Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein. (Q47630396)

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7 November 2019

title

Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein (English)

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Mario Salmona

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Giovanna Musco

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Daniel A Kirschner

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Fabrizio Tagliavini

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author name string

Tania Massignan

3

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Laura Colombo

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Giulia Mazzoleni

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Raffaella Capobianco

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Luisa Diomede

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Florian Thaler

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Luca Mollica

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Joseph J Kourie

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Orso Bugiani

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Deepak Sharma

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Hideyo Inouye

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Gianluigi Forloni

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language of work or name

English

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publication date

11 September 2003

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Journal of Biological Chemistry

7 November 2019

published in

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volume

278

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issue

48

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page(s)

48146-48153

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Molecular biology of prion diseases

7 November 2019

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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

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Scrapie prions aggregate to form amyloid-like birefringent rods

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Prion protein amyloidosis

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Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP.

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A new variant of Creutzfeldt-Jakob disease in the UK.

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Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent

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Prion protein preamyloid and amyloid deposits in Gerstmann-Sträussler-Scheinker disease, Indiana kindred

21 January 2018

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A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.

21 January 2018

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Proteinase-K-resistant prion protein isoforms in Gerstmann-Sträussler-Scheinker disease (Indiana kindred).

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Phenotypic variability of Gerstmann-Sträussler-Scheinker disease is associated with prion protein heterogeneity.

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Different patterns of truncated prion protein fragments correlate with distinct phenotypes in P102L Gerstmann-Sträussler-Scheinker disease

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Recombinant scrapie-like prion protein of 106 amino acids is soluble

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Prion protein of 106 residues creates an artifical transmission barrier for prion replication in transgenic mice

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Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro

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Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein

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Tetracycline affects abnormal properties of synthetic PrP peptides and PrP(Sc) in vitro.

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A simple method for displaying the hydropathic character of a protein

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Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes

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In vitro characterization of lactoferrin aggregation and amyloid formation

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A neurotoxic and gliotrophic fragment of the prion protein increases plasma membrane microviscosity.

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Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

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X-ray diffraction analysis of scrapie prion: intermediate and folded structures in a peptide containing two putative alpha-helices

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An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

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NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)

21 January 2018

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NMR solution structure of the human prion protein

21 January 2018

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Genetic influence on the structural variations of the abnormal prion protein

21 January 2018

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Amyloid fibrils in Gerstmann-Sträussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele

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Identifiers

DOI

10.1074/JBC.M307295200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12970341 AND SRC:MED&resulttype=core&format=json

7 November 2019

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