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Related Concept Videos

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...
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

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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...
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Dementia l: Introduction

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Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...

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Related Experiment Video

Updated: May 8, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Tauopathies and tau oligomers.

Akihiko Takashima1

  • 1Department of Aging Neurobiology, National Center for Geriatrics and Gerontology, Oobu-shi, Aichi, Japan.

Journal of Alzheimer'S Disease : JAD
|August 17, 2013
PubMed
Summary

Different tau aggregates contribute to distinct pathologies in tauopathies, a group of neurodegenerative diseases. Understanding these tau forms is key to addressing dementia and neuronal loss.

Area of Science:

  • Neuroscience
  • Pathology
  • Genetics

Background:

  • Tauopathies are neurodegenerative diseases marked by dementia and neurofibrillary tangles.
  • Mutations in the tau gene are linked to frontotemporal dementia with parkinsonism, indicating tau's role in disease.
  • In vitro studies reveal tau aggregates form intermediate oligomers before fibril formation.

Purpose of the Study:

  • To investigate the distinct roles of different tau aggregate forms in neurodegeneration.
  • To elucidate the pathological mechanisms underlying tauopathies.

Main Methods:

  • In vitro studies of tau aggregation kinetics.
  • Analysis of a mouse model expressing human tau protein.
  • Differential analysis of tau oligomers, granular tau oligomers, and fibrils.

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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

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Related Experiment Videos

Last Updated: May 8, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

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09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Main Results:

  • Tau forms intermediate aggregates (oligomers and granular oligomers) prior to fibril formation.
  • Neurofibrillary tangle formation, not the tangles themselves, correlates with synapse and neuron loss.
  • Hyperphosphorylated or oligomeric tau is implicated in synaptic loss.
  • Granular tau oligomers are specifically linked to neuronal loss.

Conclusions:

  • Distinct tau aggregate species mediate different pathological outcomes in tauopathies.
  • Targeting specific tau forms may offer therapeutic strategies for neurodegenerative diseases.