Author

Stephan Kiontke

Philipps University of MarburgORCID 0000-0001-5822-913XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Research Focus:differential expression· 1 Assay:metabolomics· 1

Frequent Co-Authors

Gert BangeiD· 3 shared Fabiana BurchertiD· 2 shared Paul Stanley WeilandiD· 2 shared Victor ZegarraiD· 2 shared Agnieszka K. BronowskaiD· 1 shared Alfonso Méndez-GodoyiD· 1 shared Andreas BurchertiD· 1 shared Antonia Kern· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

Gert BangeORCID

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3 papers

Recent·Most cited

BiochemistrybioRxivPreprintAug 20, 2026

NUDT2 loss defines quantitative limits for dinucleoside polyphosphate action on the cGAS-STING-TBK1 axis

Paul Stanley Weiland, Shivakumar Renuka Dharani, Ekaterina Jalomo-Khayrova…·Gert Bange

This study investigates whether NUDT2 loss and subsequent Ap4A accumulation affects the cGAS-STING-TBK1 pathway, finding that physiological levels of Ap4A do not inhibit the pathway.

DOI 10.64898/2026.08.18.745545

humanproteomics

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BiochemistryNucleic Acids ResearchPeer-reviewedMar 19, 2026

Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1

Sébastien Favre, Benjamin Pillet, Fabiana Burchert…·Dieter Kressler

The paper identifies Acl1 and Bcl1 as dedicated chaperones for Rpl1 by using proximity labeling and structural analysis in yeast.

2 citations

yeastproteomics

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MicrobiologymBioPeer-reviewedDec 31, 2025

Structural basis of quinone-sensing by the MarR-type repressor MhqR in Staphylococcus aureus

Thao Thi-Phuong Nguyen, Paul Stanley Weiland, Vu Van Loi…·Haike Antelmann

This paper identifies the quinone-binding pocket of SaMhqR and elucidates its mechanism of inactivation through structural and mutational analyses.

1 citation

humanstructural biology

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