royal Society of Medicine (United Kingdom)
  • 1993-2004
    The Editor, Annual Review of Biophysics and Biomolecular Structure
  • 1997
    Member National Committee for the IUPAB
  • 1998
    Founding Fellow of the Biophysical Society of the United States
  • 2003
    Member of the National Academies of Science (NAS)
  • 2004
    Tenth Annual Lectureship on Applications of Molecular Biology to Biomedical Sciences, Carnegie Mellon University
  • 2005
    The 'Fred Richards' Lecturer at Yale University
  • 2006
    The 'Friedman' Lecturer Rutgers University

Selected Publications

  • Fu, D., Libson, A., Miercke, L., Weitzman, C., Nollert, P., Krucinski, J., and Stroud, R.M. (2000) Science 290, 481-486. The Structure of a Glycerol Conducting Channel Reveals the Basis for its Selectivity.
  • Erlanson, D.A., Braisted, A.C., Raphael, D.R., Randal, M., Stroud, R.M., Gordon, E.M., and Wells, J.A. (2000). Proc. Natl Acad Sci 97, 9367-72. Site-directed Ligand Discovery.
  • Nollert, P., Harries, W.E.C., Fu, D., Miercke, L.J.W., Stroud, R.M. (2001). FEBS Letters 504, 112-7. Atomic Structure of a Glycerol Channel and Implications for Substrate Permeation in Aqua(glyero)porins.
  • Tajkhorshid, E. Nollert, P. Jensen, M.O. Miercke, L.J.W. O'Connell, J. Stroud, R.M. Schulten, K. (2002) Science 296, 525-530. Control of the Selectivity of the Aquaporin Water Channel Family by Global Orientational Tuning
  • Fu D., Libson A., Stroud R. (2002). Novartis Found Symp 245, 51-61. The structure of GlpF, a glycerol conducting channel.
  • Finer-Moore, J. S., Santi, D. V., Stroud, R. M. (2003). Biochemistry 42, 248-256. Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: thymidylate synthase mutagenesis, function, and structure.
  • Stroud, R.M., and Finer-Moore, J.S. (2003). Biochemistry 42, 239-247. Conformational dynamics along an enzymatic reaction pathway: thymidylate synthase, "the Movie"
  • Stroud, R.M., Miercke, L.J.W., O'Connell, J., Khademi, S., Lee, J. K., Remis, J., Harries, W., Robles, Y., and Akhavan, D. (2003). Curr Opin Struct Biol 13, 424-431. Glycerol facilitator GlpF and the aquaporin family of channels
  • Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J.W., O'Connell, J.D.3rd., Khosla, C., and Stroud, R.M. Structure 11, 147-154. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA: ACP transacylase
  • Pan, H. Agarwalla, S., Moustakas, D.T., Finer-Moore, J.S., and Stroud, R.M. (2003) Proc Nat. Acad. Sci 100, 12648-12653. Crystal Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA-protein recognition through a combination of rigid docking and induced fit
  • Lee, T. L., Agarwalla S., and Stroud, R.M. (2003) Structure 12, 397-407. The first structure of an RNA 5-methyluridine methyltransferase contains an iron-sulfur cluster
  • Savage, D. F., Egea, P.F., Robles, Y.C., O'Connell III, J.D., and Stroud, R.M. (2003) PLoS Biology 1, 334-340. [with Journal Cover, and Synopsis 1 302.] Architecture and selectivity in aquaporins: 2.5A X-ray structure of aquaporin Z
  • O'Neil R.H., Lilien R.H., Donald B.R., Stroud R.M., Anderson A.C. (2003). J Biol Chem 278, 52980-52987. Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase.
  • Stroud R.M., Savage D., Miercke L.J., Lee J.K., Khademi S., Harries W. (2003). FEBS Lett 555, 79-84. Selectivity and conductance among the glycerol and water conducting aquaporin family of channels.
  • Agarwalla, S., Stroud, RM., Gaffney B.J. (2004). J Biol Chem 279, 34123-34129. Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies.
  • Foster P.G., Nunes C.R., Greene P., Moustakas D., Stroud R.M. (2003). Structure (Camb) 11, 1609-1620. The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.
  • Keatinge-Clay A.T., Shelat A.A., Savage D.F., Tsai S.C., Miercke L.J., O'Connell, J., Khosla, C., and Stroud, R.M. (2003). Structure (Camb) 11, 147-154. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase.
  • Lee J.K., Khademi S., Harries W., Savage D., Miercke L., Stroud R.M. (2004). J Synchrotron Radiat 11, 86-88. Water and glycerol permeation through the glycerol channel GlpF and the aquaporin family.
  • Egea, P.F., Shan, S.O., Napetschnig, J., Savage, D.F., Walter, P., and Stroud, R.M. (2004) Nature 426, 215-221. Substrate twinning activates the signal recognition particle and its receptor
  • Stroud R.M., Wells J.A. (2004). Science STKE 2004, re7. May 4th. Mechanistic diversity of cytokine receptor signaling across cell membranes.
  • Harries, W.E.C., Akhavan, D., Miercke, L.J.W., Khademi, S., Stroud, R.M. (2004) Proc Nat Acad Sci 101, 14045-14050. The Channel Architecture of Aquaporin 0 At 2.2-A Resolution.
  • Khademi, S., O'Connell III, J., Remis, J., Robles-Colmenares, Y., Miercke L.J.W., Stroud, R.M. (2004) Science 305, 1587-1594. [Cover Article, with Perspective by Knepper and Agre. p1573-1574] Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.
  • Keatinge-Clay, A. T., Maltby, D. A., Medzihradszky, K. F., Khosla, C., Stroud, R. M. (2004) Nat Struct Mol Biol 11, 888-893. An antibiotic factory caught in action.
  • Laporte S.L., Forsyth C.M., Cunningham B.C., Miercke L.J., Akhavan D., Stroud R.M. (2005) Proc Natl Acad Sci 102, 1889-94. De novo design of an IL-4 antagonist and its structure at 1.9 A.
  • Lee T.T, Agarwalla S, Stroud R.M. (2005) Cell 120, 599-611. A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function.
  • Egea P.F, Stroud R.M, Walter P. (2005) Curr Opin Struct Biol. 15, 213-20. Targeting proteins to membranes: structure of the signal recognition particle.
  • Credle, J.J., Finer-Moore, J.S., Papa, F.R., Stroud, R.M. and Walter, P. (2005) Proc Nat Acad Sci 102, 18773-18773-18784 On the Mechanism of Sensing Unfolded Protein in the Endoplasmic Reticulum.
  • Lee, J.K., Kozono, D. Remis, J., Kitagawa, Y., Agre, P., Stroud, R.M. (2005) Proc. Nat Acad Sci 102, 18932-7. Structural Basis for Conductance by the Archaeal Aquaporin AqpM at 1.68 A
  • Keatinge-Clay, A. T. and Stroud, R. M. (2006) Structure 14, 737-748. The Structure of a Ketoreductase Determines the Organization of the beta-Carbon Processing Enzymes of Modular Polyketide Synthases