Paul T Kotzbauer, MD, PhD

Associate Professor of Neurology

Phone314-362-7165

Fax314-362-2244

Emailkotzbauerp@neuro.wustl.edu

Additional Titles

  • Assistant Professor, Molecular Biology and Pharmacology

Board Certifications

  • Neurology - Certified

Related Links

Recognition

  • James L. O’Leary Prize for Research in Neuroscience, Washington University School of Medicine, 1996
  • Spencer T. and Ann W. Olin Fellowship, Washington University School of Medicine, 1995

Publications

  • Armstrong RA, Kotzbauer PT, Perlmutter JS, Campbell MC, Hurth KM, Schmidt RE, Cairns NJ. A quantitative study of α-synuclein pathology in fifteen cases of dementia associated with Parkinson disease. J Neural Transm. 2014 Feb;121(2):171-81.
  • Bagchi DP, Yu L, Perlmutter JS, Xu J, Mach RH, Tu Z, Kotzbauer PT. Binding of the radioligand SIL23 to α-synuclein fibrils in Parkinson disease brain tissue establishes feasibility and screening approaches for developing a Parkinson disease imaging agent. PLoS One. 2013;8(2):e55031.
  • Holmes BB, DeVos SL, Kfoury N, Li M, Jacks R, Yanamandra K, Ouidja MO, Brodsky FM, Marasa J, Bagchi DP, Kotzbauer PT, Miller TM, Papy-Garcia D, Diamond MI. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci U S A. 2013 Aug 13;110(33):E3138-47.
  • Racette BA, Criswell SR, Lundin JI, Hobson A, Seixas N, Kotzbauer PT, Evanoff BA, Perlmutter JS, Zhang J, Sheppard L, Checkoway H. Increased risk of parkinsonism associated with welding exposure. Neurotoxicology. 2012 Oct;33(5):1356-61.
  • Kotzbauer PT, Cairns NJ, Campbell MC, Willis AW, Racette BA, Tabbal SD, Perlmutter JS. Pathologic accumulation of α-synuclein and Aβ in Parkinson disease patients with dementia. Arch Neurol. 2012 Oct;69(10):1326-31.
  • Yu L, Cui J, Padakanti PK, Engel L, Bagchi DP, Kotzbauer PT, Tu Z. Synthesis and in vitro evaluation of α-synuclein ligands. Bioorg Med Chem. 2012 Aug 1;20(15):4625-34.
  • Engel LA, Jing Z, O’Brien DE, Sun M, Kotzbauer PT. Catalytic function of PLA2G6 is impaired by mutations associated with infantile neuroaxonal dystrophy but not dystonia-parkinsonism. PLoS One. 2010 Sep 23;5(9):e12897.
  • Li M, Husic N, Lin Y, Christensen H, Malik I, McIver S, LaPash Daniels CM, Harris DA, Kotzbauer PT, Goldberg MP, Snider BJ. Optimal promoter usage for lentiviral vector-mediated transduction of cultured central nervous system cells. J Neurosci Methods. 2010 May 30;189(1):56-64.
  • Gregory A, Westaway SK, Holm IE, Kotzbauer PT, Hogarth P, Sonek S, Coryell JC, Nguyen TM, Nardocci N, Zorzi G, Rodriguez D, Desguerre I, Bertini E, Simonati A, Levinson B, Dias C, Barbot C, Carrilho I, Santos M, Malik I, Gitschier J, Hayflick SJ. Neurodegeneration associated with genetic defects in phospholipase A(2). Neurology. 2008 Oct 28;71(18):1402-9.
  • Gao HM, Kotzbauer PT, Uryu K, Leight S, Trojanowski JQ, Lee VM. Neuroinflammation and oxidation/nitration of alpha-synuclein linked to dopaminergic neurodegeneration. J Neurosci. 2008 Jul 23;28(30):7687-98.
  • Malik I, Turk J, Mancuso DJ, Montier L, Wohltmann M, Wozniak DF, Schmidt RE, Gross RW, Kotzbauer PT. Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystrophy caused by PLA2G6 mutations. Am J Pathol. 2008 Feb;172(2):406-16.
  • Liang TW, Truax AC, Trojanowski JQ, Lee VM, Stern MB, Kotzbauer PT. Partial deficit of pantothenate kinase 2 catalytic activity in a case of tremor-predominant neurodegeneration with brain iron accumulation. Mov Disord. 2006 May;21(5):718-22.
  • Kotzbauer PT, Holtzman DM. Expectations and challenges in the therapeutic use of neurotrophic factors. Ann Neurol. 2006 Mar;59(3):444-7. No abstract available.
  • Kotzbauer PT, Truax AC, Trojanowski JQ, Lee VM. Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2. J Neurosci. 2005 Jan 19;25(3):689-98.
  • Kotzbauer PT, Giasson BI, Kravitz AV, Golbe LI, Mark MH, Trojanowski JQ, Lee VM. Fibrillization of alpha-synuclein and tau in familial Parkinson’s disease caused by the A53T alpha-synuclein mutation. Exp Neurol. 2004 Jun;187(2):279-88.

Our research is focused on Parkinson’s disease and a group of related neurodegenerative disorders caused by PLA2G6 gene mutations. Accumulation of aggregated alpha-synuclein protein within neuronal inclusions called Lewy bodies and Lewy neurites is the hallmark pathological change in Parkinson’s disease. A central role for alpha-synuclein in pathogenesis is supported by the previous identification of dominantly-inherited alpha-synuclein gene mutations in rare familial forms of PD. PD typically causes progressive motor impairment but also can cause cognitive impairment. Disease progression is associated with progressive involvement of cortical and subcortical brain regions with pathological alpha-syn accumulation.