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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...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

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 microglia. Abnormal...
The Proteasome01:13

The Proteasome

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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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Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

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Related Experiment Video

Updated: May 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Ubiquitous amyloids.

Wojciech Pulawski1, Umesh Ghoshdastider, Vincenza Andrisano

  • 1Faculty of Chemistry, University of Warsaw, ul. Pasteura 1, 02-093 Warsaw, Poland.

Applied Biochemistry and Biotechnology
|February 22, 2012
PubMed
Summary
This summary is machine-generated.

Amyloids and prion proteins can cause incurable diseases but also have beneficial roles. Understanding their dual nature is key to health and industrial applications.

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Rapid Generation of Amyloid from Native Proteins In vitro
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomaterials

Background:

  • Amyloids and prion proteins are linked to incurable diseases and can transmit illness.
  • Organisms utilize specific, non-pathogenic amyloid forms for structural benefits.
  • Amyloid fibrils are increasingly explored for nanotechnology and industrial uses.

Purpose of the Study:

  • To explore the dual role of amyloids and prion proteins in disease and health.
  • To highlight the potential of beneficial amyloids in biological systems and engineering.

Main Methods:

  • Literature review of amyloid and prion protein research.
  • Analysis of disease transmission mechanisms.
  • Investigation of beneficial amyloid functions and properties.

Main Results:

  • Amyloidal state is intrinsic to proteins, central to aging-related diseases.
  • "Good" amyloids offer health benefits and possess valuable mechanical properties.
  • Infectious amyloids and prions pose significant health risks.

Conclusions:

  • Amyloids exhibit a dichotomy: pathogenic roles in disease and beneficial functions in health and industry.
  • Further research into amyloid structure-function relationships is crucial for therapeutic and technological advancements.