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Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Intrinsically Disordered Proteins

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[Prion protein].

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[Variant Creutzfeldt-Jakob disease (vCJD)].

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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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[Elusive function of prion protein].

Naomi S Hachiya1, Kiyotoshi Kaneko

  • 1Department of Neurophysiology, Tokyo Medical University.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|August 19, 2007
PubMed
Summary

The normal function of cellular prion protein (PrP(c)), a membrane glycoprotein, is unclear despite its role in prion diseases. Research explores its potential roles in cell survival and oxidative stress, but functional validation is ongoing.

Area of Science:

  • Neurobiology
  • Molecular Biology
  • Biochemistry

Context:

  • Cellular prion protein (PrP(c)) is a conserved glycoprotein found on cell membranes, notably in the brain, heart, and muscle.
  • Misfolding of PrP(c) into the infectious PrP(Sc) form is central to prion diseases.
  • The precise physiological function of PrP(c) remains incompletely understood.

Purpose:

  • To review current research on the biological functions of mammalian prion protein.
  • To highlight suggested roles for PrP(c) such as in oxidative stress, cell adhesion, copper uptake, and cell survival.
  • To underscore the need for further functional validation of identified PrP(c) interactions.

Summary:

  • Prion protein (PrP(c)) is a cell membrane-bound glycoprotein with an unclear normal function.

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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Last Updated: Jul 13, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Published on: August 8, 2017

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Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

  • Despite its involvement in prion infections, PrP(c) has proposed roles in cellular processes like oxidative stress defense and cell survival.
  • While numerous binding proteins and potential functions have been identified, experimental confirmation through functional assays is still lacking.
  • Impact:

    • Provides a consolidated overview of the current state of knowledge regarding PrP(c) function.
    • Identifies gaps in research and emphasizes the necessity for rigorous functional studies.
    • Contributes to a better understanding of prion protein biology, potentially aiding in the study of prion-related disorders.