Education & Certifications

  • Doctor of Medicine, Stanford University, MED-MD (2015)
  • Master of Science, New York University, Chemistry (2008)
  • Bachelor of Arts, New York University, Biochemistry (2007)


All Publications

  • The E3 Ubiquitin Ligase UBE3C Enhances Proteasome Processivity by Ubiquitinating Partially Proteolyzed Substrates JOURNAL OF BIOLOGICAL CHEMISTRY Chu, B. W., Kovary, K. M., Guillaume, J., Chen, L., Teruel, M. N., Wandless, T. J. 2013; 288 (48): 34575-34587


    To maintain protein homeostasis, cells must balance protein synthesis with protein degradation. Accumulation of misfolded or partially degraded proteins can lead to the formation of pathological protein aggregates. Here we report the use of destabilizing domains, proteins whose folding state can be reversibly tuned using a high affinity ligand, as model substrates to interrogate cellular protein quality control mechanisms in mammalian cells using a forward genetic screen. Upon knockdown of UBE3C, an E3 ubiquitin ligase, a reporter protein consisting of a destabilizing domain fused to GFP is degraded more slowly and incompletely by the proteasome. Partial proteolysis is also observed when UBE3C is present but cannot ubiquitinate substrates because its active site has been mutated, it is unable to bind to the proteasome, or the substrate lacks lysine residues. UBE3C knockdown also results in less substrate polyubiquitination. Finally, knockdown renders cells more susceptible to the Hsp90 inhibitor 17-AAG, suggesting that UBE3C protects against the harmful accumulation of protein fragments arising from incompletely degraded proteasome substrates.

    View details for DOI 10.1074/jbc.M113.499350

    View details for Web of Science ID 000329812800026

  • Site-specific inter-strand cross-links of DNA duplexes CHEMICAL SCIENCE Ye, M., Guillaume, J., Liu, Y., Sha, R., Wang, R., Seeman, N. C., Canary, J. W. 2013; 4 (3): 1319-1329

    View details for DOI 10.1039/c2sc21775a

    View details for Web of Science ID 000314474900058

  • Coupling across a DNA helical turn yields a hybrid DNA/organic catenane doubly tailed with functional termini JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Liu, Y., Kuzuya, A., Sha, R., Guillaume, J., Wang, R., Canary, J. W., Seeman, N. C. 2008; 130 (33): 10882-?


    We describe the synthesis of a hybrid DNA/organic macrocycle that is prepared by formation of an amide linkage across one full turn of DNA. Formation of a catenane proved that the linkage crossed a turn rather than running along the phosphodiester backbone contour. The product, a doubly tailed catenane, contains 5'- and 3'-termini that can be functionalized further or used to incorporate the catenane structure into other DNA assemblies.

    View details for DOI 10.1021/ja8041096

    View details for Web of Science ID 000258415900026

    View details for PubMedID 18661989

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