Article

The Protein Disulfide Isomerase P4HB/PDIA1 Modulates PrP <sup>C</sup> Levels and Prion Replication

2025-12-03

Abstract excerpt

Prions are misfolded, self-propagating versions of the cellular prion protein (PrP C ) that cause invariably fatal transmissible neurodegenerative diseases in humans and animals. Little is known about how prions replicate in the brain, including whether other proteins participate in prion replication in vivo . Several members of the protein disulfide isomerase family have been shown to reside in close spatial pr...

Topics

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

Identifiers and source

Literature Corpus work: 3cdfc277-41d9-5525-b86c-143c26bedb78
DOI: 10.64898/2025.12.01.691611

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

The Protein Disulfide Isomerase P4HB/PDIA1 Modulates PrP <sup>C</sup> Levels and Prion ReplicationDOI 10.64898/2025.12.01.691611Read

Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion.Semantic proximity Read

The prion diseases.Semantic proximity Read

Prions and Prion-like ProteinsSemantic proximity Read

Prion protein and prion disease at a glanceSemantic proximity Read

The Prion Basis of Progressive Neurodegenerative DisordersSemantic proximity Read

Prions mediated neurodegenerative disorders.Semantic proximity Read

Prions.Semantic proximity Read

In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded IsoformsSemantic proximity Read

Conformational conversion of prion protein in prion diseases.Semantic proximity Read

Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Semantic proximity Read

The prion diseases.Semantic proximity Read

A structural overview of the vertebrate prion proteins.Semantic proximity Read