IndraLab

Statements

ATP inhibits IFIH1. 6 / 6
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"Biochemical analyses of gain-of-function variants have shown that mutations in the ATP binding site such as R337G increase the affinity of MDA5 for short dsRNAs in the presence of ATP by inhibiting ATP hydrolysis and hence ATPdependent proofreading 25, 26 ."
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"Mutations in the ATP binding pocket inhibit ATP hydrolysis without affecting filament formation, whereas those at the RNA interface increase the affinity or avidity of MDA5 for RNA26."
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"Abundant ATP prevented basal activation of apo MDA5."
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"Based on these models of RIG-I and MDA5 described above, one may conclude that ATP hydrolysis negatively regulates the signaling activity of MDA5, while it is required for the RIG-I signaling activity."
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"Mutations in the ATP binding pocket inhibit ATP hydrolysis without affecting filament formation, whereas those at the RNA interface increase the affinity or avidity of MDA5 for RNA ."
34795277
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"Biochemical analyses of gain-of-function variants have shown that mutations in the ATP binding site such as R337G increase the affinity of MDA5 for short dsRNAs in the presence of ATP by inhibiting ATP hydrolysis and hence ATP-dependent proofreading ."
34795277