Author

R. P. Jakob

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· 1 Biophysics· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:mouse· 1

Frequent Co-Authors

T. Maier· 4 shared A. K. Shukla· 1 shared A. Kaczmarczyk· 1 shared A. Klotz· 1 shared A. Moroni· 1 shared A. Plueckthun· 1 shared A. Ranjan· 1 shared A. Reinders· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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4 shared papersMicrobiology

T. Maier

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A Novel Biosensor Reveals Dynamic Changes of C-di-GMP in Differentiating Cells with Ultra-High Temporal Resolution

A. Kaczmarczyk, S. van Vliet, R. P. Jakob, A. Reinders, A. Klotz, T. Maier, U. Jenal

This paper introduces a genetically-encoded c-di-GMP biosensor, cdGreen2, capable of tracking c-di-GMP dynamics in live cells with ultra-high temporal resolution.

bioRxiv · Oct 18, 2022 · PreprintMicrobiology

A key GPCR phosphorylation motif discovered in arrestin2-CCR5 phosphopeptide complexes

P. Isaikina, I. Petrovic, R. P. Jakob, P. Sarma, A. Ranjan, M. Baruah, V. Panwalkar, T. Maier, A. K. Shukla, S. Grzesiek

The paper identifies a phosphorylation motif in arrestin2-CCR5 complexes that is essential for stable interactions and functional activation of CCR5.

bioRxiv · Oct 10, 2022 · PreprintBiophysics

Structural basis for ion selectivity in TMEM175 K+ channels

J. D. Brunner, R. P. Jakob, T. Schulze, Y. Neldner, A. Moroni, G. Thiel, T. Maier, S. Schenck

This study determines the X-ray structure of a bacterial TMEM175 K+ channel, revealing a unique cation-selective mechanism involving a conserved threonine residue and conformational changes.

bioRxiv · Dec 4, 2018Biochemistry

DARPins recognizing mTFP1 as novel reagents for in vitro and in vivo protein manipulations

M. A. Vigano, D. Bieli, J. V. Schaefer, R. P. Jakob, S. Matsuda, T. Maier, A. Plueckthun, M. Affolter

This paper generates DARPins targeting mTFP1 and uses them to delocalize Rab proteins in cultured cells, demonstrating potential for direct protein manipulation in vivo.

bioRxiv · Jun 22, 2018Cell Biology