Janna Kiselar, PhD is an Assistant Professor of the Department of Nutrition and Associate Director of the CCC Case Proteomics SR at Case Western Reserve University. Dr. Kiselar has a national reputation in the field of covalent labeling/MS research and structural biology with over 40 publications. She has over twenty years of experience in the field of mass spectrometry, proteomics and structural biology. Dr. Kiselar’s contributions to science highlight her long-standing track record of developing innovative methodology in immunology for studding antigen-antibody interactions, mass spectrometry-based protein footprinting a well-known and popular MS-based technology for examining protein structure and dynamics, and qualitative and quantitative mass spectrometry and proteomics. Recently, she pioneered major technical advances in mass spectrometry-based protein footprinting that revolutionized impact of protein footprinting on biology and biophysics. This includes introducing single residue-based hydroxyl radical footprinting (HRF) methods which have allowed us to study historically-challenging problems in structural biology such as the interactions of amyloidogeneic proteins and intrinsically disordered proteins, and identification of drug target binding sites for both small molecules and biologics that often cannot be addressed by other structural techniques.
As the Associate Director of the Proteomics SR for Case Comprehensive Cancer Center and P30 grant Co-director, Dr. Kiselar facilitated successful collaboration with many PIs from Case Western Reserve University and nationwide to drive the development of new biomarkers and therapeutics in cancer that resulted in high impact publications in Cell, JCI, Nature Com., Science Advances and PNAS.
Teaching Information
Courses Taught
Office Hours
9am-6pm
Research Information
Research Projects
- Developing multiplex labeling chemistry methods for protein footprinting
- Structural Characterization of TAU in rapidly progressive Alzheimer’s disease
- Structural Characterization of major differences of prions strains that correlate with distinct inactivation susceptibility of a given human prion strain. This work is a critical step for identifying sites of structural importance in prion that can be targeted for drug development.
- Mapping protein-protein/ligand interactions of the large protein complexes including chromatin remodeling complex using protein footprinting
Recent Funding
R01GM141078 (Kiselar)
4/1/2021-03/31/2025
NIH
Multiplex labeling chemistry methods for protein footprinting
Role: PD/PI
R01NS103848 (Safar)
05/01/2018-1/31/2023
NIH
Replication mechanism of human prions
Role: Co-Investigator
RF1AG058267 (Safar, Haines Wisniewski)
7/1/2017-6/30/2022
NIH
Characterization of rapidly progressive Alzheimer’s disease.
Role: Co-Investigator
Air Force Research Laboratory (PI: Chance)
07/01/2021-06/30/2022
Nano-Biomaterials Consortium
The Case Center for Biomolecular Structure and Integration for Sensors (BioSIS) will undertake, in collaboration with the Air Force, a multi-year, interdisciplinary effort to identify and optimize key biomarker and recognition element pairs, develop and optimize devices suited to those pairs, and test those devices with realistic samples.
Role: co-Investigator
2P30 CA043703-28 (Gerson, PI)
08/01/97-03/31/23
NIH/NCI
Case Comprehensive Cancer Center Support Grant
Co-Director, Proteomics Shared Resource
RF1AG061797 (Surewicz)
09/30/18-6/30/2023
NIH
Structural determinants of amyloid strain heterogeneity in distinct phenotypes of Alzheimer's disease
Role: Co-Investigator
Awards and Honors
Publications
Selected Publications
- M K Siddiqi, C Kim, T Haldiman, M Kacirova, B Wang, J. Bohon, M R. Chance, J. Kiselar and J G. Safar. (2021) Structurally distinct external domains drive replication of major human prions. PLOS Pathogens. 2021 Jun 17;17(6):e1009642. doi: 10.1371/journal.ppat.1009642. eCollection 2021 Jun. PMID: 34138981
- Huang W, Peng Y, Kiselar J, Zhao X, Albaqami A, Mendez D, Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S. Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains. Nat Commun. 2018;9 (1):3520
- McClinch K, Avelar RA, Callejas D, Izadmehr S, Wiredja D, Perl A, Sangodkar J, Kastrinsky DB, Schlatzer D, Cooper M, Kiselar J, Stachnik A, Yao S, Hoon D, McQuaid D, Zaware N, Gong Y, Brautigan DL, Plymate SR, Sprenger CCT, Oh WK, Levine AC, Kirschenbaum A, Sfakianos JP, Sears R, DiFeo A, Ioannou Y, Ohlmeyer M, Narla G, Galsky MD. Small-Molecule Activators of Protein Phosphatase 2A for the Treatment of Castration-Resistant Prostate Cancer. Cancer Res. 2018;78(8):2065-80. Epub 2018/01/24. doi: 10.1158/0008-5472.CAN-17-0123. PubMed PMID: 29358171; PMCID: PMC5899650.
- Kiselar J, Chance MR. High-Resolution Hydroxyl Radical Protein Footprinting: Biophysics Tool for Drug Discovery. Annu Rev Biophys. 2018. Epub 2018/03/15. doi: 10.1146/annurev-biophys-070317033123. PubMed PMID: 29539273.
- 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. PMCID: PMC153027.