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• W4378894919 abstract "Protein complex assembly often occurs while subunits are being translated, resulting in complexes whose subunits were translated from the same mRNA in an allele-specific manner. It has thus been hypothesized that such cotranslational assembly may counter the assembly-mediated dominant-negative effect, whereby co-assembly of mutant and wild-type subunits poisons complex activity. Here, we show that cotranslationally assembling subunits are much less likely to be associated with autosomal dominant relative to recessive disorders, and that subunits with dominant-negative disease mutations are significantly depleted in cotranslational assembly compared to those associated with loss-of-function mutations. We also find that complexes with known dominant-negative effects tend to expose their interfaces late during translation, lessening the likelihood of cotranslational assembly. Finally, by combining complex properties with other features, we trained a computational model for predicting proteins likely to be associated with non-loss-of-function disease mechanisms, which we believe will be of considerable utility for protein variant interpretation." @default.
• W4378894919 created "2023-06-01" @default.
• W4378894919 creator A5002238592 @default.
• W4378894919 creator A5013184525 @default.
• W4378894919 date "2023-06-02" @default.
• W4378894919 modified "2023-09-30" @default.
• W4378894919 title "Buffering of genetic dominance by allele-specific protein complex assembly" @default.
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• W4378894919 doi "https://doi.org/10.1126/sciadv.adf9845" @default.
• W4378894919 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37256959" @default.
• W4378894919 hasPublicationYear "2023" @default.
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