Distinguished University Professor
- A.B. Chemistry 1961, Bryn Mawr College, Bryn Mawr, PA
- Ph.D. Organic Chemistry 1965, Stanford University (with Carl Djerassi)
- Postdoctoral Fellow 1966, Univ. Calif. Berkeley, (with Melvin Calvin) (AAUW Fellowship)
- Postdoctoral Fellow 1967, NASA Space Sciences Laboratory (with Melvin Calvin and A.L. Burlingame)
- Professor, Dept. of Chemistry & Biochemistry, University of Maryland, 1998-present
- Member, Greenebaum Cancer Center, Univ. Maryland Med. School, 2001-present
- Affiliate faculty, Fischell Dept of Bioengineering, Univ. of Maryland, 2007-present
- Chair, Dept. of Chemistry & Biochemistry, University of Maryland, 1998-2000
- Professor and Chair, Dept. of Chemistry & Biochemistry, Univ. Maryland Baltimore County, 1987-1998
- Interim Dean of the Graduate School & Assoc. Vice President for Research, UMBC 1995-1996
- Instructor to Professor, Dept. of Pharmacology and Molec. Science, Johns Hopkins Univ. Sch. of Med., 1967-1987
- Visiting Professor, Kansai Univ. (Japan) 1986
- Visiting Professor, Univ. Warwick (UK) 1980
- Exchange Lecturer Moscow Institute of Physics & Technology 1991
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
- Distinguished Contribution Award, American Society for Mass Spectrometry 2012
- Ralph Adams Award in Bioanalytical Chemistry 2010
- Board of Trustees, Maryland Science Center 1998-2010
- Fellow, American Chemical Society 2009
- Internat.Mass Spectrom.Foundation Thomson Medal 2009
- ACS Field & Franklin Award for Contributions in Mass spectrom. 2008
- Braude Award, ACS Chesapeake Section, 2006
- Honorary Foreign Member of the Japanese Society for Mass Spectrometry 2006-present
- Hillebrand Prize, ACS Capitol Section; AnaChem Award 2003
- Elected Fellow of the American Association for the Advancement of Science 2001
- Eastern Analytical Symposium Award for Achievements in Analytical Chemistry 1999
- Robert and Jane Meyerhof Chair in Biochemistry 1997-1998
- Medal of the Spectroscopy Society of Pittsburgh 1993
- NIH Merit award 1991-2001
- Maryland Chemist Award, ACS Chesapeake Section1989
- ACS Garvan Medal,1985; Best Paper of the Year in Drug Metabolism Disposition 1982
- NIH Research Career Development Award 1970-1974
- Fellow, American Association of University Women 1965-1966
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.
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.