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Lara A Gruijs da Silva

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Methods in Molecular Biology (Clifton, N.J.)|October 13, 2022
Sedimentation Assays to Assess the Impact of Posttranslational Modifications on Phase Separation of RNA-Binding Proteins In Vitro and In CellsLara A Gruijs da Silva, Dorothee Dormann
Trends in Biochemical Sciences|August 9, 2021
Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?Erin L Sternburg, Lara A Gruijs da Silva, Dorothee Dormann
The EMBO Journal|February 3, 2022
Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregationLara A Gruijs da Silva, Francesca Simonetti, Saskia Hutten, et al.
Acta Neuropathologica Communications|July 11, 2023
Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivoHenrick Riemenschneider, Francesca Simonetti, Udit Sheth, et al.
Pageof 1

Showing results (1-10 of 4) with videos related to

Sort By:
Pageof 1
Methods in Molecular Biology (Clifton, N.J.)|October 13, 2022
Sedimentation Assays to Assess the Impact of Posttranslational Modifications on Phase Separation of RNA-Binding Proteins In Vitro and In CellsLara A Gruijs da Silva, Dorothee Dormann
Trends in Biochemical Sciences|August 9, 2021
Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?Erin L Sternburg, Lara A Gruijs da Silva, Dorothee Dormann
The EMBO Journal|February 3, 2022
Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregationLara A Gruijs da Silva, Francesca Simonetti, Saskia Hutten, et al.
Acta Neuropathologica Communications|July 11, 2023
Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivoHenrick Riemenschneider, Francesca Simonetti, Udit Sheth, et al.
Pageof 1