Author

Eri Sakata

Universitätsmedizin GöttingenORCID 0000-0002-8580-3683Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1 Organism:yeast· 1

Frequent Co-Authors

Tat Cheung ChengiD· 2 shared Andreas Schweitzer· 1 shared Anne K. SchütziD· 1 shared Anton Zhornyak· 1 shared Antonia A. NemeciD· 1 shared Bilyana PopovaiD· 1 shared Florian StengeliD· 1 shared Gerhard H. BrausiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersMolecular Biology

Tat Cheung ChengORCID

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3 papers

Recent·Most cited

Blm10/PA200-activated 20S proteasomes promote α-synuclein degradation and bypass proteasome inhibition in Parkinson disease models

Tariq Tammam Ali, Anton Zhornyak, Madiha Mohieldin Merghani, Zora Buschenlange, Eri Sakata, Tiago F. Outeiro, Bilyana Popova, Gerhard H. Braus

This study shows that Blm10/PA200 activates 20S proteasomes to degrade α-synuclein and resist inhibition, improving proteostasis in Parkinson's disease models.

Aging Cell · May 28, 2026Peer-reviewedCell Biology

The vacuolar tauopathy-associated mutation D395G confers redox sensitivity to p97/VCP

Smruti Ranjan Rout, Martin Kulke, Maxim A. Droemer, Marcel Wendel, Tat Cheung Cheng, Tristan Alexander Mauck, Sean Asgari, Antonia A. Nemec, Mikhail Shein, Yusuke Sato, Shuya Fukai, Gregor Witte, Robert J. Tomko, Florian Stengel, Martin Zacharias, , Eri Sakata

This study investigates how the p97/VCP mutation D395G increases redox sensitivity, leading to oxidative inactivation and contributing to neurodegeneration.

bioRxiv · May 4, 2026 · PreprintMolecular Biology

Structures of the 26S proteasome in complex with the Hsp70 cochaperone Bag1 reveal a novel mechanism of ubiquitin-independent proteasomal degradation

Moisés Maestro-López, Tat Cheung Cheng, Jimena Muntaner, Margarita Menéndez, Melissa Alonso, Andreas Schweitzer, Jorge Cuéllar, José Valpuesta, Eri Sakata

This study presents cryo-EM structures of the Bag1-bound 26S proteasome, revealing a mechanism for ubiquitin-independent proteasomal degradation through conformational changes in the 19S regulatory particle.

bioRxiv · Jan 22, 2025 · PreprintMolecular Biology