Yingxin Zhao, Ph.D.Dr. Zhao

Assistant Professor, Dept. of , Scientist, Sealy Center for Molecular Medicine

contact info

Research Interests

My research focuses on developing and applying of state-of-the-art mass spectrometry and proteomics to elucidate protein structure and function, to accurately quantify the temporal changes in the proteome, and to identify the potential diagnostic markers and drug targets for the treatment of diseases. Specifically, I am interested in the following aspects in mass spectrometry and proteomics:

  1. Quantitative proteomics and phosphoproteomics. A multifaceted approach, which combined stable-isotope labeling, immobilized metal affinity chromatography, and 2-Dimensional HPLC tandem mass spectrometry, was established in the laboratory to accurately quantify the temporal changes in the proteome and phosphoproteome. This method is being used to identify the biomarkers and drug targets in type 2 diabetes and Alzheimer’s disease on a global scale.
  2. Quantitative proteomic and phosphoproteomic analysis of plasma integral membrane proteins. Plasma integral membrane proteins play fundamental roles in material transport between the cell and its environment. The phosphorylation of integral membrane proteins and their associated proteins is one of the most important events in signal transduction. My research focuses on establishing the dynamics of cell plasma membrane proteome and phosphoproteome in response to a stimulus and identifying aberrantly expressed cell surface proteins and phosphoproteins for drug and vaccine design.
  3. Proteomic analysis of other protein post-translational modifications. I am interested in developing and applying new technologies for analysis of other protein post-translational modifications including ubiquitination, acetylation, and methylation. Our strategy involves in the specific isolation of peptides containing post-translation modifications and the interpretation of the modified peptides by mass spectrometry.
  4. Characterization of signal pathways and protein networks by identifying the composition of protein complexes using mass spectrometry-based proteomic methods.

Selected Publications

  1. Zhao Y, Zhang W, White M., Zhao Y. Capillary HPLC/MS spectrometric analysis of proteins from affinity-purified plasma membrane. Anal Chem 2003; 75: 3751-3757.
  2. Zhang W, Zhou G, Zhao Y, White MA, Zhao Y. Affinity-purification of plasma membrane for proteomics analysis. Electrophoresis 2003; 24:2855-2863.
  3. Zhao Y, Zhang W, Kho Y, Zhao Y. Proteomics analysis of integral plasma Membrane proteins. Anal Chem 2004; 76:1817-1823.
  4. Geiman TM, Sankpal UT, Robertson AK, Zhao Y, Zhao Y, Robertson KD. DNMT3B interacts with hSNF2H chromatin remodeling enzyme, HDACs 1 and 2, and components of the histone methylation system. Biochem Biophys Res Commun 2004; 318:544-555.
  5. Intine RV, Dundr M, Vassilev A, Schwartz E; Zhao Y, Zhao Y, DePamphilis ML, Maraia RJ. Nonphosphorylated human La antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis. Mol Cell Biol 2004; 24:10894-10904.
  6. Xu HM, Liao B, Zhang QJ, Wang BB, Li H, Zhong XM, Sheng HZ, Zhao Y, Zhao Y, Jin Y. Wwp2, an E3 ubiquitin ligase that targets transcription factor Oct-4 for ubiquitinaion. J Biol Chem 2004; 279:23495-23503.
  7. Zhao Y, Giorgianni F, Desiderio DM, Fang B, Beranova-Giorgianni S. Toward a global analysis of the human pituitary proteome by multiple gel-based technology. Anal Chem 2005; 77:5324-5331.
  8. Cheng J, Zhang D, Kim K, Zhao Y, Zhao Y, Su B. Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. Mol Cell Biol 2005; 25:5955-5964.
  9. Zhao G, Li H, Gong Y, Zhao Y, Cheng J, Lee P, Zhao Y. Proteomic analysis of global alteration of protein expression in squamous cell carcinoma of the esophagus. Proteomics 2005; 5: 3814-3821.
  10. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F. Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9:109-120.