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Coauthors
Raymond Pauszek III Department of Integrative Structural & Computational Biology, the Scripps Research Institute, USA
1 protocol

Jeffrey Liu Department of Integrative Structural & Computational Biology, the Scripps Research Institute, USA
1 protocol

Rajan Lamichhane Department of Integrative Structural & Computational Biology, the Scripps Research Institute, USA
1 protocol

David P. Millar
  • 1 Author merit

Education

Ph.D in Chemistry, California Institute of Technology, 1982

Current position

Professor, Department of Integrative Structural & Computational Biology, The Scripps Research Institute, La Jolla CA USA

Publications (since 2005)

  1. Lamichhane, R., Hammond, J. A., Pauszek, R. F., 3rd, Anderson, R. M., Pedron, I., van der Schans, E., Williamson, J. R. and Millar, D. P. (2017). A DEAD-box protein acts through RNA to promote HIV-1 Rev-RRE assembly. Nucleic Acids Res 45(8): 4632-4641.
  2. Hammond, J. A., Lamichhane, R., Millar, D. P. and Williamson, J. R. (2017). A DEAD-Box Helicase Mediates an RNA Structural Transition in the HIV-1 Rev Response Element. J Mol Biol 429(5): 697-714.
  3. Lamichhane, R., Mukherjee, S., Smolin, N., Pauszek, R. F., 3rd, Bradley, M., Sastri, J., Robia, S. L., Millar, D. and Campbell, E. M. (2017). Dynamic conformational changes in the rhesus TRIM5alpha dimer dictate the potency of HIV-1 restriction. Virology 500: 161-168.
  4. Lavergne, T., Lamichhane, R., Malyshev, D. A., Li, Z., Li, L., Sperling, E., Williamson, J. R., Millar, D. P. and Romesberg, F. E. (2016). FRET Characterization of Complex Conformational Changes in a Large 16S Ribosomal RNA Fragment Site-Specifically Labeled Using Unnatural Base Pairs. ACS Chem Biol 11(5): 1347-1353.
  5. Lamichhane, R., Liu, J. J., Pljevaljcic, G., White, K. L., van der Schans, E., Katritch, V., Stevens, R. C., Wuthrich, K. and Millar, D. P. (2015). Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor beta2AR. Proc Natl Acad Sci U S A 112(46): 14254-14259.
  6. Lamichhane, R., Berezhna, S. Y., Gill, J. P., Van der Schans, E. and Millar, D. P. (2013). Dynamics of site switching in DNA polymerase. J Am Chem Soc 135(12): 4735-4742.
  7. Ridgeway, W. K., Millar, D. P. and Williamson, J. R. (2013). Vectorized data acquisition and fast triple-correlation integrals for Fluorescence Triple Correlation Spectroscopy. Comput Phys Commun 184(4): 1322-1332.
  8. Pljevaljcic, G., Robertson-Anderson, R., van der Schans, E. and Millar, D. (2012). Analysis of RNA folding and ribonucleoprotein assembly by single-molecule fluorescence spectroscopy. Methods Mol Biol 875: 271-295.
  9. Ridgeway, W. K., Millar, D. P. and Williamson, J. R. (2012). Quantitation of ten 30S ribosomal assembly intermediates using fluorescence triple correlation spectroscopy. Proc Natl Acad Sci U S A 109(34): 13614-13619.
  10. Berezhna, S. Y., Gill, J. P., Lamichhane, R. and Millar, D. P. (2012). Single-molecule Forster resonance energy transfer reveals an innate fidelity checkpoint in DNA polymerase I. J Am Chem Soc 134(27): 11261-11268.
  11. Hoffmann, D., Schwarck, D., Banning, C., Brenner, M., Mariyanna, L., Krepstakies, M., Schindler, M., Millar, D. P. and Hauber, J. (2012). Formation of trans-activation competent HIV-1 Rev:RRE complexes requires the recruitment of multiple protein activation domains. PLoS One 7(6): e38305.
  12. Ridgeway, W. K., Millar, D. P. and Williamson, J. R. (2012). The spectroscopic basis of fluorescence triple correlation spectroscopy. J Phys Chem B 116(6): 1908-1919.
  13. Robertson-Anderson, R. M., Wang, J., Edgcomb, S. P., Carmel, A. B., Williamson, J. R. and Millar, D. P. (2011). Single-molecule studies reveal that DEAD box protein DDX1 promotes oligomerization of HIV-1 Rev on the Rev response element. J Mol Biol 410(5): 959-971.
  14. Scholes, C. A., Millar, D. P., Gee, M. L. and Smith, T. A. (2011). Resonance energy-transfer studies of the conformational change on the adsorption of oligonucleotides to a silica interface. J Phys Chem B 115(19): 6329-6339.
  15. Gill, J. P., Wang, J. and Millar, D. P. (2011). DNA polymerase activity at the single-molecule level. Biochem Soc Trans 39(2): 595-599.
  16. Shi, X., Mollova, E. T., Pljevaljcic, G., Millar, D. P. and Herschlag, D. (2009). Probing the dynamics of the P1 helix within the Tetrahymena group I intron. J Am Chem Soc 131(27): 9571-9578.
  17. Tahmassebi, D. C. and Millar, D. P. (2009). Fluorophore-quencher pair for monitoring protein motion. Biochem Biophys Res Commun 380(2): 277-280.
  18. Pond, S. J., Ridgeway, W. K., Robertson, R., Wang, J. and Millar, D. P. (2009). HIV-1 Rev protein assembles on viral RNA one molecule at a time. Proc Natl Acad Sci U S A 106(5): 1404-1408.
  19. Pljevaljcic, G. and Millar, D. P. (2008). Single-molecule fluorescence methods for the analysis of RNA folding and ribonucleoprotein assembly. Methods Enzymol 450: 233-252.
  20. Debler, E. W., Kaufmann, G. F., Meijler, M. M., Heine, A., Mee, J. M., Pljevaljcic, G., Di Bilio, A. J., Schultz, P. G., Millar, D. P., Janda, K. D., Wilson, I. A., Gray, H. B. and Lerner, R. A. (2008). Deeply inverted electron-hole recombination in a luminescent antibody-stilbene complex. Science 319(5867): 1232-1235.
  21. Stengel, G., Gill, J. P., Sandin, P., Wilhelmsson, L. M., Albinsson, B., Norden, B. and Millar, D. (2007). Conformational dynamics of DNA polymerase probed with a novel fluorescent DNA base analogue. Biochemistry 46(43): 12289-12297.
  22. Bailey, M. F., Van der Schans, E. J. and Millar, D. P. (2007). Dimerization of the Klenow fragment of Escherichia coli DNA polymerase I is linked to its mode of DNA binding. Biochemistry 46(27): 8085-8099.
  23. Grover, R. K., Pond, S. J., Cui, Q., Subramaniam, P., Case, D. A., Millar, D. P. and Wentworth, P., Jr. (2007). O-glycoside orientation is an essential aspect of base J recognition by the kinetoplastid DNA-binding protein JBP1. Angew Chem Int Ed Engl 46(16): 2839-2843.
  24. Tian, F., Debler, E. W., Millar, D. P., Deniz, A. A., Wilson, I. A. and Schultz, P. G. (2006). The effects of antibodies on stilbene excited-state energetics. Angew Chem Int Ed Engl 45(46): 7763-7765.
  25. Pljevaljcic, G., Klostermeier, D. and Millar, D. P. (2005). The tertiary structure of the hairpin ribozyme is formed through a slow conformational search. Biochemistry 44(12): 4870-4876.
1 Protocol published
Fluorophore Labeling, Nanodisc Reconstitution and Single-molecule Observation of a G Protein-coupled Receptor
Authors:  Rajan Lamichhane, Jeffrey J. Liu, Raymond F. Pauszek III and David P. Millar, date: 06/20/2017, view: 2197, Q&A: 0
Activation of G protein-coupled receptors (GPCRs) by agonist ligands is mediated by a transition from an inactive to active receptor conformation. We describe a novel single-molecule assay that monitors activation-linked conformational transitions ...