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. 2017 Aug 7;216(8):2295–2304. doi: 10.1083/jcb.201612165

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© 2017 Hamdan et al.

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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Figure 2. — Aggregated proteins in wild-type and ER stress mutants have similar localization and physicochemical properties. (A) Venn diagram showing the overlaps between proteins aggregating in wild-type (green), hac1 (pink), and hrd1 (yellow) mutant strains. (B) Diagrams showing the localization of the proteins aggregating in wild-type, hac1, and hrd1 strains. (C–H) Box plots showing comparisons of physicochemical properties for the aggregated proteins common to the wild-type, hac1, and hrd1 mutant strains (common), present in the hac1 mutant, but not the wild-type, strain (hac1 only), and present in the hrd1 mutant, but not the wild-type, strain (hrd1 only). Aggregated proteins were compared with unaggregated proteins (MS). (C) Protein abundance. (D) Codon adaptation index (CAI). (E) Translation rates. (F) Grand mean of hydrophobicity (GRAVY). (G) Isoelectric points (pI). (H) Protein stability. Mann–Whitney U tests were used to assess the statistical significance of observed differences; *, P < 0.05; **, P < 0.01; ***, P < 0.005.