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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. 
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Related Experiment Video

Updated: Jun 19, 2026

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

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 6, 2013

Amyloidosis.

Mark B Pepys1

  • 1Center for Amyloidosis and Acute Phase Proteins, Department of Medicine, Royal Free and University College Medical School, London NW3 2PF, United Kingdom. m.pepys@medsch.ucl.ac.uk

Annual Review of Medicine
|January 18, 2006
PubMed
Summary
This summary is machine-generated.

Amyloidosis involves abnormal protein buildup, leading to organ damage and often delayed diagnosis. Advances in understanding, diagnosis, and treatment are improving patient outcomes, particularly with specialized care.

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Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

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Published on: March 7, 2019

Area of Science:

  • Biochemistry
  • Pathology
  • Medicine

Background:

  • Amyloidosis is a rare, often fatal disorder caused by extracellular deposition of misfolded proteins forming abnormal fibrils.
  • Over 23 different proteins can form amyloid in vivo, sharing a common structure but causing distinct clinical conditions.
  • Systemic amyloidosis affects multiple organs, leading to diagnostic challenges due to its rarity and variable presentation.

Purpose of the Study:

  • To provide an overview of amyloidosis, highlighting challenges in diagnosis and management.
  • To discuss recent advancements in understanding amyloidosis pathogenesis.
  • To emphasize the importance of specialized centers for improved patient outcomes.

Main Methods:

  • Literature review of amyloidosis pathogenesis, diagnosis, and treatment.
  • Analysis of clinical data and outcomes from specialist centers.
  • Synthesis of current knowledge on amyloid fibril formation and deposition.

Main Results:

  • Despite diverse protein origins, amyloid fibrils share a characteristic structure.
  • Delayed diagnosis is common due to rarity and variable organ involvement.
  • Recent progress in pathogenesis, diagnosis, and treatment has significantly improved outcomes.

Conclusions:

  • Amyloidosis remains a clinical challenge but is increasingly manageable with advanced understanding and specialized care.
  • Early diagnosis and management in specialist centers are crucial for improving survival and quality of life.
  • Continued research into amyloidosis pathogenesis holds promise for further therapeutic developments.