Office Phone: 301-405-1877
 Office Address: 1506
 Group Website

Associate Professor (1/1/2018)


  • M.S. Chemistry (Analytical) (summa cum laude), 1999–2004, Eotvos Lorand University, Budapest, Hungary (with Prof. Karoly Vekey, Chemical Research Center, Hungarian Academy of Sciences, Budapest, Hungary)
  • Ph.D. Chemistry (Analytical), 2005–2009, The George Washington University, Washington, DC (with Prof. Akos Vertes)
  • Postdoctoral Fellow (Bioanalytical Neuroscience), 2009–2011, University of Illinois at Urbana-Champaign, Champaign, IL (with Prof. Jonathan V. Sweedler)

Professional Experience

  • Associate Professor, Department of Chemistry & Biochemistry, University of Maryland at College Park, 2018–Present
  • Assistant Professor, Department of Chemistry, The George Washington University, 2013–2017
  • Co-Chair, Washington-Baltimore Mass Spectrometry Discussion Group, 2011–2013
  • Staff Fellow and Laboratory Leader, US Food and Drug Administration, Silver Spring, MD (FDA), 2011–2013

Research Interests

Next-generation technologies for mass spectrometry; metabolomics; proteomics; mechanisms of cell and embryonic development; cell fate specification; neurodegenerative diseases

Major Recognitions and Honors

  • Research Award, American Society for Mass Spectrometry (ASMS), 2017
  • Scientific Achievement Award, US Food and Drug Administration (FDA), 2017 (FDA co-recipients: Samanthi Wickramasekara, Hongli Li, and David Keire)
  • Robert J. Cotter New Investigator Award, US Human Proteome Organization (HUPO), 2017
  • DuPont Young Professor Award, DuPont company (Wilmington, DE), 2017
  • Arthur F. Findeis Award for Achievements by a Young Analytical Chemist, American Chemical Society (ACS) Division of Analytical Chemistry, 2016
  • Helmsley Fellowship for cross-disciplinary academic and scientific career, Cold Spring Harbor Laboratory (Cold Spring Harbor, NY), 2016
  • Emerging Investigator, Journal of American Society for Mass Spectrometry (JASMS), 2016
  • Emerging Investigator, Analyst, 2016
  • Beckman Young Investigator, Arnold and Mabel Beckman Foundation (Irvine, CA), 2015
  • FDA Special Recognition Award, US Food and Drug Administration (Silver Spring, MD), 2011
  • Science and Technology Innovation Award, Baxter Healthcare Corporation (Chicago, IL), 2010
  • American Institute of Chemists prize in Chemistry, The American Institute of Chemists (Washington, DC), 2009
  • Young Investigator Travel Award, Washington-Baltimore Mass Spectrometry Discussion Group, 2009
  • International Research Fellowship Award, Dimitris N. Chorafas Foundation (Luzern, Switzerland), 2008
  • Young Investigator Travel Award, Washington-Baltimore Mass Spectrometry Discussion Group, 2007

Significant Professional Service and Activities

Ad hoc reviewer for the National Science Foundation (NSF), National Institutes of Health (NIH), ACS Petroleum Research Fund, Hungarian Academy of Sciences, ACS Arthur F. Findeis Award

Students Mentored

Currently mentoring: 5 PhD students and 1 post-doctoral fellow. Completed mentoring: 2 post-doctoral fellows, 4 undergraduate students, and 3 high school students.


Topics: Bioanalytical Mass Spectrometry, Microanalytical Separations, Metabolomics, Proteomics, Systems Biology, Cell and Developmental Biology, Neuroscience, Human Health

Research Goals. During normal development, the embryo must properly execute molecular programs to differentiate from the one-cell zygote into all the different types of cells that form the organism. While decades of research have identified genes with key roles during development, very little is known about the production of proteins and metabolites and the functions of these molecules during development. The challenge has been insufficient sensitivity, primarily by mass spectrometry, to detect these important biomolecules in single cells and limited amounts of tissues.  The Nemes Research Laboratory takes an interdisciplinary approach to fill these technology and knowledge gaps at the interface of bioanalytical mass spectrometry, neuroscience, and cell and developmental biology.

Objective 1. We Build Trace-sensitive Mass Spectrometry Platforms for Metabolites

Figure 1Figure 1

Metabolites are highly dynamic and sensitive to intrinsic and extrinsic events, making the metabolome an excellent descriptor of cellular phenotype. However, cells contain vanishing amounts of material, which has traditionally hindered metabolite detection by mass spectrometry, the technology of choice for the analysis of these small molecules. To overcome this limitation, we undertake multiple projects to develop high-resolution mass spectrometry instruments capable of trace-level sensitivity. For example, in “R. M. Onjiko, S. A. Moody, and P. Nemes*, PNAS 2015, 112, 6545,” we custom-built a single-cell mass spectrometer instrument to allow us to characterize metabolites in single embryonic cells.  Furthermore, in “R. M. Onjiko, E. P. Portero, S. A. Moody, and P. Nemes*, Anal. Chem. 2017, 89, 7069,“ we equipped this single-cell mass spectrometer with a capability for direct analysis of cells directly in live embryos (Figure 1).

Objective 2. We Build Trace-sensitive Mass Spectrometry Platforms for Proteins

Figure 2Figure 2

Proteins carry out critical molecular functions during cell differentiation and development. However, without molecular amplification of the whole proteome, it has been historically challenging to detect diverse proteins over a broad dynamic concentration range in limited amounts of samples. We have several projects aimed at advancing ultrahigh-resolution mass spectrometry to ultrasensitivity to enable the characterization of large numbers of proteins in single cells. For example, in “C. Lombard-Banek, S. A. Moody, and P. Nemes*, Angew. Chem. Int. Ed. 2016, 55, 2454,” we built a single-cell mass spectrometry instrument capable of identifying and quantifying ~1000–2,000 different proteins between single embryonic cells (Figure 2). Furthermore, in “B. S. Choi, M. Zamarbide, M. Chiara Manzini, and P. Nemes*, J. Am. Soc. Mass Spectrom. 2016, 28, 597,” we empowered this instrument with a record sensitivity to detect proteins in protein digests that approximate the content of a single mammalian neuron.

Figure 3Figure 3

Objective 3. We Uncover Molecular Players during Normal and Impaired Development

Using our unique mass spectrometry platforms, we ask the question how the metabolome and proteome changes and what molecules roles these functionally important molecules play during key stages of development. Specifically, we study these molecular players during cell differentiation and body patterning using the frog Xenopus laevis embryo and neurogenesis using the mouse (Mus musculus). For example, in “Onjiko et al., PNAS 2015,” we quantified metabolic differences between identified embryonic cells. Furthermore, we discovered metabolites that are able to alter the normal tissue fate of cells in the X. laevis embryo: the normally neural tissue-fated D11 cell gave rise to epidermal tissue (Figure 3).  In “C. Lombard-Banek, Sally A. Moody, and P. Nemes*, Mol. Cell. Prot. 2016, 15, 2756,” we uncovered previously unknown proteomic cell heterogeneity in the 16-cell X. laevis embryo.

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