Article

Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation

2026-04-24

Abstract excerpt

<h4>ABSTRACT</h4> The pathogenic conversion of the cellular prion protein (PrP C ) into the β-sheet-rich isoform PrP Sc is the pivotal pathogenic event in prion disease, yet the molecular steps that govern this structural transition remain elusive. In this study, we introduce a new approach to monitor site-specific conformational transitions that occur during infectious prion formation. The method relies on gen...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 5c506f81-6abc-5eb6-a688-d8efd26267b9
DOI: 10.64898/2026.04.21.719968

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formationDOI 10.64898/2026.04.21.719968Read

In vitro generation of highly infectious recombinant prions adopting structural architectures of bona fide prionsSemantic proximity Read

Generation of Infectious Prions Amenable to Site-specific Click ChemistrySemantic proximity Read

Human PrP E219K as a new and promising substrate for RT-QuIC amplification of human prion strains: a first step towards strain discriminationSemantic proximity Read

Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generationSemantic proximity Read

Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategySemantic proximity Read

Correlation of structural elements and infectivity of the HET-s prion.Semantic proximity Read

Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.Semantic proximity Read

Computationally engineered cyclic peptides reduce prion levels <i>in vitro</i>Semantic proximity Read

Intercellular transmission of a bacterial cytotoxic prion-like protein in mammalian cellsSemantic proximity Read

Full Atomistic Model of Prion Structure and ConversionSemantic proximity Read

Membrane-anchored PrP <sup>Sc</sup> is the trigger for prion synaptotoxicitySemantic proximity Read

A dividing cell model for stable propagation and curing of <i>bona fide</i> human sporadic Creutzfeldt-Jakob Disease prionsSemantic proximity Read