Author

J. Lassak

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

Biology Disciplines

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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:E. coli· 2 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:gene regulatory network inference· 1 Research Focus:host-pathogen & immune response· 1 Assay:metagenomics· 1

Frequent Co-Authors

J. Hennig· 2 shared P. K. A. Jagtap· 2 shared R. Krafczyk· 2 shared A. Hoffmann-Roeder· 1 shared A. K. Jha· 1 shared A. M. Sieber· 1 shared A. Schaepers· 1 shared A. Schlundt· 1 shared

Activity by Year

2017-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersMicrobiology

J. Hennig

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

EF-P and its paralog EfpL (YeiP) differentially control translation of proline containing sequences

A. M. Sieber, M. Parr, J. von Ehr, K. Dhamotharan, P. Kielkowski, T. Brewer, A. Schaepers, R. Krafczyk, F. Qi, A. Schlundt, D. Frishman, J. Lassak

This study identifies EfpL as a ribosome rescue factor that senses cellular metabolic state, complementing EF-P in proline-containing sequence translation.

bioRxiv · Apr 15, 2024Microbiology

Transcriptional regulation of the Nε-fructoselysine metabolism in Escherichia coli by global and substrate-specific cues

B. Graf von Armansperg, F. Koller, N. Gericke, M. Hellwig, P. K. A. Jagtap, R. Heermann, J. Hennig, T. Henle, J. Lassak

The paper shows that Escherichia coli regulates fructoselysine metabolism through global and substrate-specific transcriptional regulators to efficiently utilize this compound in the gut.

bioRxiv · Jan 13, 2020Microbiology

Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P

R. Krafczyk, J. Macosek, D. Gast, S. Wunder, P. K. A. Jagtap, P. Mitra, A. K. Jha, J. Rohr, A. Hoffmann-Roeder, K. Jung, J. Hennig, J. Lassak

The paper determines the crystal structure of EarP, revealing its mechanism for arginine glycosylation of EF-P and its role in bacterial pathogenicity.

bioRxiv · Mar 13, 2017Biochemistry