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Director of Proteomics at the Broad Institute of MIT and Harvard, Steven Carr, to Deliver Pittcon 2014 Wallace H. Coulter Plenary Lecture
Date:5/15/2013

Pittsburgh, PA (PRWEB) May 15, 2013

Dr. Carr is internationally recognized as a leader in the development of novel proteomics methods and in their application in biology and medicine. Dr. Carr and his group collaborate with scientists throughout the greater Broad community (Broad Institute, Harvard, Harvard Medical School, and the 17 Harvard affiliated hospitals) to apply state-of-the art proteomics technology to address compelling questions in biology, chemistry and clinical medicine. He has over 200 publications on development and use of proteomics and biological mass spectrometry.

Carr’s lecture will address the new era of quantitative biology enabled by mass spectrometry based proteomic technologies that has arrived. The content, relative abundance, modification states and interaction partners of proteins in a dynamic and temporal manner on a near-global basis in organelles, whole cells and clinical samples, providing information of unprecedented detail can now be defined. At the Broad Institute, Carr and his team are employing these technologies in a wide array of studies including delineating the genetic underpinnings of mitochondrial disorders, connecting cancer genotype to molecular phenotype, unraveling the basis of the innate-immune response, identifying the mechanism of action of drug-like molecules and to discover and verify protein biomarkers of disease. A representative set of project vignettes will be presented to convey a sense of the breadth and depth of application of modern proteomics to biology and medicine.

When asked to comment on his work, Dr. Carr stated, "Significant improvements in mass spectrometry-based proteomic technologies over the past few years have greatly increased the value and necessity of analyzing proteins and their modifications in biology and medicine. The number of proteins observed in cells and tissues now begins to approximate the expected expressed proteome.” H
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