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The FEBS Journal|March 16, 2021
Stress granules: regulators or by-products?Daniel Mateju, Jeffrey A Chao
Frontiers in Molecular Neuroscience|April 12, 2017
Granulostasis: Protein Quality Control of RNP GranulesSimon Alberti, Daniel Mateju, Laura Mediani, et al.
Molecular Cell|February 2, 2023
Single-molecule imaging reveals translation-dependent destabilization of mRNAsPratik Dave, Gregory Roth, Esther Griesbach, et al.
Cell|December 14, 2020
Single-Molecule Imaging Reveals Translation of mRNAs Localized to Stress GranulesDaniel Mateju, Bastian Eichenberger, Franka Voigt, et al.
Elife|August 5, 2015
Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granulesSonja Kroschwald, Shovamayee Maharana, Daniel Mateju, et al.
The EMBO Journal|April 6, 2017
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone functionDaniel Mateju, Titus M Franzmann, Avinash Patel, et al.
The EMBO Journal|July 5, 2019
Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitinLaura Mediani, Jordina Guillén-Boixet, Jonathan Vinet, et al.
Molecular Cell|August 30, 2016
A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and DynamismMassimo Ganassi, Daniel Mateju, Ilaria Bigi, et al.
Cell Stress & Chaperones|July 23, 2020
BAG3 and BAG6 differentially affect the dynamics of stress granules by targeting distinct subsets of defective polypeptides released from ribosomesLaura Mediani, Veronica Galli, Arianna Dorotea Carrà, et al.
Elife|September 6, 2021
HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domainEdgar E Boczek, Julius Fürsch, Marie Laura Niedermeier, et al.
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