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Article

Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein.

Nature - 15 Feb 1990

Yost C S, Lopez C D, Prusiner S B, Myers R M, Lingappa V R

Abstract excerpt

A universal feature of integral transmembrane proteins is a hydrophobic peptide segment that spans the lipid bilayer. These hydrophobic domains are important for terminating the translocation of the polypeptide chain across the membrane of the endoplasmic reticulum (a process termed stop transfer) and for integrating the protein into the bilayer. But a role for extracytoplasmic sequences in stop transfer and...

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PMID: 1968226
DOI: 10.1038/343669a0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein.PMID 1968226Read ↗

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Essential role of the prion protein N terminus in subcellular trafficking and half-life of cellular prion protein.Semantic proximity Read ↗

Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: a critical role for the putative transmembrane domain.Semantic proximity Read ↗

Loss of the first β-strand of human prion protein generates an aggregation-competent partially “open” formSemantic proximity Read ↗

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