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Prion peptide 106-126 as a model for prion replication and neurotoxicity

Data up to Jan 2025

Published2002
Citations45
References28

Total Citations Per Year

Abstract

References (28)

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The Chaperone Protein BiP Binds to a Mutant Prion Protein and Mediates Its Degradation by the Proteasome

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Proteasomal Degradation and N-terminal Protease Resistance of the Codon 145 Mutant Prion Protein

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1998 • 133 citations

Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform.

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Prion Peptide 106–126 Modulates the Aggregation of Cellular Prion Protein and Induces the Synthesis of Potentially Neurotoxic Transmembrane PrP

2002 • 104 citations

PrPSc-like prion protein peptide inhibits the function of cellular prion protein

2000 • 97 citations

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The Role of Prion Peptide Structure and Aggregation in Toxicity and Membrane Binding

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A Neurotoxic and Gliotrophic Fragment of the Prion Protein Increases Plasma Membrane Microviscosity

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Cellular uptake of the prion protein fragment PrP106-126 in vitro.

1999 • 42 citations

Prion protein fragment interacts with PrP-deficient cells

1998 • 35 citations

Submicroscopic immunodetection of PrP in the brain of a patient with a new-variant of Creutzfeldt–Jakob disease

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Prion peptide 106-126 as a model for prion replication and neurotoxicity (2002) – Frontiers in bioscience | Metascience Observatory Explorer