Jorg Tatzelt

Professor/ head of department

Ruhr-Universität Bochum Medizinische Fakultät

Germany

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Jorg Tatzelt is a Professor and head of the department at Ruhr-Universität Bochum Medizinische Fakultät in Germany. His research focuses on neurodegenerative diseases, prion proteins, and the mechanisms of protein aggregation and phase separation. Recent articles include studies on the interactions of the prion protein with α-Synuclein and the role of certain mutations in neuronal development associated with autism.

Articles (21)

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2025

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2024

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2021

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2021

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2021

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2020

Collaborators (9)

Emiliano Biasini

Assistant Professor

Università degli Studi di Torino

ITALY

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Rune Busk Damgaard

Technical University of Denmark

DENMARK

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Konstanze F Winklhofer

GERMANY

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Julia E. Neumann

Prof. Dr. med.

University Medical Center Hamburg-Eppendorf

GERMANY

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Jan-Erik Hoffmann

Head of Biological Applications

GERMANY

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Hermann Altmeppen

University Medical Center Hamburg-Eppendorf (UKE)

GERMANY

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Luise Linsenmeier

MSH Medical School Hamburg University of Applied Sciences and Medical University

GERMANY

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Karl Frontzek

University College London

UNITED KINGDOM

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Benjamin Englert

University of Helsinki

FINLAND

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Jorg Tatzelt

Research Interests

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About

Articles (21)

Soluble N-Terminal Domain of the Prion Protein Interferes with Fibrillization of α-Synuclein to Form Off-Pathway Assemblies that Lack Cellular Seeding Activity

Sex-specific perturbations of neuronal development caused by mutations in the autism risk gene DDX3X.

Topological confinement by a membrane anchor suppresses phase separation into protein aggregates: Implications for prion diseases

Cleavage site-directed antibodies reveal the prion protein in humans is shed by ADAM10 at Y226 and associates with misfolded protein deposits in neurodegenerative diseases

Liquid–liquid phase separation of the prion protein is regulated by the octarepeat domain independently of histidines and copper

VCP/p97 mediates nuclear targeting of non-ER-imported prion protein to maintain proteostasis

Cover Feature: Morphological Transformations of SARS‐CoV‐2 Nucleocapsid Protein Biocondensates Mediated by Antimicrobial Peptides (Chem. Eur. J. 29/2024)

Morphological Transformations of SARS-CoV-2 Nucleocapsid Protein Biocondensates Mediated by Antimicrobial Peptides.

Regulated Proteolysis Induces Aberrant Phase Transition of Biomolecular Condensates into Aggregates: A Protective Role for the Chaperone Clusterin.

Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling.

NEMO reshapes the protein aggregate interface and promotes aggrephagy by co-1 condensation with p62

Hydration makes a difference! How to tune protein complexes between liquid–liquid and liquid–solid phase separation

LUBAC assembles a ubiquitin signaling platform at mitochondria for signal amplification and transport of NF-κB to the nucleus.

Bivalent metal ions induce formation of α-synuclein fibril polymorphs with different cytotoxicities.

Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies

Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid–Liquid Phase Separation

Remodeling of the Fibrillation Pathway of α-Synuclein by Interaction with Antimicrobial Peptide LL-III.

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

The key role of solvent in condensation: Mapping water in liquid-liquid phase-separated FUS

The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.

SecY-mediated quality control prevents the translocation of non-gated porins

Collaborators (9)

Emiliano Biasini

Rune Busk Damgaard

Konstanze F Winklhofer

Julia E. Neumann

Jan-Erik Hoffmann

Hermann Altmeppen

Luise Linsenmeier

Karl Frontzek

Benjamin Englert

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