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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...
Shearing Stress01:18

Shearing Stress

Shearing stress, denoted by the Greek letter tau (τ), is stress caused by forces acting transversely on an object. These forces create internal ones within the entity in the plane where the external forces are applied. The resultant of these internal forces is the shear in the section.
The average shearing stress can be calculated by dividing the shear by the area of the cross-section.
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.

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Related Experiment Video

Updated: Jun 24, 2026

Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

How does shear affect Abeta fibrillogenesis?

Paul Hamilton-Brown, Innocent Bekard, William A Ducker

    The Journal of Physical Chemistry. B
    |April 16, 2009
    PubMed
    Summary
    This summary is machine-generated.

    Shear stress accelerates amyloid-beta (Abeta1-40) aggregation and protofibril formation but inhibits the creation of mature fibrils. This study reveals shear

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    Area of Science:

    • Biochemistry and Biophysics
    • Protein Misfolding Diseases
    • Amyloid Formation Dynamics

    Background:

    • Amyloid-beta (Abeta1-40) fibrillogenesis involves monomer aggregation, protofibril formation, and mature fibril maturation.
    • Understanding the influence of external forces like shear is crucial for elucidating amyloid formation pathways.

    Discussion:

    • Shear stress significantly impacts Abeta1-40 fibrillogenesis by accelerating early aggregation and protofibril assembly.
    • Conversely, continuous shear flow appears to hinder the final maturation into stable fibrils.
    • Hydrophobic interactions and drag minimization are proposed mechanisms for shear's effects on aggregation and alignment.

    Key Insights:

    • Shear enhances the rate of Abeta1-40 monomer aggregation and protofibril formation.
    • Shear inhibits the fusion and structural reorganization into mature Abeta1-40 fibrils.
    • Mechanical forces play a critical role in modulating the kinetics of amyloid fibril formation.

    Outlook:

    • Further investigation into shear-dependent amyloid formation could inform therapeutic strategies.
    • Exploring shear effects on other amyloidogenic proteins may reveal general principles of protein misfolding.
    • Developing controlled shear environments could aid in designing amyloid structures with specific properties.