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Mission

To understand the regulation of protein ubiquitination and the pathogenesis of neurodegenerative disease

Background

An ultimate goal in biology is to discover the molecular mechanism of life. During decades, the main approaches are reductionism methods such as studying one or a few genes. Although those methods have contributed to our understanding of many basic principles, a comprehensive picture of biology will not be captured until more integrative approaches are utilized. Recently, efforts in genomics, proteomics and bioinformatics have made it possible to study systems biology.

Mass spectrometry is the current choice for proteomic analyses. It is a powerful technology for identifying proteins and their modifications such as phosphorylation and ubiquitination. Moreover, the technology can be used to quantify the relative and absolute amount of proteins in a mixture. Using a technique termed multidimensional liquid chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS), we can profile hundreds to thousands of protein components in a complex sample at a sensitivity in the range of femtomoles or even attomoles.

Neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's share some common features: an age-related onset and deposition of protein aggregates. We are interested in mapping and profiling proteins and their modifications from patient samples and animal models. Combining with other tools in molecular biology, cell biology and genetics, we will explore the function of these proteins and their modifications in the development of these devastating diseases. These studies may provide proteins for drug targeting and strategies for therapeutic intervention.

Our Website for Proteomics Core:

http://proteo.whitehead.emory.edu/facility/