Mechanisms of tumor resistance to chemotherapy and immunotherapy; new methods for proteomics; exosomes and their proteomes and analysis of polyubiquitins
ASMS, ACS, ASPET, AACR, HUPO, USHUPO
Major Recognitions and Honors
Significant Professional Service and Activities
National Research Council Board on Chemical Sciences and Technology 2000-2006; NIH: study section Medicinal Chemistry B 1975-1979; study section Pharmacological Sciences 1989-1993; Council member, Institute for Research Resources 2003-2007; NSF: Director’s Advisory Council 1979-1983; ACS: Associate Editor Analytical Chemistry 1990-present; Chair Analytical Chemistry Division 2001-2002; Division Councilor 2005-2013; International Human Proteome Organization (HUPO): Vice President, 2007-2008; Service Award 2006; U.S.HUPO: founding president 2004-2006; American Society for Mass Spectrometry: President 1982-1984; Founding Editor Biological Mass Spectrometry (now Journal of Mass Spectrometry) 1973-1989; Editorial Advisory Boards (current & past): J. Proteome Research; Clinical Proteomics; Protein Structure, Function and Genetics; Mass Spectrometry Reviews; Drug Discovery; Drug Metabolism and Disposition; Journal of Mass Spectrometry; Biological Mass Spectrometry; Pharmaceutical and Biomedical Analysis; Chemical Research in Toxicology; Journal of the Amer. Soc. Mass Spectrometry; Chemical & Engineering News.
More than 150 post-doctoral fellows, graduate students and undergraduate students have received training in Dr. Fenselau’s laboratories at Johns Hopkins Med School, UMBC and the University of Maryland.
Catherine Fenselau Research
Historically our research program has focused on the exploitation of mass spectrometry in biomedical research. Through the last fifteen years we have helped to open proteomics, the post-genomic science that provides unbiased and high throughput interrogation of large protein mixtures.
Middle-out and top-down proteomics. Classic proteomic workflows analyze tryptic peptides, which generally weigh less than 3000 Da (bottom up). The importance of multiple and coordinated post-translational modifications compels analysis of longer peptides (middle out) and intact proteins (top down). We have introduced microwave-enhanced acid proteolysis into proteomic workflows. This rapid (<30 min) chemical reaction produces longer peptides by kinetically selective cleavage at aspartic acid residues (Cannon et al, J. Proteome Research-2010). We have also successfully implemented top-down analysis of small proteins to characterize bacteria (Wynne et al, Analytical Chemistry 2009). On-going applications include characterization of intact and processed proteins in exosomes.
Analysis of branched proteins. We are applying middle-out and top-down strategies to decipher the number of subunits and points of attachment of ubiquitins in anchored and unanchored polyubiquitins isolated from exosomes (Cannon et al, Analytical Chemistry 2012).
Exosomes and their proteomes. We are characterizing the protein and RNA cargos carried by exosomes shed by myeloid derived suppressor cells in the tumor microenvironment (Burke et al, J. Proteome Research 2014). This continues our long-standing interest in mechanisms of tumor resistance to therapeutics.