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Mass spectrometry-based proteomics of cell signaling, regulation and disease

The mission of the Griffin laboratory is to develop, disseminate and apply mass spectrometry-based tools for studying proteins and their role in cell signaling, regulation and disease. Our work is highly collaborative and interdisciplinary in nature, bringing together aspects of molecular and cellular biology, biochemistry, analytical chemistry, computer science, statistics and the clinical sciences.
Our laboratory is located within the Department of Biochemistry, Molecular Biology and Biophysics, which is located in the Molecular and Cellular Biology building (MCB).

Research interests within our lab include:

  • Making new discoveries which will lead to better treatment of patients in the clinic. A current focus is using proteomics to discover and verify salivary proteins which could be used for the early detection and monitoring of oral cancer

  • Studying basic mechanisms of cell signaling and regulation. A current focus is a collaborative project studying the target-of-rapamycin (TOR) protein, the main regulator of nutrient response and cell growth

  • Characterizing post-translationally modified proteins. A current focus is proteomic studies of protein carbonylation, a poorly understood modification associated with the aging process and a variety of diseases

 

Research Interests

Clinical Proteomics

Using proteomics to discover and verify salivary proteins which could be used for the early detection and monitoring of oral cancer.

Clinical ProteomicsClinical Proteomics

 

Cell Signaling and Regulation

Proteomic studies of the target-of-rapamycin (TOR) protein, the main regulator of nutrient response and cell growth.

Cell Signalling and RegulationCell Signaling and Regulation

 

Post-translational protein modifications

Proteomic studies of protein carbonylation, a poorly understood modification associated with the aging process and a variety of diseases.

Post-translational problem modificationsPost-transitional protein modifications

 

© Arsen Bagyan 2008
University of Minnesota, Twin Cities Dept. Biochemistry, Molecular Biology and Biophysics Griffin Lab