Biography

Dr. David S. Waugh

Macromolecular Crystallography Laboratory

NCI-Frederick, USA


Email: waughd@mail.nih.gov


Qualifications

1989 Ph.D., Biochemistry, Indiana University
1982 B.Sc., Molecular Biophysics & Biochemistry, Yale University


Publications (Selected)

  1. Brabson, G.D. and Waugh, D.S. (1986). Two electrophoresis experiments for freshmen in the health professions.J. Chem. Ed.63: 540-542.
  2. Waugh, D.S. and Pace, N.R. (1986). Catalysis by RNA.Bioessays 4: 56-61.
  3. Pace, N.R., James, B.D., Reich, C., Waugh, D.S., Olsen, G.J., and Marsh, T.L. (1987). TheBacillussubtilisRNase P. In “Molecular Biology of RNA: New Perspectives,” M. Inouye and B. Dudock (eds.), Academic Press, pp. 17-36.
  4. Pace, N.R., Reich, C., James, B.D., Olsen, G.J., Pace, B., and Waugh, D.S. (1987). Structure and catalytic function in ribonuclease P.Cold Spring Harb. Symp. Quant. Biol.52: 239-247.
  5. Waugh, D.S., Sganga, M.W., Raff, M., and Pace, N.R. (1989). A site-directed mutation in theBacillussubtilisRNase P RNA that selectively influences its protein-dependent reaction. In “Molecular Biology of RNA,” T. Cech (ed.), Alan R. Liss, pp. 67-77.
  6. Waugh, D.S., Green, C.J., and Pace, N.R. (1989). The design and catalytic properties of a simplified ribonuclease P RNA.Science244: 1569-1571.
  7. Waugh, D.S. and Pace, N.R. (1990). Complementation of an RNase P RNA (rnpB) gene deletion inEscherichia coliby homologous genes from distantly related eubacteria.J. Bacteriol.172: 6316-6322.
  8. Pace, N.R. and Waugh, D.S. (1991). Design of a simplified ribonuclease P RNA by phylogenetic comparison. Methods Enzymol.203: 500-510.
  9. Waugh, D.S. and Pace, N.R. (1993). Gap-scan deletion analysis ofBacillus subtilisRNase P RNA.FASEB J.7: 188-195.
  10. Waugh, D.S.and Sauer, R.T. (1993). Single amino acid substitutions uncouple the DNA binding and strand scission activities ofFokI endonuclease.Proc. Natl. Acad. Sci. USA90: 9596-9600.
  11. Waugh, D.S. and Sauer, R.T. (1994). A novel class of Fok I restriction endonuclease mutants that cleave hemi-methylated substrates. J. Biol. Chem.269: 12298-12303.
  12. Emerson, S.D., Waugh, D.S., Scheffler, J.E., Tsao, K.-L., Prinzo, K.M., and Fry, D.C. (1994). Chemical shift assignments and folding topology of the ras-binding domain of human raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy. Biochemistry33: 7745-7752.
  13. Scheffler, J.E., Waugh, D.S., Bekesi, E., Kiefer, S.E., Losardo, J.L., Neri, A., Prinzo, K. M., Tsao, K.-L., Wegrzynski, B., Emerson, S.D., and Fry, D.C. (1994). Characterization of a 78-residue fragment of c-raf-1 that comprises a minimal binding domain for the interaction with ras-GTP.J. Biol. Chem.269: 22340-22346.
  14. Emerson, S.D, Madison, V.S., Palermo, R.E., Waugh, D.S., Scheffler, J.E., Tsao, K.-L., Kiefer, S.E., Liu, S.P., and Fry, D.C. (1995). Structure of the ras-binding domain of c-raf-1 and identification of its ras-interaction surface.Biochemistry 34: 6911-6918.
  15. Dracheva, S., Palermo, R.E., Powers, G.D., and Waugh, D.S. (1995). Expression of soluble human interleukin-2 receptor chain inEscherichia coli. Protein Expr. Purif.6: 737-747.
  16. Tsao, K.-L., DeBarbieri, B., Michel, H., and Waugh, D.S. (1996).A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification inEscherichia coli.Gene169: 59-64.
  17. Emerson, S.D, Madison, V.S., Palermo, R.E., Waugh, D.S., Scheffler, J.E., Tsao, K.-L., Kiefer, S.E., Liu, S.P., and Fry, D.C. (1996). Structure of the ras binding domain of c-raf-1 as determined by NMR spectroscopy and identification of the region that interacts with ras.Drug. Des. Discov.13: 83-93.
  18. Chen, T., Repetto, B., Chizzonite, R., Pullar, C., Burghard, C., Dharm, E., Zhao, Z., Carroll, R., Nunes, P., Basu, M., Danho, W., Visnick, M., Kochan, J., Waugh, D.S., and Gilfillan, A. (1996).
  19. Interaction of phosphorylated FcRI immunoglobulin receptor tyrosine activation motif-based peptides with dual and single SH2 domains of p72syk: Assessment of binding parameters and real time binding kinetics by a novel scintillation proximity assay. J. Biol. Chem. 271: 25308-25315.
  20. Waugh, D.S.(1996). Genetic tools for selective labeling of proteins with -15N amino acids.J. Biomol. NMR8: 184-192.
  21. Tsao, K.-L. and Waugh, D.S.(1997). Balancing the production of two recombinant proteins inEscherichia coliby manipulating plasmid copy number: High-level expression of heterodimeric Ras farnesyl transferase.Protein Expr. Purif.11: 233-240.
  22. Duffy, S., Tsao, K.-L., and Waugh, D.S. (1998). Efficient, site-specific biotinylation of recombinant proteins inSpodoptera frugiperdacells using biotin acceptor peptides. Anal. Biochem.262: 122-128.
  23. Baden, H.A., Sarma, S.P., Kapust, R.B., Byrd, R.A., and Waugh, D.S. (1998). The amino-terminal domain of human STAT4: Overexpression, purification, and biophysical characterization.J. Biol. Chem. 273: 17109-17114.
  24. Kervinen, J., Tobin, G.J., Costa, J.,Waugh, D.S., Wlodawer, A., and Zdanov, A. (1999). Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.EMBO J.18: 3947-3955.
  25. Kapust, R.B. and Waugh, D.S. (1999).Escherichia colimaltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused.Protein Sci.8: 1668-1674.
  26. Kireeva, M., Komissarova, N., Waugh, D.S., and Kashlev, M. (2000). The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex.J. Biol. Chem. 275: 6530-6536.
  27. Kapust, R.B. and Waugh, D.S. (2000). Controlled intracellular processing of fusion proteins by TEV protease.Protein Expr. Purif. 19: 312-318.
  28. Eisenmesser, E.Z., Kapust, R.B., Nawrocki, J.P., Mazzulla, M.J., Pannell, L.K., Waugh, D.S., and Byrd, R.A. (2000). Expression, purification, refolding, and characterization of recombinant human interleukin-13: utilization of intracellular processing.Protein Expr. Purif. 20: 186-195.
  29. Evdokimov, A.G., Anderson, D.E., Routzahn, K.M., and Waugh, D.S. (2000). Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of YopM, an essential virulence factor extruded by the plague bacterium,Yersinia pestis. Acta Cryst.D56: 1676-1679.
  30. Evdokimov, A.G., Anderson, D.E., Routzahn, K.M., and Waugh, D.S. (2001). Structural basis for oligosaccharide recognition byPyrococcus furiosusmaltodextrin-binding protein.J. Mol. Biol.305: 891-904.
  31. Fox, J.D., Kapust, R.B., and Waugh, D.S. (2001). Single amino acid substitutions on the surface ofEscherichia colimaltose-binding protein can have a profound impact on the solubility of fusion proteins.Protein Sci.10: 622-630.
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