Recommended Readings: Tom Muir, Ph.D., March 27

Friday Lecture Series
Friday, March 27, 2015
3:45 p.m., Caspary Auditorium

Tom Muir, Ph.D.
Van Zandt Williams Jr. Class of ‘65 Professor of Chemistry,
Chair, Department of chemistry
Princeton University

‘Houdini’ Proteins: Discovery and Applications of Ultrafast Inteins

Recommended Readings

Empirical Articles

Shah, N. H., Dann, G. P., Vila-Perelló, M., Liu, Z., & Muir, T. W. (2012). Ultrafast protein splicing is common among cyanobacterial split inteins: Implications for protein engineering. Journal of the American Chemical Society, 134(28), 11338–11341. doi:10.1021/ja303226x

Shah, N. H., Eryilmaz, E., Cowburn, D., & Muir, T. W. (2013). Naturally split inteins assemble through a “capture and collapse” mechanism. Journal of the American Chemical Society, 135(49), 18673–18681. doi:10.1021/ja4104364

Shah, N. H., Vila-Perelló, M., & Muir, T. W. (2011). Kinetic control of one-pot trans-splicing reactions by using a wild-type and designed split intein. Angewandte Chemie, 50(290, 6511–6515. doi:10.1002/anie.201102909

Vila-Perelló, M., Liu, Z., Shah, N. H., Willis, J. A., Idoyaga, J., & Muir, T. W. (2013). Streamlined expressed protein ligation using split inteins. Journal of the American Chemical Society, 135(1), 286–292. doi:10.1021/ja309126m

Review Papers

Eryilma, E., Shah, N. H., Muir, T. W., & Cowburn, D. (2014). Structural and dynamical features of Inteins and implications on protein splicing. Journal of Biological Chemistry, 289(21), 14506–14511. doi:10.1074/jbc.R113.540302

Shah, N. H., & Muir, T. W. (2014). Inteins: Nature’s Gift to Protein Chemists. Chemical Science, 5(1), 446–461. doi:10.1016/j.biotechadv.2011.08.021.Secreted

Recommended Readings: Hermann Steller, Ph.D May 5

Monday Lecture Series
Monday, May 5, 2014
4:00 p.m., Carson Family Auditorium

Hermann Steller, Ph.D
Strang Professor, Strang Laboratory of Apoptosis and Cancer Biology
The Rockefeller University
Investigator, Howard Hughes Medical Institute

Regulation of Protein Degradation in Development, Aging and Disease

Recommended Readings:

Empirical Articles

Bader, M., Benjamin, S., Wapinski, O. L., Smith, D. M., Goldberg, A. L., & Steller, H. (2011). A conserved F box regulatory complex controls proteasome activity in Drosophila. Cell, 145(3), 371–382. doi:10.1016/j.cell.2011.03.021

Cho-Park, P. F., & Steller, H. (2013). Proteasome regulation by ADP-ribosylation. Cell, 153(3), 614–627. doi:10.1016/j.cell.2013.03.040

Review Papers

Finley, D. (2009). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annual Review of Biochemistry, 78(1), 477–513. doi:10.1146/annurev.biochem.78.081507.101607

Glickman, M. H., & Ciechanover, A. (2002). The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiological Reviews, 82(2), 373–428. doi:10.1152/physrev.00027.2001

Murata, S., Yashiroda, H., & Tanaka, K. (2009). Molecular mechanisms of proteasome assembly. Nature Reviews Molecular Cell Biology, 10(2), 104–15. doi:10.1038/nrm2630

Recommended Readings: Debora Marks, Ph.D. March 31

SPECIAL SEMINAR
Wednesday, March 31, 2014
4:00 p.m., Carson Family Auditorium

Debora Marks, Ph.D.
Instructor
Department of Systems Biology
Harvard Medical School

Evolutionary Co-variation in Genomic Sequences Gives Protein 3D and Quantitative Mutation Effects

Recommended Readings:

Empirical Articles

Hopf, T. A., Colwell, L. J., Sheridan, R., Rost, B., Sander, C., & Marks, D. S. (2012). Three-dimensional structures of membrane proteins from genomic sequencing. Cell, 149(7), 1607–1621. doi:10.1016/j.cell.2012.04.012

Marks, D. S., Colwell, L. J., Sheridan, R., Hopf, T. a, Pagnani, A., Zecchina, R., & Sander, C. (2011). Protein 3D structure computed from evolutionary sequence variation. PLOS One, 6(12), e28766. doi:10.1371/journal.pone.0028766

Morcos, F., Pagnani, A., Lunt, B., Bertolino, A., Marks, D. S., Sander, C., … Weigt, M. (2011). Direct-coupling analysis of residue coevolution captures native contacts across many protein families. Proceedings of the National Academy of Sciences, 108(49), 1293–1301. doi:10.1073/pnas.1111471108

Review Papers

Marks, D. S., Hopf, T. A, & Sander, C. (2012). Protein structure prediction from sequence variation. Nature Biotechnology, 30(11), 1072–1080. doi:10.1038/nbt.2419