In vitro conversion of normal prion protein into pathologic isoforms

A. Bossers, A. Rigter, R. de Vries, M.A. Smits

    Research output: Contribution to journalArticleAcademicpeer-review

    10 Citations (Scopus)


    This article describes the various available in vitro systems used to study transmissible spongiform encephalopathy (TSE) replication and the processes involved in prion protein (PrP) conversion. Advantages and disadvantages of these in vitro systems and the underlying molecular mechanisms of PrP conversion are discussed. Several applications of these systems are outlined more extensively, including their species specificity, polymorphism specificity, strain specificity, and the potential that these systems have in screening and discovering TSE therapeutics.
    Original languageEnglish
    Pages (from-to)227-247
    JournalClinics in Laboratory Medicine
    Issue number1
    Publication statusPublished - 2003


    • creutzfeldt-jakob-disease
    • mouse neuroblastoma-cells
    • transmissible mink encephalopathy
    • scrapie-associated form
    • natural scrapie
    • resistant state
    • cultured-cells
    • synthetic peptides
    • incubation period
    • species barriers


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