Supplemental data for 'Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization''
Authors/Creators
- 1. Department of Cell Biochemistry, University of Groningen, Groningen 9747 AG, The Netherlands
- 2. German Centre for Neurodegenerative Diseases, 72076 Tübingen, Germany
Description
Supplemental mass photomerty raw data used in Figure 3 of 'Guaitoli, G., Zhang, X., Saitta, F., Miglionico, P., Silbermann, L.M., Ho, F.Y., Zweydorf, F.v., Signorelli, M., Tych, K., Fessas, D., Raimondi, F., Kortholt, A., and Gloeckner, C.J. (2023). Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization. bioRxiv, 2023.2008.2011.549911 doi: 10.1101/2023.08.11.549911'
Raw data Figure 3A: Mass photometry raw data for LRRK2 wild-type in presence of different G-nucleotides at different LRRK2 concentrations. Three biological replicates have been considered for the statistical analysis.
Raw data Figure 3B: Mass photometry raw data for LRRK2 WT (left panel), LRRK2 WT + MLi-2 (middle panel) and kinase-dead LRRK2 (right panel) without and with ATP pre-incubation (-/+ ATP). Two biological and three technical replicates have been considered for the statistical analysis.
Raw data Figure 3C: Mass photometry raw data for pathogenic LRRK2 variants in presence of different G-nucleotides. Two biological and two technical replicates have been considered for the statistical analysis.
Files
Raw data Figure 3A.zip
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- Preprint: 10.1101/2023.08.11.549911 (DOI)