Author

H.-G. Koch

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 2 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Organism:E. coli· 2 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Research Focus:differential expression· 1

Frequent Co-Authors

M. H. Ulbrich· 2 shared A. Natriashvili· 1 shared A. Origi· 1 shared A. Tholey· 1 shared A. Vogt· 1 shared A. Wilde· 1 shared B. A. Berghoff· 1 shared B. Warscheid· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersMicrobiology

M. H. Ulbrich

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in Escherichia coli

F. H. Leinberger, L. Cassidy, D. Edelmann, N. E. Schmid, P. Blumenkamp, S. Schmidt, A. Natriashvili, M. H. Ulbrich, A. Tholey, H.-G. Koch, B. A. Berghoff

This study shows that the membrane toxin TisB in E. coli causes protein aggregation, which enhances cellular dormancy and antibiotic tolerance.

bioRxiv · Feb 22, 2024 · PreprintMicrobiology

YidC from Escherichia coli forms an ion-conducting pore upon activation by ribosomes.

D. G. Knyazev, L. Winter, A. Vogt, S. Posch, C. Siligan, N. Goessweiner-Mohr, N. Hagleitner-Ertugrul, H.-G. Koch, P. Pohl

The paper shows that E. coli YidC forms an ion-conducting pore when bound to a ribosome or ribosome-nascent chain complex, suggesting an alternative mechanism for membrane protein insertion.

bioRxiv · May 10, 2023Biophysics

mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria

P. Sarmah, W. Shang, A. Origi, M. Licheva, C. Kraft, M. H. Ulbrich, E. Lichtenberg, A. Wilde, H.-G. Koch

The paper shows that mRNA targeting can replace the SRP pathway for membrane protein insertion in bacteria, using in vivo and in vitro assays.

bioRxiv · Nov 21, 2022Microbiology

Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

S. Dannenmaier, C. Desroches Altamirano, L. Schueler, Y. Zhang, J. Hummel, S. Oeljeklaus, H.-G. Koch, S. Rospert, S. Alberti, B. Warscheid

The paper identifies Ola1p as a positive regulator of heat shock response in yeast through proteomics and cell-based assays, showing its role in stabilizing misfolded proteins and facilitating translation resumption after stress.

bioRxiv · May 12, 2021Cell Biology