Author

P. Pohl

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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Biophysics· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Organism:bacteria (other)· 2 Assay:electrophysiology· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Research Focus:differential expression· 1

Frequent Co-Authors

C. Siligan· 4 shared N. Goessweiner-Mohr· 3 shared C. Hannesschlaeger· 2 shared D. G. Knyazev· 2 shared N. Hagleitner-Ertugrul· 2 shared R. Kuttner· 2 shared A. Horner· 1 shared A. Karner· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersBiophysics

C. Siligan

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Photolipid excitation triggers depolarizing optocapacitive currents and action potentials

C. A. Z. Bassetto, J. Pfeffermann, R. Yadav, S. Strassgschwandtner, T. Glasnov, F. Bezanilla, P. Pohl

The paper demonstrates that photolipids can trigger optocapacitive currents and action potentials through light-induced changes in membrane capacitance and mechanosensitive channel activity.

bioRxiv · Aug 11, 2023Biophysics

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

Steady-state polypeptide transfer from the translocon to the membrane

D. G. Knyazev, M. Schaur, R. Kuttner, C. Siligan, N. Goessweiner-Mohr, N. Hagleitner-Ertugrul, P. Pohl

The paper tests the hypothesis that nascent polypeptide integration into membranes is determined by hydrophobicity, using a reconstituted SecYEG system with a stalled ribosome.

bioRxiv · Jan 10, 2023 · PreprintBiophysics

Trapped pore waters in the open proton channel HV1

D. Boytsov, S. Brescia, G. Chaves, S. Koefler, C. Hannesschlaeger, C. Siligan, N. Goessweiner-Mohr, B. Musset, P. Pohl

The paper investigates proton transport through HV1 channels, finding that water is trapped in the pore and that H+ conductance is reduced by removing a charged amino acid.

bioRxiv · May 9, 2022Biophysics

Binding of the motor protein SecA to the bacterial protein translocation channel SecYEG in the absence of ATP

K. Winkler, A. Karner, A. Horner, C. Hannesschlaeger, D. Knyazev, C. Siligan, M. Zimmermann, R. Kuttner, P. Pohl, J. Preiner

The paper investigates how SecA remains bound to SecYEG without ATP, showing stable interactions and conformational changes that support protein translocation.

Nanoscale Advances · Jan 1, 2020Peer-reviewedBiophysics