Author

A. Bracher

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 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

F. U. Hartl· 3 shared H. Wang· 3 shared M. Hayer-Hartl· 2 shared A. M. Miller· 1 shared C. M. Dobson· 1 shared E. Andrzejwska· 1 shared F. S. Ruggeri· 1 shared F.-U. Hartl· 1 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersBiochemistry

F. U. Hartl

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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

The Hsc70 Disaggregation Machinery RemovesMonomer Units Directly from α-Synuclein FibrilEnds

M. M. Schneider, S. Gautam, T. W. Herling, E. Andrzejwska, G. Krainer, A. M. Miller, Q. A. E. Peter, F. S. Ruggeri, M. Vendruscolo, A. Bracher, C. M. Dobson, F.-U. Hartl, T. Knowles

This study shows the Hsc70-DnaJB1-Apg2 chaperone system removes monomer units directly from α-synuclein fibril ends, reversing aggregation without intermediate fragmentation.

bioRxiv · Nov 2, 2020Biophysics

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