Daniel Matějů
Daniel Matějů
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Cited by
Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
S Kroschwald, S Maharana, D Mateju, L Malinovska, E Nüske, I Poser, ...
elife 4, e06807, 2015
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function
D Mateju, TM Franzmann, A Patel, A Kopach, EE Boczek, S Maharana, ...
The EMBO journal 36 (12), 1669-1687, 2017
RNA-induced conformational switching and clustering of G3BP drive stress granule assembly by condensation
J Guillén-Boixet, A Kopach, AS Holehouse, S Wittmann, M Jahnel, ...
Cell 181 (2), 346-361. e17, 2020
A surveillance function of the HSPB8-BAG3-HSP70 chaperone complex ensures stress granule integrity and dynamism
M Ganassi, D Mateju, I Bigi, L Mediani, I Poser, HO Lee, SJ Seguin, ...
Molecular cell 63 (5), 796-810, 2016
Granulostasis: protein quality control of RNP granules
S Alberti, D Mateju, L Mediani, S Carra
Frontiers in molecular neuroscience 10, 84, 2017
Single-molecule imaging reveals translation of mRNAs localized to stress granules
D Mateju, B Eichenberger, F Voigt, J Eglinger, G Roth, JA Chao
Cell 183 (7), 1801-1812. e13, 2020
Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones
A Malinová, Z Cvačková, D Matějů, Z Hořejší, C Abéza, F Vandermoere, ...
Journal of Cell Biology 216 (6), 1579-1596, 2017
SART3-dependent accumulation of incomplete spliceosomal snRNPs in Cajal bodies
I Novotnŭ, A Malinová, E Stejskalová, D Matějů, K Klimešová, A Roithová, ...
Cell reports 10 (3), 429-440, 2015
Retinitis Pigmentosa Mutations of SNRNP200 Enhance Cryptic Splice‐Site Recognition
Z Cvačková, D Matějů, D Staněk
Human mutation 35 (3), 308-317, 2014
Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitin
L Mediani, J Guillén‐Boixet, J Vinet, TM Franzmann, I Bigi, D Mateju, ...
The EMBO journal 38 (15), e101341, 2019
HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain
EE Boczek, J Fürsch, ML Niedermeier, L Jawerth, M Jahnel, M Ruer-Gruß, ...
Elife 10, e69377, 2021
BAG3 and BAG6 differentially affect the dynamics of stress granules by targeting distinct subsets of defective polypeptides released from ribosomes
L Mediani, V Galli, AD Carrà, I Bigi, J Vinet, M Ganassi, F Antoniani, ...
Cell Stress and Chaperones 25 (6), 1045-1058, 2020
Stress granules: regulators or by‐products?
D Mateju, JA Chao
The FEBS Journal 289 (2), 363-373, 2022
Single-molecule imaging reveals the coupling of translation and mRNA decay
P Dave, E Griesbach, G Roth, D Mateju, JA Chao
Available at SSRN 3885982, 2021
The Integrated Stress Response: Methods and Protocols
D Mateju, JA Chao
Springer, 2021
Molecular Chaperones Regulating the Dynamics, Composition and Functionality of RNP Granules: Implications for Age-Related Diseases
D Mateju, L Mediani, FF Morelli, S Alberti, S Carra
HSP70 in Human Diseases and Disorders, 205-222, 2018
Effect of misfolded proteins and the proteostasis machinery on the properties of stress-inducible RNP granules
D Mateju
Technische Universität Dresden, 2017
Functional analysis of hPrp8 mutations linked to retinitis pigmentosa.
D Matějů
Univerzita Karlova, Přírodovědecká fakulta, 2013
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