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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...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

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Related Experiment Video

Updated: Jun 15, 2026

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

Protein aggregation diseases: pathogenicity and therapeutic perspectives.

Adriano Aguzzi1, Tracy O'Connor

  • 1Institute of Neuropathology, University Hospital of Zürich, Schmelzbergstrasse 12, CH8091 Zürich, Switzerland. adriano.aguzzi@usz.ch

Nature Reviews. Drug Discovery
|March 2, 2010
PubMed
Summary

Protein aggregation diseases, including Alzheimer's disease, are increasingly recognized. Understanding shared features offers new therapeutic strategies for these proteinopathies.

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Related Experiment Videos

Last Updated: Jun 15, 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

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

Published on: March 12, 2018

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Published on: December 17, 2021

Area of Science:

  • Biochemistry
  • Pathology
  • Neuroscience

Background:

  • Many diseases are linked to abnormal protein aggregate deposition.
  • Conditions like Alzheimer's disease and systemic amyloidoses are well-known examples.
  • Pathogenic protein aggregation occurs in extracellular, cytoplasmic, and nuclear compartments.

Purpose of the Study:

  • To highlight the expanding scope of diseases classified as amyloidoses.
  • To underscore the importance of understanding common structural and pathogenic features.
  • To explore novel therapeutic avenues for protein aggregation diseases.

Main Methods:

  • Review of current literature on protein aggregation diseases.
  • Analysis of common structural and pathogenic mechanisms.
  • Identification of potential overarching therapeutic targets.

Main Results:

  • Protein aggregation is implicated in a wider range of diseases than previously thought.
  • Shared molecular and cellular pathways underlie diverse protein aggregation disorders.
  • Therapeutic strategies targeting common mechanisms show promise.

Conclusions:

  • Many diseases previously unclassified may be considered amyloidoses.
  • A unified understanding of protein aggregation diseases facilitates therapeutic development.
  • Targeting precursor protein levels, aggregation processes, clearance, or toxicity pathways offers broad therapeutic potential.