Fig. 1: Screening of molecular chaperones from yeast and humans for their ability to rescue the proteotoxicity of various neurodegenerative disease and protein misfolding models. | Nature Communications

Fig. 1: Screening of molecular chaperones from yeast and humans for their ability to rescue the proteotoxicity of various neurodegenerative disease and protein misfolding models.

From: Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity

Fig. 1: Screening of molecular chaperones from yeast and humans for their ability to rescue the proteotoxicity of various neurodegenerative disease and protein misfolding models.

a Models included in screen and disease association. b Log2 fold change plotted for interactions between selected yeast chaperones and models. Log2 fold changes are shown as an average of all barcoded strains associated with that model. c Statistically significant interactions between selected yeast chaperones and models. d Validation of interactions between yeast chaperones and models. Data are shown as mean ± s.d. for three biological replicates. **P = 0.0017, ****P = < 0.0001, **P = 0.0091, ***P = 0.0006. e Log2 fold change plotted for interactions between selected human chaperones and models. f Statistically significant interactions between selected human chaperones and models. g Validation of interactions between human chaperones and models. Data are shown as mean ± s.d. for three biological replicates. ***P =  0.0007, **P = 0.001, **P = 0.0011, ****P = < 0.0001, ****P = < 0.0001, ****P = 0.0001. Comparisons between two conditions were conducted with two-sided Welch’s t tests while multiple comparisons were conducted with ordinary one-way ANOVA; **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001.

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