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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Related Experiment Video

Updated: Jun 20, 2026

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

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

Published on: January 8, 2015

Prion protein and metal interaction: physiological and pathological implications.

Neena Singh1, Dola Das, Ajay Singh

  • 1The Department of Pathology, Case Western Reserve University, 2103, Cornell Road, Cleveland, Ohio 44106, USA. neena.singh@case.edu

Current Issues in Molecular Biology
|September 22, 2009
PubMed
Summary

Metal interactions contribute to neurotoxicity in prion diseases. Understanding prion protein (PrP) metal binding is crucial for explaining disease mechanisms and developing treatments for neurodegenerative disorders.

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Last Updated: Jun 20, 2026

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

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Published on: March 12, 2018

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Metal-induced free radicals mediate neurotoxicity in neurodegenerative diseases like Alzheimer's and Parkinson's.
  • Emerging evidence links metal dysregulation to neurotoxicity in prion diseases, involving PrP-scrapie (PrP(Sc)).

Purpose of the Study:

  • To review the physiological and pathological implications of prion protein (PrP) metal interactions in prion disease pathogenesis.
  • To elucidate the mechanisms underlying PrP(Sc)-associated neurotoxicity and brain metal imbalance.

Main Methods:

  • Literature review synthesizing current research on PrP-metal interactions.
  • Analysis of proposed hypotheses regarding PrP(C) function in metal metabolism and PrP(Sc) gain-of-toxic-function.

Main Results:

  • PrP(C) may play a role in metal homeostasis; its aggregation into PrP(Sc) could cause imbalance.
  • PrP(Sc) aggregates may sequester metals, forming redox-active complexes and inducing oxidative damage.
  • PrP-metal interactions can lead to oxidative damage and conversion of PrP(C) to a PrP(Sc)-like form.

Conclusions:

  • PrP-metal interactions are significant in prion disease pathogenesis, contributing to neurotoxicity.
  • Further research is needed to fully understand these interactions and their pathological consequences.