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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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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Subviral Agents01:29

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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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Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

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Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and...
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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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When amyloids become prions.

Raimon Sabate1

  • 1Conformational Diseases Group; Department of Physical Chemistry; Faculty of Pharmacy; University of Barcelona (UB); Barcelona, Spain; Institut of Nanoscience and Nanotechnology of the University of Barcelona (IN2UB); Barcelona, Spain.

Prion
|May 17, 2014
PubMed
Summary
This summary is machine-generated.

Protein aggregation causes conformational diseases like Alzheimer disease and prion diseases. Intrinsic cytotoxicity and aggregation nuclei per cell may explain differing infectious capacities of amyloid proteins.

Keywords:
Alzheimer diseaseCreutzfeldt–Jakob diseaseamyloidamyloid cytotoxicityamyloid transmissionpriontransmissible spongiform encephalopathy

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Conformational diseases involve protein aggregation into amyloid structures.
  • These diseases range from neurodegenerative disorders like Alzheimer disease (AD) to infectious transmissible spongiform encephalopathies (TSEs), collectively known as prion diseases.
  • The varying infectious potential of different amyloid-forming proteins remains unexplained.

Purpose of the Study:

  • To investigate the underlying factors determining the infectious capacity of amyloid proteins.
  • To explore the roles of intrinsic cytotoxicity and intracellular aggregation nucleation in prion disease transmission.

Main Methods:

  • This study proposes a theoretical framework based on existing literature and biochemical principles.
  • It analyzes the relationship between protein aggregation kinetics, cellular toxicity, and disease transmissibility.

Main Results:

  • Amyloid proteins share the potential to act as prions, facilitating cell-to-cell or organism-to-organism spread.
  • Intrinsic cytotoxicity and the number of aggregation nuclei within a cell are proposed as key determinants of an amyloid's infectious capacity.

Conclusions:

  • Understanding the factors governing amyloid infectivity is crucial for differentiating between various conformational diseases.
  • Intrinsic cytotoxicity and aggregation nucleation offer a potential explanation for the spectrum of prion disease infectivity.