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Related Concept Videos

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...
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. 
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Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Published on: January 8, 2015

Allosteric function and dysfunction of the prion protein.

Rafael Linden1, Yraima Cordeiro, Luis Mauricio T R Lima

  • 1Instituto de Biofísica Carlos Chagas Filho, UFRJ, CCS, Cidade Universitária, Rio de Janeiro, Brazil. rlinden@biof.ufrj.br

Cellular and Molecular Life Sciences : CMLS
|October 11, 2011
PubMed
Summary
This summary is machine-generated.

Transmissible spongiform encephalopathies (TSEs) involve prion protein (PrP(C)) misfolding. PrP(C) acts as a scaffold protein, where allosteric dysfunction may corrupt cell signaling and contribute to neurodegenerative diseases.

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Protein Misfolding Cyclic Amplification of Prions
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Protein Misfolding Cyclic Amplification of Prions

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Last Updated: May 28, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

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Published on: January 8, 2015

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

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Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are neurodegenerative conditions.
  • Prion protein (PrP(C)) aggregation and conformational changes are central to TSE pathogenesis.
  • PrP(C) is increasingly recognized for its role as a cell surface scaffold protein.

Purpose of the Study:

  • To review evidence for the allosteric functions of PrP(C).
  • To explore the involvement of PrP(C) allosteric effects in signaling module assembly and conformational responses.
  • To discuss the potential role of allosteric dysfunction in TSE pathogenesis and other diseases.

Main Methods:

  • Literature review of existing research on PrP(C) function and allosteric mechanisms.
  • Analysis of data linking PrP(C) interactions to signaling pathways.
  • Synthesis of evidence regarding PrP(C) conformational changes and disease association.

Main Results:

  • PrP(C) exhibits allosteric functions, a common trait of scaffold proteins.
  • Allosteric effects mediate the assembly of multi-component signaling modules at the cell surface.
  • PrP(C) allosteric dysfunction is implicated in progressive signal corruption, relevant to both physiology and pathology.

Conclusions:

  • Allosteric modulation of PrP(C) is crucial for its physiological roles and pathological involvement in TSEs.
  • Dysfunctional allosteric activity of PrP(C) may underlie signal transduction errors in neurodegenerative diseases.
  • Understanding PrP(C) allosteric properties offers insights into TSEs and other non-communicable degenerative conditions.