Author

P. Hildebrandt

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· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Assay:metagenomics· 1 Organism:mouse· 1

Frequent Co-Authors

A. Keidel· 1 shared A. Silapetere· 1 shared B. Liepe· 1 shared C. Hentschker· 1 shared D. Becher· 1 shared D. Buhrke· 1 shared D. V. Zlenko· 1 shared E. G. Maksimov· 1 shared

Activity by Year

2016-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiophysics

A. Keidel

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Metabolic differences between symbiont subpopulations in the deep-sea tubeworm Riftia pachyptila

T. Hinzke, M. Kleiner, M. Meister, R. Schlueter, C. Hentschker, J. Pane-Farre, P. Hildebrandt, H. Felbeck, S. M. Sievert, F. Bonn, U. Voelker, D. Becher, T. Schweder, S. Markert

The paper identifies metabolic differences between symbiont subpopulations in Riftia pachyptila, showing small symbionts focus on division and host interaction while large ones specialize in carbon fixation and biosynthesis.

bioRxiv · Apr 8, 2020 · PreprintMicrobiology

MerMAIDs: A novel family of metagenomically discovered, marine, anion-conducting and intensely desensitizing channelrhodopsins.

J. Oppermann, P. Fischer, A. Silapetere, B. Liepe, S. Rodriguez-Rozada, J. Flores-Uribe, E. Peter, A. Keidel, J. Vierock, J. Kaufmann, M. Broser, M. Luck, F. Bartl, P. Hildebrandt, J. S. Wiegert, , J. Wietek

The paper identifies a new family of marine anion-conducting channelrhodopsins (MerMAIDs) that rapidly desensitize under continuous light, enabling their use as optogenetic silencers.

bioRxiv · Apr 12, 2019Biophysics

Assembly of photoactive Orange Carotenoid Protein from its domains unravels a carotenoid shuttle mechanism

M. Moldenhauer, N. N. Sluchanko, D. Buhrke, D. V. Zlenko, N. N. Tavraz, F.-J. Schmitt, P. Hildebrandt, E. G. Maksimov, T. Friedrich

The study reassembles the Orange Carotenoid Protein (OCP) from its domains, revealing a carotenoid shuttle mechanism where the CTD binds carotenoid and transfers it to the NTD.

bioRxiv · Dec 24, 2016Biophysics