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- W1989087417 abstract "Protein kinase R (PKR) is a central component of the interferon antiviral defense pathway. Upon binding to dsRNA, PKR undergoes autophosphorylation reactions that activate the kinase, resulting in the inhibition of protein synthesis in virally-infected cells. We have used analytical ultracentrifugation and related biophysical methods to quantitatively characterize the stoichiometries, affinities, and free energy couplings that govern the assembly of the macromolecular complexes in the PKR activation pathway. These studies demonstrate that PKR dimerization play a key role in enzymatic activation and support a model where the role of dsRNA is to bring two or more PKR monomers in close proximity to enhance dimerization." @default.
- W1989087417 created "2016-06-24" @default.
- W1989087417 creator A5033273566 @default.
- W1989087417 date "2010-06-09" @default.
- W1989087417 modified "2023-09-27" @default.
- W1989087417 title "Analysis of PKR Activation Using Analytical Ultracentrifugation" @default.
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- W1989087417 doi "https://doi.org/10.1002/mabi.201000069" @default.
- W1989087417 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2926283" @default.
- W1989087417 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20533534" @default.
- W1989087417 hasPublicationYear "2010" @default.
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