Education:

1984，B.Sc., Physical Chemistry，East China Institute of Chemical Technology，Shanghai, People’s Republic of China

1989，M.Sc. program, Medicinal Chemistry，Shanghai Institute of Materia Medica，Shanghai, People’s Republic of China        

1990，M.Sc., Organic Chemistry，New York University，New York, New York          

1997，Ph.D., Analytical Biochemistry，The Rockefeller University，New York, New York，Sponsor: Brian T. Chait, Ph.D.

Research Experience:

10/11-present   Professor, Ben May Department for Cancer Research, The University of Chicago

10/08-09/11   Associate Professor, Ben May Department for Cancer Research, The University of Chicago

02/05-09/08   Associate Professor, Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas; Co-Director, Protein Chemistry Core Center

09/00-01/05   Assistant Professor, Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas; Co-Director, Protein Chemistry Core Center

09/98-09/00   Assistant Professor; Director, Mass spectrometry Core Facility, Department of Human Genetics, The Mount Sinai School of Medicine.

08/93-03/98  Graduate Fellow and Postdoctral Associate, Laboratory of Mass Spectrometry and Gas Phase Chemistry, The Rockefeller University

Research Summary

    The Zhao lab’s main research interests lie in developing and applying mass spectrometry-based proteomics technologies to discovery of previously undescribed cellular pathways and to identifying biomarkers for personalized medicine. He also use an integrated approach, involving proteomics, biochemistry, molecular biology, and cell biology to decode protein post-translational modification (PTM) networks that have implications for human health and are not amenable to conventional techniques.

    Lysine acylations and new PTM pathways. Our lab carried out first few proteomic studies of lysine acetylation that led to identifying thousands of acetyllysine substrate peptides. These landmark works challenge a long-standing notion that lysine acetylation is restricted to nuclei and catalyze extensive investigation of non-nuclear functions of this modification pathway.  Our lab recently discovered eight types of new lysine acylation pathways: propionylation, butyrylation, crotonylation, malonylation, succinylation, glutarylation, 2-hydroxyisobutyrylation and 3-hydroxybutyrylation. They identified about 350 new histone marks, which more than doubles the tally of the previous known histone marks discovered during the first forty years of chromatin biology. They revealed numerous enzymes for the new PTM pathways, such as Sirt5 as a desuccinylase, demalonylase, and deglutarylase, as well as specific binding proteins (or “readers’) for the novel histone marks. His laboratory demonstrates that the new PTM pathways have critical roles in epigenetic regulation and cellular metabolism, and contribute to multiple inborn metabolic diseases.

    Discovery of biomarkers and tumor antigens. In the past few years, we have built a proteomic technology and bioinformatics platforms for quantifying protein expression, protein modifications (e.g., phosphorylation and acetylation), and histone epigenetic marks. We have use the technology for identifying proteomic signatures that can classify tumors and predicting drug sensitivity. We are also using proteomics approaches to identify tumor-specific antigens.  We are using these approaches for identifying predictive biomarkers for precision medicine and for immune oncotherapy.