Author

P. K. A. Jagtap

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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Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

J. Hennig· 3 shared J. Lassak· 2 shared A. Hoffmann-Roeder· 1 shared A. K. Jha· 1 shared A. W. Thomae· 1 shared B. Graf von Armansperg· 1 shared B. Simon· 1 shared D. Gast· 1 shared

Activity by Year

2017-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiochemistry

J. Hennig

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Author profile →

3 papers

Recent·Most cited

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

Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless

P. K. A. Jagtap, M. Mueller, P. Masiewicz, S. von Buelow, N. M. Hollmann, B. Simon, A. W. Thomae, P. B. Becker, J. Hennig

This study determines the NMR structure of MLE's dsRBD1 and dsRBD2 and shows they bind dsRNA independently, but dsRBD1 mutants do not affect roX2 binding or MLE localization.

bioRxiv · Nov 9, 2018Biochemistry

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