Honors & Awards

  • Junior Faculty Award, AD/PD 2019 Congress (2019)
  • Ruth L. Kirchstein NRSA Postdoctoral Fellowship, NIH/NIA (2018-2021)
  • Young Investigator Award, Alzheimer?s Association Bay Area (2018)
  • Postdoctoral Fellowship for Translational Research on Aging, Glenn/AFAR (2015)
  • Harold M. Weintraub Graduate Student Award Nominee, University of Southern California (2014)
  • Spring Scholar Award, University of Southern California (2014)
  • Young Investigator Award, Alzheimer?s Association Los Angeles (2014)
  • Zach Hall Award, Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, CA (2014)
  • Ruth L. Kirchstein NRSA Pre-doctoral Fellowship, NIH/NINDS (2013-2015)
  • Excellence in Research Award, Department of Neurosurgery, Cedars-Sinai Medical Center, Los Angeles, CA (2009)

Professional Education

  • Bachelor of Arts, University of California Santa Barbara (2007)
  • Doctor of Philosophy, University of Southern California (2015)

Stanford Advisors


All Publications

  • Multiple Click-Selective tRNA Synthetases Expand Mammalian Cell-Specific Proteomics JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Yang, A. C., Du Bois, H., Olsson, N., Gate, D., Lehallier, B., Berdnik, D., Brewer, K. D., Bertozzi, C. R., Elias, J. E., Wyss-Coray, T. 2018; 140 (23): 7046?51


    Bioorthogonal tools enable cell-type-specific proteomics, a prerequisite to understanding biological processes in multicellular organisms. Here we report two engineered aminoacyl-tRNA synthetases for mammalian bioorthogonal labeling: a tyrosyl ( ScTyrY43G) and a phenylalanyl ( MmPheT413G) tRNA synthetase that incorporate azide-bearing noncanonical amino acids specifically into the nascent proteomes of host cells. Azide-labeled proteins are chemoselectively tagged via azide-alkyne cycloadditions with fluorophores for imaging or affinity resins for mass spectrometric characterization. Both mutant synthetases label human, hamster, and mouse cell line proteins and selectively activate their azido-bearing amino acids over 10-fold above the canonical. ScTyrY43G and MmPheT413G label overlapping but distinct proteomes in human cell lines, with broader proteome coverage upon their coexpression. In mice, ScTyrY43G and MmPheT413G label the melanoma tumor proteome and plasma secretome. This work furnishes new tools for mammalian residue-specific bioorthogonal chemistry, and enables more robust and comprehensive cell-type-specific proteomics in live mammals.

    View details for DOI 10.1021/jacs.8b03074

    View details for Web of Science ID 000435525500001

    View details for PubMedID 29775058

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