Prof. Dr. Jörg Tatzelt

Institute of Biochemistry and Pathobiochemistry
Biochemistry of Neurodegenerative Dieseases
Tel.: +49-(0)234-32-22429


Various approaches coming from neuropathology, genetics, animal modeling and biophysics have established a crucial role of protein misfolding in the pathogenic process of different neurodegenerative diseases, such as Alzheimer's disease, Parkinson’s disease, polyglutamine expansion diseases and prion diseases. However, there is an ongoing debate about the nature of the harmful proteinaceous species and how toxic conformers selectively damage neuronal populations.

The main aim of our biochemical research is to identify cellular factors and signaling cascades implicated in neuronal integrity and in the pathophysiological alterations leading to neurodegeneration. Our integrative research has a strong focus on the biochemical and cell biological analysis of cellular pathways, which are also of broad neurobiological interest. Specifically, we are employing in vitro, neuronal cell culture, and animal models to focus on four major topics:

  • Cellular mechanisms underlying the formation and toxic activity of aberrant protein conformers
  • Liquid-liquid phase separation and neurodegeneration
  • Signaling pathways induced by neurotoxic conformers
  • Therapeutic strategies for neurodegenerative diseases



  • We have an open PhD position embedded in the interdisciplinary program of the International Max Planck Research School for Living Matter (IMPRS-LM). - Please apply here!
  • Signaling in the immune and nervous systems using NEMO - Read more

Recent Publications

  • Polido SA, Stuani C, Voigt A, Banik P, Kamps J, Bader V, Grover P, Krause LJ, Zerr I, Matschke J, Glatzel M, Winklhofer KF, Buratti E, Tatzelt J. (2023) Cross-seeding by prion protein inactivates TDP-43. Brain 2023 Sep 5. doi: 10.1093/brain/awad289
  • Goel S, Oliva R, Jeganathan S, Bader V, Krause LJ, Kriegler S, Stender ID, Christine CW, Nakamura K, Hoffmann JE, Winter R, Tatzelt J*, Winklhofer KF* (2023) Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling. Life Sci Alliance Jan 31, 2023. doi: 10.26508/lsa.202201607
    * - corresponding author
  • Wu Z, Berlemann LA, Bader V, Sehr DA, Dawin E, Covallero A, Meschede J, Angersbach L, Showkat C, Michaelis JB, Münch C, Rieger B, Namgaladze D, Herrera MG, Fiesel FC, Springer W, Mendes M, Stepien J, Barkovits K, Marcus K, Sickmann A, Dittmar G, Busch KB, Riedel D, Brini M, Tatzelt J, Cali T, Winklhofer KF. (2022) LUBAC assembles a ubiquitin signaling platform at mitochondria for signal amplification and transport of NF-κB to the nucleus. EMBO J. 18: e112006. doi: 10.15252/embj.2022112006.

  • Polido SA, Kamps J, Tatzelt J. (2021) Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid-Liquid Phase Separation. Biomolecules 12; 11(8):1201. doi: 10.3390/biom11081201

  • Kamps J,Lin YH, Oliva R, Bader V, Winter R, Winklhofer KF, Tatzelt J. (2021) The N-terminal domain of the prion protein is required and sufficient for liquid-liquid phase separation: A crucial role of the Aβ-binding domain. J Biol Chem 6; 297(1): 100860. doi: 10.1016/j.jbc.2021.10086