Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation
SA Bondarev, VV Shchepachev, AV Kajava… - Journal of Biological …, 2013 - ASBMB
Background: The prion domain (PrD) of Sup35p can aggregate to form the [PSI+] prion.
Results: Introduction of charged lysine residues (sup35 KK) in the Sup35p PrD alters prion
properties. Conclusion: Some sup35 KK alleles lead to the formation of new prion variants.
Significance: Establishment of molecular interactions influencing [PSI+] prion stability and
maintenance is a step toward an understanding of prion folding. Recent studies have shown
that Sup35p prion fibrils probably have a parallel in-register β-structure. However, the part …
Results: Introduction of charged lysine residues (sup35 KK) in the Sup35p PrD alters prion
properties. Conclusion: Some sup35 KK alleles lead to the formation of new prion variants.
Significance: Establishment of molecular interactions influencing [PSI+] prion stability and
maintenance is a step toward an understanding of prion folding. Recent studies have shown
that Sup35p prion fibrils probably have a parallel in-register β-structure. However, the part …
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