ZMB Member Markus Kaiser
ZMB Member
Markus Kaiser
Next ZMB-Member
Prof. Dr. Markus Kaiser
Group
Chemical BiologyCenter of Medical Biotechnology (ZMB)
Faculty of Biology
University of Duisburg-Essen
Universitätsstr. 2
45141 Essen
- +49 201 183 4980
- Website
- Press Releases
- Selected Publications
- Publication Metrics
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- ZMB Research Program
Molecular and Chemical Cell Biology
Research Overview
The Kaiser group develops and uses chemical biology approaches to investigate diverse aspects of regulated proteolysis and to study the molecular mechanisms behind bioactive small molecule action. Our interests are however not limited to basic research; rather, we aim to capitalize on our scientific findings for drug discovery or other medicinal applications.
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Press Releases


Publication in Cell Chemical Biology New principle for treating tuberculosis
[26.07.2024] Researchers from Heinrich Heine University Düsseldorf (HHU) and the University of Duisburg-Essen (UDE) have together succeeded in identifying and synthesising a group of molecules that can act against the cause of tuberculosis in a new way. In the scientific journal Cell Chemical Biology, they describe that the so-called callyaerins act against the infectious disease by employing a fundamentally different mechanism compared to antibiotic agents used to date.


Veröffentlichung in „Cell“ Antibiotika der Zukunft
[30.06.2022] Bakterielle Infektionen führen jährlich zu hunderttausenden Todesfällen; verstärkt auftretende Antibiotikaresistenzen machen weltweite Pandemien immer wahrscheinlicher. Umso wichtiger ist die Erforschung alternativer Antibiotika. In einer im Fachmagazin Cell veröffentlichten Studie entwickelten Wissenschaftler:innen vom Forschungsinstitut für Molekulare Pathologie in Wien gemeinsam mit der Gruppe von UDE-Professor Dr. Markus Kaiser neuartige Wirkstoffe, sogenannte BacPROTACs. Sie können gezielt bakterielle Proteine abbauen und Bakterien somit unschädlich machen. Perspektivisch können sie gegen jedes bakterielle Protein gerichtet werden und stellen somit eine komplett neuartige Antibiotika-Klasse dar.
Selected Publications
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Molecular glues of the regulatory ChREBP/14-3-3 complex protect beta cells from glucolipotoxicityIn: Nature Communications Vol. 16 (2025) Nr. 1, 2110Online Full Text: dx.doi.org/ (Open Access)
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Extracellular plant subtilases dampen cold-shock peptide elicitor levelsIn: Nature Plants Vol. 10 (2024) Nr. 11, pp. 1749 - 1760Online Full Text: dx.doi.org/ (Open Access)
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Rational correction of pathogenic conformational defects in HTRA1In: Nature Communications Vol. 15 (2024) Nr. 1, 5944Online Full Text: dx.doi.org/ (Open Access)
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Subtilase SBT5.2 inactivates flagellin immunogenicity in the plant apoplastIn: Nature Communications Vol. 15 (2024) Nr. 1, 10431Online Full Text: dx.doi.org/ (Open Access)
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TopBP1 utilises a bipartite GINS binding mode to support genome replicationIn: Nature Communications Vol. 15 (2024) Nr. 1, 1797
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Clp-targeting BacPROTACs impair mycobacterial proteostasis and survivalIn: Cell Vol. 186 (2023) Nr. 10, pp. 2176 - 2192.e22Online Full Text: dx.doi.org/ (Open Access)
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The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPaseIn: Nature Communications Vol. 14 (2023) Nr. 1, 3258Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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BacPROTACs mediate targeted protein degradation in bacteriaIn: Cell Vol. 185 (2022) Nr. 13, pp. 2338 - 2353.e18Online Full Text: dx.doi.org/ (Open Access)
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Persister state-directed transitioning and vulnerability in melanoma
32. Deutscher Hautkrebskongress (ADO-Jahrestagung), 14.–17. September 2022, Hannover, Germany,In: Nature Communications Vol. 13 (2022) Nr. 1, pp. 35 - 36 -
Structure-based evolution of a promiscuous inhibitor to a selective stabilizer of protein–protein interactionsIn: Nature Communications Vol. 11 (2020) Nr. 1, pp. 3954Online Full Text: dx.doi.org/ (Open Access)
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An apoplastic peptide activates salicylic acid signalling in maizeIn: Nature Plants Vol. 4 (2018) Nr. 3, pp. 172 - 180Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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Ubiquitin-Independent Disassembly by a p97 AAA-ATPase Complex Drives PP1 Holoenzyme FormationIn: Molecular Cell Vol. 72 (2018) Nr. 4, pp. 766 - 777Online Full Text: dx.doi.org/ (Open Access)
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Activity-based protein profiling as a robust method for enzyme identification and screening in extremophilic ArchaeaIn: Nature Communications Vol. 8 (2017) pp. 15352Online Full Text: dx.doi.org/ (Open Access)
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VCP/p97 Extracts Sterically Trapped Ku70/80 Rings from DNA in Double-Strand Break RepairIn: Molecular Cell Vol. 64 (2016) Nr. 1, pp. 189 - 198Online Full Text: dx.doi.org/ (Open Access)
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Determinants of amyloid fibril degradation by the PDZ protease HTRA1In: Nature Chemical Biology Vol. 11 (2015) Nr. 11, pp. 862 - 869Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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A chemical inhibitor of jasmonate signaling targets JAR1 in Arabidopsis thalianaIn: Nature Chemical Biology Vol. 10 (2014) Nr. 10, pp. 830 - 836Online Full Text: dx.doi.org/
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HTRA proteases : regulated proteolysis in protein quality controlIn: Nature Reviews Molecular Cell Biology Vol. 12 (2011) Nr. 3, pp. 152 - 162Online Full Text: dx.doi.org/
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A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanismIn: Nature Vol. 452 (2008) pp. 755 - 758
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β-lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana.In: Nature Chemical Biology Vol. 4 (2008) Nr. 9, pp. 557 - 563