Cristina M. Furdui, Ph.D.
Assistant Professor, Internal Medicine - Molecular Medicine
Email: cfurdui@wfubmc.edu
Education:
B.S. 1996, Department of Chemistry, Babes-Bolyai University, Romania
M.S. 1997, Catalysis and Biocatalysis, Babes-Bolyai University, Romania
Ph.D. 2002, Department of Biochemistry, University of Nebraska, Lincoln
Postdoctoral Training 2002-2006, Department of Pharmacology, Yale University School of Medicine
Current Research: Mass Spectrometry: Development of Novel Proteomics Methodologies; Dynamic Analysis of Cell Signaling, Targeted Drug Design through the Identification of Transient Kinetic Intermediates
Our laboratory focuses on translational research in cancer, cardiovascular and aging-related diseases. A brief description of our ongoing projects is presented below. More detailed information about the experimental approach and instrumentation can be found on our laboratory webpage.
(I) Dynamic analysis of signaling events at molecular and cellular level using quantitative, mass spectrometry based proteomics experiments.
Posttranslational modifications like phosphorylation and oxidation are at the core of cell signaling and their role in the modulation of protein activity has been widely studied. However, less is known about the timing and coordination of these events in the cellular environment. In this context, we are taking a kinetics approach to proteomics to determine the impact of oxidation and occurring oncogenic mutations on signaling pathways.
(II) Instrumentation development for systems biology studies - in vitro and in vivo kinetics by interfacing time-resolved mass spectrometry with microfluidics technology.
We are continuing to develop mass spectrometry as a new tool to determine the nature of transient species in the catalytic mechanism of enzymes and to apply the recent developments in mass spectrometry/microfluidics based metabolomics and proteomics to improve our understanding of enzyme kinetics and signaling networks in the cellular context.
(III) Rapid enzyme kinetics to further our understanding of potential drug targets at molecular level; apply novel time-resolved mass spectrometry to study the kinetics of several enzymes for which current kinetic techniques/methods are limiting.
Recent Publications:
Furdui, C.M., Lew, E.D., Schlessinger, J., Anderson, K.S. Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol. Cell, 21(5):711-7, 2006.
Li, Z., Sau, A.K., Furdui, C. and Anderson K.S. “Probing the role of tightly bound phosphoenolpyruvate in E. coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase catalysis using time-resolved electrospray ionization mass spectrometry in the millisecond time range”, Analytical Biochemistry, 343(1):35-47, 2005.
Furdui, C., Sau, A., Baasov, T., Woodard, R.W. and Anderson, K.S. “The Use of (E)- and (Z)-[3F]-Phosphoenolpyruvate as Mechanistic Probes Reveals Significant Differences Between the Active Sites of 3-Deoxy-D-Manno-2-Octulosonate-8-Phosphate Synthase and 3-Deoxy-D-Arabino-2-Heptulosonate-7-Phosphate Synthase”, Biochemistry, 44(19):7326-35, 2005.
Furdui, C., Zhou, L., Woodard, R., and Anderson, K.S. “Insights into the Mechansim of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHP Synthase) (Phe) from E. coli Using a Transient Kinetic Analysis”, Journal of Biological Chemistry, 279(44):45618-25, 2004.
Furdui, C. and Ragsdale, S.W. “The Roles of CoASH in the Pyruvate:Ferredoxin Oxidoreductase Reaction Mechanism: Rate Enhancement by CoASH of Electron Transfer from a Radical Intermediate to an Iron-Sulfur Cluster”, Biochemistry, 41:9921-37, 2002.
Publications:
For a listing of additional publications, refer to PubMed, a service provided by the National Library of Medicine