ZMB Member Doris Hellerschmied-Jelinek
ZMB Member
Doris Hellerschmied-Jelinek
Next ZMB-Member
Prof. Dr. Doris Hellerschmied-Jelinek
Group
Mechanistic Cell BiologyCenter of Medical Biotechnology
University of Duisburg-Essen
Universitätsstr. 2
45141 Essen
- +49 201 183 3120
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- ZMB Research Program
Molecular and Chemical Cell Biology
Research Overview
Understanding how cells maintain homeostasis is critical to understanding cell survival during stress. Cells have to withstand stress from changing environmental conditions, such as temperature, pH, nutrient or oxygen supply, but also during cell differentiation and aging. Eukaryotic cells have evolved to use distinct cellular compartments, known as organelles, which maintain homeostatic mechanisms to ensure their distinct functionalities and overall cellular homeostasis. Within the secretory pathway, these stress response mechanisms have been extensively studied at the level of the endoplasmic reticulum (ER). In contrast, the mechanism(s) by which the Golgi apparatus deals with unfolded proteins and how it reacts to stress are only beginning to be unraveled.
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Publications
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Ubiquitin-mediated degradation at the Golgi apparatusIn: Frontiers in Molecular Biosciences Vol. 10 (2023) 1197921Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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Zellen unter Stress : Entspannung mit Hilfe von ProteinenIn: Unikate: Berichte aus Forschung und Lehre (2021) Nr. 56, Heft "Junge Wilde" - Die nächste Generation,Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosinIn: Nature Communications Vol. 10 (2019) Nr. 1, 4781Online Full Text: dx.doi.org/ (Open Access)
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Protein folding state-dependent sorting at the Golgi apparatusIn: Molecular Biology of the Cell Vol. 30 (2019) Nr. 17, pp. 2296 - 2308Online Full Text: dx.doi.org/ (Open Access)
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Targeted protein unfolding uncovers a Golgi-specific transcriptional stress responseIn: Molecular Biology of the Cell Vol. 29 (2018) Nr. 11, pp. 1284 - 1298Online Full Text: dx.doi.org/ (Open Access)
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UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteinsIn: Nature Communications Vol. 9 (2018) Nr. 1, 484Online Full Text: dx.doi.org/ (Open Access)
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Modular PROTAC Design for the Degradation of Oncogenic BCR-ABLIn: Angewandte Chemie International Edition Vol. 55 (2016) Nr. 2, pp. 807 - 810Online Full Text: dx.doi.org/
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The Nuclear Pore-Associated TREX-2 Complex Employs Mediator to Regulate Gene ExpressionIn: Cell Vol. 162 (2015) Nr. 5, pp. 1016 - 1028Online Full Text: dx.doi.org/ (Open Access)
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Myosin chaperonesIn: Current Opinion in Structural Biology Vol. 25 (2014) pp. 9 - 15Online Full Text: dx.doi.org/ (Open Access)
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The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegansIn: Cell Vol. 152 (2013) Nr. 1-2, pp. 183 - 195Online Full Text: dx.doi.org/ (Open Access)