Explore: Prpsc Proteins

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Source: The Open Library

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1Novel infectious agents and the central nervous system

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“Novel infectious agents and the central nervous system” Metadata:

  • Title: ➤  Novel infectious agents and the central nervous system
  • Author:
  • Language: English
  • Number of Pages: Median: 277
  • Publisher: Wiley
  • Publish Date:
  • Publish Location: New York - Chichester

“Novel infectious agents and the central nervous system” Subjects and Themes:

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Access and General Info:

  • First Year Published: 1988
  • Is Full Text Available: Yes
  • Is The Book Public: No
  • Access Status: Borrowable

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2Virus non conventionnels et affections du système nerveux central

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“Virus non conventionnels et affections du système nerveux central” Metadata:

  • Title: ➤  Virus non conventionnels et affections du système nerveux central
  • Authors:
  • Languages: fre - English
  • Number of Pages: Median: 258
  • Publisher: Masson
  • Publish Date:
  • Publish Location: Paris - New York

“Virus non conventionnels et affections du système nerveux central” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1983
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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Wiki

Source: Wikipedia

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Prion

that can normally break down proteins. The normal form of the protein is called PrPC, while the infectious form is called PrPSc – the C refers to 'cellular'

Creutzfeldt–Jakob disease

abnormal folding of a protein known as a prion. Infectious prions are misfolded proteins that can cause normally folded proteins to also become misfolded

Major prion protein

The protein can exist in multiple isoforms: the normal PrPC form, and the protease-resistant form designated PrPRes such as the disease-causing PrPSc (scrapie)

Kuru (disease)

forms of prion are designated as PrPC, which is a normally folded protein, and PrPSc, a misfolded form which gives rise to the disease. The two forms do

Scrapie

achieved by applying immunohistochemistry of disease-associated prion protein (PrPSC) to tissues collected post mortem, including obex (a brainstem structure)

Transmissible spongiform encephalopathy

seeding process. Because the abnormal proteins stick to each other, and because PrP is continuously produced by cells, PrPSc accumulates in the brain, harming

Bovine spongiform encephalopathy

normal brain prion protein (PrP) into the toxic, disease-related PrPSc form has started. At present, no way is known to detect PrPSc reliably except by

List of MeSH codes (D12.776)

100 – fusion proteins, bcr-abl MeSH D12.776.624.664.500.320 – fusion proteins, gag-onc MeSH D12.776.624.664.500.320.700 – oncogene protein p65(gag-jun)

Amyloid

healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells. These protein misfolding

Protein misfolding cyclic amplification

protein from diverse species. The newly generated protein exhibits the same biochemical, biological, and structural properties as brain-derived PrPSc