Neena Singh, M.D., Ph.D. Professor Mailing Address: 2103 Cornell Rd. WRB 5128 Cleveland, OH 44106-7288 phone: (216) 368-2617 fax: (216) 368-0494 email: Neena.Singh@Case.edu

Biography
Academic Background

1982	Specialization in Anatomic and Clinical Pathology (M.D), Maulana Azad Medical College, New Delhi, India
1990	Ph.D. in Cell Biology, Case Western Reserve University, Cleveland, Ohio

Academic/Professional Experience

1990-1993	Residency in Clinical Pathology, University Hospitals, Cleveland, Ohio
1992-1995	Post-doctoral Research Fellowship, Case Western Reserve University, Cleveland, Ohio. (Funded by the National Institutes of Health)
1993	Visiting scholar, Department of Pediatrics and Biochemistry, Amsterdam Medical Center, The Netherlands
1994	Fellowship in Immunopathology, University Hospitals, Cleveland, Ohio.
1994-2001	Assistant Professor, Department of Pathology, Case Western Reserve University, Cleveland, Ohio
2001-2011	Associate Professor, Department of Pathology, Case Western Reserve University, Cleveland, Ohio
2011-present	Professor, Departments of Pathology and Neurology, Case Western Reserve University, Cleveland, Ohio

Research
Research in my laboratory is directed at understanding the role of iron, copper, and zinc in the pathogenesis of neurodegenerative conditions of protein misfolding such as sporadic Creutzfeldt-Jakob disease (sCJD), Alzheimer's disease (AD), Parkinson's disease (PD), and Huntington's disease (HD). Ongoing investigations are focused on the function of prion protein in systemic and brain iron metabolism, the cross-talk between prion protein and Alzheimer precursor protein and A-beta, and the underlying cause of iron imbalance in sCJD and AD brains. Considerable effort is being directed at developing a disease-specific pre-mortem diagnostic test for sCJD and AD based on the change in brain iron status with disease progression. The ultimate goal is to identify common pathogenic processes leading to metal dyshomeostasis in sCJD, AD, PD, and HD, and to develop therapeutic strategies based on restoring metal homeostasis in diseased brains.

A variety of experimental systems are used for these studies, including primary and transformed cells of neuronal, hematopoietic, hepatic, and intestinal origin transfected to express relevant proteins, C. elegans models expressing normal and mutant prion protein, and mouse models representing these disorders. Adequate training and safe facilities for performing the studies are accessible.

Publications
Mishra, R.S., Basu, S., Gu, Y., Luo, X., Zou, W., Mishra, R., Li, R., Chen, S.G., Gambetti, P., Fujioka, H., and Singh, N. (2004) Protease resistant human prion protein and ferritin are co-transported across Caco-2 epithelial cells: Implications for species barrier in prion uptake from the intestine. J. Neurosci. 24:11280-11290.
Featured in "This week in the Journal" in J. Neurosci.(Vol. 24 p0), News@nature.com, BBC news.com, MSNBC news.com, and other local, national, and international news agencies. Featured in Lancet Neurology (Vol. 4, p81), JAMA (Vol. 293: p285)

Basu, S., Mohan, M.L., Luo, X., Kundu, B., Kong, Q., and Singh, N. (2007) Modulation of PK-resistant PrPSc in cells and infectious brain homogenate by redox-iron: Implications for prion replication and disease pathogenesis. Mol Biol Cell. 18: 3302-3312.

Singh, A, Mohan, M.L., Isaac, Alfred O., Luo, X., and Singh, N. (2009) Prion protein modulates cellular iron metabolism: Implications for prion disease pathogenesis. PLoS ONE 4: e4468. PMCID: PMC2637434

Singh, A., Isaac, A.O., Luo, X., Mohan, M.L., Bartz, J., Kong, K., Cohen, M., and Singh, N. (2009) Abnormal brain iron homeostasis in human and animal prion disorders. PLoS Pathogens 5:e1000336. PMCID: PMC2652663.
Selected as 'Featured Research' in February 2009 issue of Plos Pathogens, and cited by several local, National, and International news agencies. Featured in 'Nature Journal club' ( 460: 669, 2009).

Singh, A., Kong, Q., Luo, X., Petersen, R.B., Meyerson, H., and Singh, N. (2009) Prion protein knock-out mice show altered iron metabolism: A functional role for PrP in iron metabolism. Plos ONE 4:e6115. PMID: 19568430. PMCID:PMC2699477.
Published in the autumn 2009 issue of Prion Science. Prionics AG 15.

Singh, N., Singh, A., Das, D., and Mohan, M.L. (2010) Redox control of prion and disease pathogenesis. Antioxid Redox Signal. 12:1271-94.

Singh, N., Das, D., Singh, A., and Mohan, M.L. (2009) Prion protein and metal interactions: physiological and pathological implications. Curr. Issues Mol. Biol. 12:99-108.

Das, D., Luo, X., Singh, A., Gu, Y., Ghosh, S., Mukhopadhyay, C., Chen, SG, Sy, M-S, Kong, Q, and Singh, N. (2010) Paradoxical role of prion protein aggregates in redox-iron induced toxicity. PLoS ONE, 5: e11420. doi:10.1371/journal.pone.0011420.

Singh, A., Beveridge, AJ., and Singh, N. (2011) CSF transferrin is down-regulated in sCJD: a potential pre-mortem diagnostic test for prion disorders. PloS ONE, 6(3): e16804. doi:10.1371/journal.pone.0016804. Selected for press release by the journal.
This paper was cited by several news agencies.

Singh, A., Qing, L., Kong, Q., and Singh, N. (2011) Aggregation of ferritin contributes to brain iron dyshomeostasis in prion disorders. Neurobiology of disease, Published ahead of print.