Dr. Erdem Tamguney
Group Leader
German Center for Neurodegenerative Diseases (DZNE)
Building 344, BMZ 1
Sigmund-Freud-Str. 25
53127 Bonn
erdem(at)dzne.de
+49 (0) 228 / 287-52131
More information
Areas of investigation/research focus
Dementing diseases such as Alzheimer’s disease (AD), Parkinson’s disease (PD), and prion diseases have in common that naturally occurring proteins of the nervous system misfold and accumulate in the brains of patients, eventually leading to neuronal degeneration and death. It is not clear why these proteins misfold and accumulate in the brain, why neurons die in the presence of protein aggregates, nor how this could be prevented. Using cell culture and disease models, we seek to understand the underlying mechanisms that lead to protein misfolding in the brain and the ensuing neuropathology. In contrast to AD and PD, prions accumulate very rapidly in the brains of patients once clinical symptoms show. Thus cell and disease models of prion disease are very useful to study protein misfolding, the ‘invasive’ nature of aberrantly folded proteins, and their toxic effect on neurons and neuronal plasticity.
Our goals are
- to identify early pathologic processes in the brain that cause protein misfolding and neuronal loss
- to discover early markers that signal these pathological changes
- to develop therapeutic interventions that prevent protein misfolding and neuronal loss
Publications
Salivary prions in sheep and deer.
G Tamgüney, JR Richt, AN Hamir, JJ Greenlee, MW Miller, LL Wolfe, TM Sirochman, AJ Young, DV Glidden, NL Johnson, K Giles, SJ DeArmond, SB Prusiner SB (2011), Prion, in press. DOI: 10.4161/pri.6.1.16984
Asymptomatic deer excrete infectious prions in feces.
G Tamgüney, MW Miller, LL Wolfe, TM Sirochman, DV Glidden, C Palmer, A Lemus, SJ DeArmond, SB Prusiner (2009), Nature 461, 529-32.
Measuring prions by bioluminescence imaging.
G Tamgüney, KP Francis, K Giles, A Lemus, SJ DeArmond, SB Prusiner SB (2009), Proc Natl Acad Sci U S A 106, 15002-6.
Transmission of scrapie and sheep-passaged bovine spongiform encephalopathy prions to transgenic mice expressing elk prion protein.
GTamgüney, MW Miller, K Giles, A Lemus, DV Glidden, SJ DeArmond, SB Prusiner (2009), J Gen Virol 90, 1035-47.
Genes contributing to prion pathogenesis.
G Tamgüney, K Giles, DV Glidden, P Lessard, H Wille, P Tremblay, DF Groth, F Yehiely, C Korth, RC Moore, J Tatzelt, E Rubinstein, C Boucheix, X Yang, P Stanley, MP Lisanti, RA Dwek, PM Rudd, J Moskovitz, CJ Epstein, T Dawson Cruz, WA Kuziel, N Maeda, J Sap, K Hsiao Ashe, GA Carlson, I Tesseur, T Wyss-Coray, L Mucke, KH Weisgraber, RW Mahley, FE Cohen, SB Prusiner (2008), J Gen Virol 89, 1777-88.
Transmission and detection of prions in feces.
JG Safar, P Lessard, G Tamgüney, Y Freyman, C Deering, F Letessier, SJ DeArmond, SB Pusiner (2008), J Infect Dis 198, 81-9.
Transmission of elk and deer prions to transgenic mice.
G Tamgüney, K Giles, E Bouzamondo-Bernstein, PJ Bosque, MW Miller, J Safar , SJ DeArmond, SB Prusiner (2006), J Virol 80, 9104-14.
Autocrine stimulation of rhadinovirus-transformed T cells by the chemokine CCL1/I-309.
G Tamgüney, J van Snick, H Fickenscher (2004), Oncogene 23, 8475-85.
Downregulation of p56lck kinase activity in T cells of squirrel monkeys (Saimiri sciureus) correlates with the non-transforming and apathogenic properties of herpesvirus saimiri in its natural host.
T Greve*, G Tamgüney*, B Fleischer, H Fickenscher, BM Bröker (2001), J Virol 75, 9252-61. (*equal contribution).
Identification of leptin in human saliva.
M Gröschl, M Rauh, R Wagner, W Neuhuber, M Metzler, G Tamgüney, J Zenk, E Schoof, HG Dörr, WF Blum, W Rascher, J Dötsch (2001), J Clin Endocrinol Metab 86, 5234-9.
Herpesvirus saimiri pathogenicity enhanced by thymidine kinase of herpes simplex virus.
C Hiller, G Tamgüney, N Stolte, K Mätz‑Rensing, D Lorenzen, S Hör, M Thurau, S Wittmann, S Slavin, H Fickenscher (2000), Virology 278, 445‑55.