Author

F. U. Hartl

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 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell type annotation· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1

Frequent Co-Authors

A. Bracher· 3 shared H. Wang· 3 shared I. Dudanova· 2 shared I. Riera-Tur· 2 shared M. Hayer-Hartl· 2 shared M. S. Hipp· 2 shared V. A. Trinkaus· 2 shared A. Martinez-Sanchez· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

A. Bracher

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Author profile →

4 papers

Recent·Most cited

The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model

P. Yuste-Checa, V. A. Trinkaus, I. Riera-Tur, R. Imamoglu, T. Schaller, H. Wang, I. Dudanova, M. S. Hipp, A. Bracher, F. U. Hartl

This study shows that Clusterin enhances Tau aggregate seeding in a cellular model by stabilizing soluble seed species and facilitating their transfer to recipient cells.

bioRxiv · Jul 16, 2021Cell Biology

In situ architecture of neuronal alpha-Synuclein inclusions

V. A. Trinkaus, I. Riera-Tur, A. Martinez-Sanchez, F. J. B. Baeuerlein, Q. Guo, T. Arzberger, W. Baumeister, I. Dudanova, M. S. Hipp, F. U. Hartl, R. Fernandez-Busnadiego

This study uses cryo-ET to show that neuronal alpha-Synuclein inclusions contain fibrils intermixed with cellular membranes and are nucleated by oligomers.

Nature Communications · Apr 14, 2021Peer-reviewedCell Biology

Dual Role of a Rubisco Activase in Metabolic Repair and Carboxysome Organization

M. Hayer-Hartl, M. Flecken, H. Wang, L. Popilka, F. U. Hartl, A. Bracher

This study investigates the structural and mechanistic role of cyanobacterial Rubisco activase in Rubisco repair and carboxysome organization.

bioRxiv · May 16, 2020 · PreprintBiochemistry

Structure and conformational cycle of a bacteriophage-encoded chaperonin

M. Hayer-Hartl, A. Bracher, S. S. Paul, H. Wang, N. Wischnewski, F. U. Hartl

This study characterizes the structure and conformational cycle of the bacteriophage-encoded chaperonin gp146 (φEL), showing it functions in aggregation prevention without substrate encapsulation.

bioRxiv · Feb 24, 2020Biochemistry