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• W1999463253 abstract "Biosynthetic studies of the prion protein (PrP) have shown that two forms of different topology can be generated from the same pool of nascent chains in cell-free translation systems supplemented with microsomal membranes. A transmembrane form is the predominant product generated in wheat germ (WG) extracts, whereas a completely translocated (secretory) form is the major product synthesized in rabbit reticulocyte lysates (RRL). An unusual topogenic sequence within PrP is now shown to direct this system-dependent difference. The actions of this topogenic sequence were independent of on-going translation and could be conferred to heterologous proteins by the engineering of a discrete set of codons. System-dependent topology conferred by addition of RRL to WG translation products suggests that this sequence interacts with one or more cytosolic factors." @default.
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• W1999463253 date "1990-04-13" @default.
• W1999463253 modified "2023-09-25" @default.
• W1999463253 title "Unusual Topogenic Sequence Directs Prion Protein Biogenesis" @default.
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• W1999463253 doi "https://doi.org/10.1126/science.1970195" @default.
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