The current focus of my laboratory is investigation of protein-protein and protein-nucleic acid interactions in the context of stress granule assembly. Specifically, we are interested in the role of G4 DNA structures and their protein interactors in mediating intracellular stress during aging. Over the past 12 years I worked in the area of quantitative mass spectrometry developing label-free and stable isotope-based proteomics methods and applying them to various bio-analytical problems. First, during my post-doctoral training with Mike Washburn at Stowers Institute (Kansas City, MO) I developed the statistical framework for the spectral counting methods and applied it to the study of differential accumulation of yeast membrane proteins. During my second post-doc with Klaas van Wijk at Cornell University (Ithaca, NY) I used spectral counting to study organelle proteome dynamics and protein homeostasis in Arabidopsis. In addition to the large-scale proteomics studies I also was involved in targeted analysis of protein complexes: mammalian mediator complex (at Stowers) and Clp protease complex (at Cornell). During my work as a Research Associate with David Goldfarb, as a part of newly formed company - Calorics Pharmaceuticals - I designed proteomics screens to identify targets of caloric restriction mimetics – small molecules extending replicative lifespan in yeast. We routinely use methods of systems biology, mass-spectrometry based proteomics, large-scale OMICS data integration and big data mining.

American Society for Mass Spectrometry

Kevin D Raney
Galina Glazko

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