Erdem Tamgüney, Prof. Dr. (PhD)
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Affiliation(s):
Heinrich-Heine University Düsseldorf; Insitute for Biological Information Processing (Structural biochemistry) IBI-7
ORCID URL:
Areas of Interest:
Protein misfolding diseases; Neurodegeneration; Prions; Amyloid; Molecular Biology; alpha-Synuclein; Synucleinopathies; Parkinson's disease; Multiple System Atrophy
Biography & Research:
Erdem Gültekin Tamgüney, Ph.D., holds a dual affiliation and is a Professor for Protein Misfolding and Neurodegeneration at the Institute for Physical Biology at the Heinrich-Heine University Düsseldorf and the Institute for Information Processing – Structural Biochemistry (IBI-7) at the Forschungszentrum Jülich in Germany. He obtained his Ph.D. in Virology from the Friedrich-Alexander University of Erlangen-Nuremberg in 2001 and received a postdoctoral fellowship at the Institute for Neurodegenerative Diseases at the University of California, San Francisco (UCSF), where he laid the foundation for his observations of cellular misfolding and systemic propagation of prions. Dr. Tamgüney is a past recipient of a Ph.D. fellowship of the Boehringer Ingelheim Fonds and a postdoctoral fellowship of the Larry L. Hillblom Foundation. He discovered the fecal-to-oral transmission mechanism for prions causing chronic wasting disease in deer and elk as an Assistant Professor at UCSF. From 2011–2019 Dr. Tamgüney was an independent research group leader at the German Center for Neurodegenerative Diseases (DZNE) in Bonn, Germany, where he became interested in alpha-synuclein and its prion-like behavior in Parkinson’s disease and related synucleinopathies. In 2017 Dr. Tamgüney was awarded the AD/PD Junior Faculty Award for his discovery that alpha-synuclein prions can neuroinvade the CNS from peripheral tissues. Dr. Tamgüney’s research is primarily focused on the diagnosis, treatment, and prevention of synucleinopathies. He is currently developing a diagnostic assay for the detection of alpha-synuclein aggregates in body fluids, compounds inhibiting alpha-synuclein aggregation, and vaccines preventing aggregation-associated neurodegeneration.
