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Profil • Service


  • Since 2021: Professor of Biochemistry
  • Since 2019: Project leader in the DFG-funded GRK 2155 ProMoAge.
  • Since 2018: Principal investigator at the Institute of Physiological Chemistry, Medical Faculty, Martin Luther University Halle-Wittenberg.
  • 2016 – 2018: Celgene Fellow, Department of Oncology, Medical Faculty, University of Oxford, United Kingdom.
  • Since 2016: Associated Fellow of the Higher Education Academy (AFHEA), University of Oxford, United Kingdom.
  • 2013 – 2016:  Fulford Junior Research Fellow in Medicine, Somerville College, University of Oxford, United Kingdom.
  • 2011 – 2013: EMBO long-term Fellow, Department of Oncology, Medical Faculty, University of Oxford, United Kingdom.
  • 2005 – 2007:  PhD Kekulé Fellow, Funds of the Chemical Industry, Germany.
  • 2005 – 2010: Graduate studies at the Max Planck Institute of Biochemistry, PhD in Biochemistry from the Ludwig Maximilian University in Munich, Germany, about structural determinants underlying the cytotoxic effects of aggregating proteins.
  • 1999 – 2004:  Biochemistry and Molecular Biology, University of Hamburg, Diploma thesis in tumour biology at the Institute of Clinical Chemistry/Central Laboratory, Medical Faculty, University Hospital Hamburg-Eppendorf, Germany.



Protein folding is one of the fundamental processes in life, and therefore needs to be tightly regulated. Many cellular protein quality control (PQC) systems are in place to ensure that protein homeostasis (proteostasis) is optimally adjusted for a changing environment, facilitating protein biogenesis, folding, translocation and degradation. Among these systems are the molecular chaperones and the major protein degradation machineries, namely the ubiquitin proteasome system and autophagy. However, as a result of ageing, mutations or exogenous influences, the capacity of the PQC systems can be exhausted and protein misfolding and aggregation, including the formation of amyloids, can occur. There are many known diseases in which protein misfolding and aggregation is the underlying cause of the pathological conditions; these are referred to as proteinopathies and include neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease and Huntington’s disease. Scientists in the group of Heidi Olzscha aim to understand the underlying mechanisms of PQC systems, in particular Ubiquitin-like domain (UBL) containing proteins and find approaches to prevent cytotoxicity due to protein misfolding. Over the last decade, it has become clear that posttranslational modifications (PTMs) can govern and modulate protein folding, and that aberrant PTMs can cause or contribute to proteinopathies. The scientists also study the influence of PTMs, especially ubiquitination, acetylation and citrullination, and how they affect the PQC systems as well as the turnover and interactors of proteins prone to misfolding.


Collaboration in the field of protein folding, misfolding, proteinopathies, neurodegenerative diseases, posttranslational modifications, proteostasis, ubiquitin proteasome system


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