Janna Kiselar, Ph.D.
Case Western Reserve University
Center for Proteomics
10900 Euclid Ave., BRB 934
Cleveland, OH 44106-4988
Phone: (216) 368-0979
Fax: (216) 368-6846
Email: janna.kiselar@case.edu
Faculty Appointments
Case Center for Proteomics (Assistant Director, Instructor)
Academic History
| 1987-1993 | M.S., Medical Biochemistry, Moscow State Medical University, Russia |
| 1993-1997 | Ph.D., Biochemistry, Institute of Biomedical Chemistry, Moscow, Russia |
| 1997-2003 | Post-Doc, Proteins & Mass Spectrometry, Albert Einstein College of Medicine, Bronx, NY |
Positions and Employment
| 2004-2005 | Associate, Proteins & Mass Spectrometry, Albert Einstein College of Medicine, Bronx, NY |
| 2005- | Instructor, Proteins & Mass Spectrometry, Case Western Reserve University, Cleveland, OH |
Honors
| 1995-1996 | J. Soros award for the best Scientist’s research. Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, Russia. |
| 1997- | American Society of Mass Spectrometry |
| 2005 | Second best poster, awarded with the free registration for the 8th International meeting on mass Spectrometry in the Health and Life Sciences. |
Research
My research is focused on two primary areas:
- Development of a new sensitive quantitative approach (SRM) for protein footprinting in order to improve detection and quantitation of oxidized products that are present in less then 1% of the unmodified peptide and remained undetected in the current analysis. Hydroxyl radical-mediated protein footprinting in combination with mass spectrometry has recently been developed to define protein structure, protein folding, and protein-protein and protein-DNA interactions in solution. This method is based on the measurement of the reactivity of amino acid side-chain groups with hydroxyl radicals resulting in covalent modification (oxidation) of these residues according to their solvent accessibility. Digested protein then analyzed by mass spectrometry for the sites of oxidation.
- Developing and implementing new mass spectrometry based approaches for examining the post-translational modifications of proteins. Post-translational modifications (PTMs) are covalent modification of the proteins after its translation. PTMs have been shown to be important features for regulating protein functions, determining their activity state, cellular location and dynamic interaction with other proteins. Because they are present in substoichiometric amounts on protein molecules, the comprehensive analysis has some analytical limitations.
Instrument Training
I offer training courses for CWRU users on mass spectrometry instruments including prOTOF, LTQ, Deca XP.
Recent Publications
- Strachen, R.T, Sheffler, D.J, Willard, B., Kinter, M., Kiselar, J.G,, Roth BL. (2008) Ribosomal S6 kinase 2 directly phosphorylates the 5-HT2A serotonin receptor thereby modulating 5-HT2A signaling. J Biol Chem., in press.
- Takamoto, K. and Kiselar J. (2008) “Covalent Labeling Methods for Examining Protein Structure and Protein Interaction”, chapter from “Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics” Wiley, New Jersey, pp 45-68
- Gupta S, Sullivan M, Toomey J, Kiselar J, Chance MR. (2007) The Beamline X28C of the Center for Synchrotron Biosciences: a national resource for biomolecular structure and dynamics experiments using synchrotron footprinting. J Synchrotron Radiat., May;14(Pt 3), 233-243
- Kiselar J.G., Mahaffy R., Pollard T.D., Almo S.C., and Chance M.R. (2007) Arp2/3 activation mediated by binding of nucleotides and WASp: Structural mass spectrometry approaches to large macromolecular complexes. Proc Natl Acad Sci U S A.,104, 1552-1557.
- Guozhong Xu, Janna Kiselar, Qin He, and Mark R. Chance (2005) Secondary reactions and strategies to improve quantitative protein footprinting, Anal. Chem., 77, 3029-3037.
- Kiselar J. G., Janmey P. A., Almo S. C., and Chance M. R. (2003) Structural analysis of gelsolin using synchrotron protein footprinting. Mol. & Cell Proteom., 2.10, 1120-1132.
- Kiselar J. G., Janmey P. A., Almo S. C., and Chance M. R. (2003) Visualizing the Ca2+ dependent activation of gelsolin using synchrotron footprinting. Proc Natl Acad Sci U S A., 100, 3942-3947.