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To distinguish between these models, we directly compared binding of MW1 and 3B5H10 to normal and expanded polyQ repeats within huntingtin exon 1 fusion proteins.
In order to make it easier to assess the exact differences between these models, we list the abbreviations of all methods, their full name, and corresponding energy functionals in Table 1.
To help distinguish between these models we immunoprecipitated Parkin from wt flies and subjected the immunoprecipitate to western blot analysis with an anti-dMfn antiserum.
To distinguish between these models, we examined the effects of mutants that disrupt osk mRNA localization.
To distinguish between these models, we reduced RhoA levels by mutationally inactivating NOP-1.
To distinguish between these models, we manipulated levels of progeny production by controlling sperm availability.
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In order to differentiate between the parameters of these models, we use asterisks for the parameters β 1 * and β 2 * of the simulation model to indicate that these are true parameters.
In both of these models, we observed steric clashes between Met311 and residues in HP2.
For these models we report mean changes between visits, with 95% confidence intervals.
To measure the distance between the models, we apply a novel Euclidean distance, approximations of Kullback-Leibler divergence, and a cross-likelihood ratio test.
To compare the fitness between the models, we used −2logL methods.
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