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- W2000572271 endingPage "319" @default.
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- W2000572271 abstract "Prions are viewed as enigmatic infectious entities whose genetic properties are enciphered solely in an array of self-propagating protein aggregate conformations. Rnq1, a yeast protein with yet unknown function, forms a prion named [PIN + ] for its ability to facilitate the de novo induction of another prion, [PSI + ]. Here we investigate a set of RNQ1 truncations that were designed to cover major Rnq1 sequence elements similar to those important for the propagation of other yeast prions: a region rich in asparagines and glutamines and several types of oligopeptide repeats. Proteins encoded by these RNQ1 truncations were tested for their ability to (a) join (decorate) pre-existing [PIN + ] aggregates made of wild-type Rnq1 and (b) maintain the heritable aggregated state in the absence of wild-type RNQ1. While the possible involvement of particular sequence elements in the propagation of [PIN + ] is discussed, the major result is that the efficiency of transmission of [PIN + ] from wild-type Rnq1 to a fragment decreased with the fragment’s length." @default.
- W2000572271 created "2016-06-24" @default.
- W2000572271 creator A5024750924 @default.
- W2000572271 creator A5051898020 @default.
- W2000572271 creator A5068578200 @default.
- W2000572271 creator A5073859263 @default.
- W2000572271 date "2007-04-06" @default.
- W2000572271 modified "2023-10-17" @default.
- W2000572271 title "Propagation of the [PIN + ] prion by fragments of Rnq1 fused to GFP" @default.
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- W2000572271 doi "https://doi.org/10.1007/s00294-007-0127-0" @default.
- W2000572271 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2597802" @default.
- W2000572271 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17415568" @default.
- W2000572271 hasPublicationYear "2007" @default.
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