Time：9:00 am, Oct. 31th of 2016
Location：Academic Report Hall of Department of Biotechnology
Reporter：
Dr. Yi Shi currently works in Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, National Center for the Mass Spectrometric Analysis of Biological Macromolecules of The Rockefeller University.
He obtained his bachelor degree of engineering from Dalian University of Technology in 2003. From August of 2006,he began to study as a PH. D candidate in Baylor College of Medicine and obtained his Ph. D degree in 2011. He carried out his postdoctoral research from 2011 to 2014 and worked as research associate from 2014 to 2016in the Rockefeller University. He is appointed as Assistant Professor in Department of Cell Biology, University of Pittsburgh School of Medicine and will work there from November of 2016.
His research interest is focused on Mass Spectrometry & Proteomics,Integrative Structural Biology, DNA damage and Autophagy as well as Antibody and Immunology.He has published several articles in famous international scientific journals such as Cell, Nature Methods, Nature Structural Molecular Biology and Molecular & Cellular Proteomics.
Abstract：
The extraordinarily emergent properties of living cells have evolved largely as a consequence of the intricately ordered interactions of their biomolecular components. These cellular building blocks (DNA, RNA, proteins, lipids etc.) interact with one another to form a hierarchy of dynamic, information-rich, macromolecular assemblies that drive a plethora of intriguing biological processes. Unfortunately, despite their central role in cell biology, the requisite structure-functional studies of endogenous multi-subunit macromolecular assemblies still prove to extraordinarily challenging- partially due to their low cellular abundance , dynamic nature, and heterogeneity of these native assemblies.
Over the years we have developed enabling integrative structural proteomic technologies to overcome these challenges. We have also applied these new tools to study the architectures and functions of large native macromolecular assemblies that regulate several fundamentally important processes of cell biology including DNA replication, basal gene transcription and its regulations. Most recently, we have begun to unravel the mechanistic details of the eukaryotic nuclear pore complex- the gigantic, ~500 protein machine that has been conserved for over a billion years of evolution, and the sole mediator for nuclear-cytoplasmic transport.
Contact：Prof. Lihua Zhang of group 1810（phone: 9720）