(Q34214314)

31 July 2017

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title

Interactions between prion protein isoforms: the kiss of death? (English)

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31 July 2017

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Caughey B

1

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31 July 2017

publication date

1 April 2001

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31 July 2017

number of pages

8

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Trends in Biochemical Sciences

inferred from page(s)

published in

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31 July 2017

volume

26

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31 July 2017

issue

4

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31 July 2017

page(s)

235-242

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Prions and neurodegenerative diseases

31 July 2017

cites work

1 reference

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Prion protein and the transmissible spongiform encephalopathies

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Prion protein interconversions and the transmissible spongiform encephalopathies

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Self-replication and scrapie

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Normal host prion protein necessary for scrapie-induced neurotoxicity.

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Signal transduction through prion protein

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A transmembrane form of the prion protein in neurodegenerative disease

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A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP.

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Morphogenesis of amyloid plaques in 87V murine scrapie

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Three-dimensional structures of prion proteins

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Biosynthesis and cellular processing of the prion protein.

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Sphingolipid Depletion Increases Formation of the Scrapie Prion Protein in Neuroblastoma Cells Infected with Prions

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Chaperone-supervised conversion of prion protein to its protease-resistant form

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Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state

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Cell-free formation of protease-resistant prion protein.

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In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices

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Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers

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Protease-resistant prion protein produced in vitro lacks detectable infectivity.

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Prion protein and species barriers in the transmissible spongiform encephalopathies

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Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease

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Transmissible spongiform encephalopathies, amyloidoses and yeast prions: common threads?

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Non-genetic propagation of strain-specific properties of scrapie prion protein.

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Strain-specific prion-protein conformation determined by metal ions

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Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state

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Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein

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7 January 2021

Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone

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7 January 2021

Characterization and polyanion-binding properties of purified recombinant prion protein

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7 January 2021

Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules

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A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice

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Novel therapeutic uses for porphyrins and phthalocyanines in the transmissible spongiform encephalopathies

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7 January 2021

Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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7 January 2021

Molecular biology of prion diseases

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7 January 2021

A kinetic model for amyloid formation in the prion diseases: importance of seeding

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7 January 2021

Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides

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7 January 2021

Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence

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7 January 2021

Sulfated glycosaminoglycans in amyloid plaques of prion diseases

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7 January 2021

Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain.

1 reference

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7 January 2021

10.1016/S0968-0004(01)01792-3

Identifiers

DOI

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31 July 2017

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