boyangzhao > academics
email: info [at] boyangzhao.com
profile at LinkedIn
PubMed search term: zhao, boyang
Education
Ph.D. in Computational and Systems Biology, 2011 - Present
Massachusetts Institute of Technology
B.S.E. in Biomedical Engineering (Biochemical Concentration), 2011
Minor in Computer Science
College of Engineering
University of Michigan, Ann Arbor
Academic/Research Interests
Aside from my interest in all aspect of science, technology, business, and patent law, my current research interest is on using a quantitative systems biology approach to elucidate pathologically relevant signaling networks and developing and translating novel therapeutics for pressing healthcare problems.
Selected Previous Research Works
Phosphoproteomic profiling & conservation analysis of phosphotyrosine sites in native rat renal collecting duct
The renal collecting duct plays an essential role in the body's electrolyte and fluid balance. In many cell types, the tyrosine phosphorylation signaling network is crucial in cellular signaling processes controlling many important biological functions. However, this signaling network has not been broadly studied in the renal collecting duct cell. To systematically investigate the signaling network in this cell type, the first objective was to identify the phosphotyrosine (pY) sites using a tandem mass spectrometry. A major obstacle in profiling the tyrosine phosphorylation is its low abundance. In this study, the renal collecting ducts were freshly isolated from rat kidneys and two strategies were applied to enrich for pY peptides: 1) by globally inhibiting tyrosine phosphatases using pervanadate and 2) by performing anti-pY immunoprecipitation in series with Ga3+-immobilized metal affinity chromatography. This results of this study expands on the known pY sites in renal collecting duct cell.
A novel algorithm was also developed to determine the likelihood of functional relevance for the identified pY sites. The algorithm utilizes information theory and is based on site/sequence conservation. This provides an additional method for assessing the functional relevance of novel phosphorylation sites.
Repair mechanism of 3-methlyadenine DNA glycosylase II (AlkA)
Escherichia coli 3-methlyadenine DNA glycosylase II (AlkA) is known to remove a variety of bases such as 1,N6-ethenoadenosine (εA) and inosine from DNA. However, the mechanism by which AlkA searches and catalyzes base excision at damaged sites is poorly understood. The current proposed minimal mechanism involves AlkA binding to the substrate, flipping out the damaged based, followed by catalyzing the hydrolysis of the N-glycosidic bond. The processivity and kinetic mechanism of the glycosylase was studied using a number of processivity and kinetic assays. A better understanding of the mechanism of how AlkA searches and repairs damaged bases would give further insight into the fundamental principles of lesion recognition and excision.
Publications
* indicates co-first authorship
Curriculum vitae available upon request