Abnormalities in stress proteins in prion diseases. (Q48775242)

15 February 2018

review article

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title

Abnormalities in stress proteins in prion diseases. (English)

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15 February 2018

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1

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15 February 2018

author name string

R Voellmy

series ordinal

2

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W J Welch

series ordinal

3

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publication date

1 December 1998

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Cellular and Molecular Neurobiology

published in

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15 February 2018

volume

18

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15 February 2018

issue

6

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15 February 2018

page(s)

721-729

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15 February 2018

https://scigraph.springernature.com/pub.10.1023/a:1020282205041

exact match

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cites work

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Conservation of the cellular gene encoding the scrapie prion protein

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Synthetic peptides corresponding to different mutated regions of the amyloid gene in familial Creutzfeldt-Jakob disease show enhanced in vitro formation of morphologically different amyloid fibrils

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Protein traffic on the heat shock promoter: parking, stalling, and trucking along

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Neurotoxicity of a prion protein fragment.

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Protein disaggregation mediated by heat-shock protein Hsp104.

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Molecular chaperone functions of heat-shock proteins

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Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern

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Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein

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Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells

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Lysosomes as key organelles in the pathogenesis of prion encephalopathies

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Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication.

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

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Expression of heat shock proteins in Alzheimer's disease

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Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid

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[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

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Cytoplasmic inheritance. Prion-like factors in yeast.

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Spontaneous neurodegeneration in transgenic mice with mutant prion protein

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Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein

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Ultrastructural localization of scrapie prion proteins in cytoplasmic vesicles of infected cultured cells

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Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells

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

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Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing.

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Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain.

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Scrapie prions selectively modify the stress response in neuroblastoma cells

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Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes.

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Prion diseases and neurodegeneration

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Etiology and pathogenesis of prion diseases.

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Novel proteinaceous infectious particles cause scrapie

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Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

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Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins

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Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells

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12 December 2020

Identifiers

DOI

10.1023/A:1020282205041

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15 February 2018

Dimensions Publication ID

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15 February 2018