Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

1.5K
Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
1.5K
Amyloid Fibrils03:03

Amyloid Fibrils

11.4K
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,...
11.4K
Alzheimer's Disease: Treatment01:22

Alzheimer's Disease: Treatment

667
Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
667

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Non-Classical Binding Mechanisms of Ferrocene-Modified Imatinib and Nilotinib Analogues in BCR-ABL1 Kinase Revealed by Computational Analysis.

Molecules (Basel, Switzerland)·2026
Same author

Novel Cinnamaldehyde Hydrazones: Design, In Silico Evaluation, Synthesis, and Cytotoxic Activity.

Molecules (Basel, Switzerland)·2026
Same author

An efficient computational chemistry approach to generating negative data for drug discovery pipeline validation.

Frontiers in bioinformatics·2026
Same author

Rational Design, Synthesis, and Molecular Docking of Novel Terpene Analogues of Imatinib, and Their Inhibition on Downstream BCR-ABL Signaling.

Pharmaceuticals (Basel, Switzerland)·2026
Same author

Percutaneous Drainage of a Post-ERCP Liver Abscess: Successful Management of a Rare Complication-A Case Report.

Clinical case reports·2026
Same author

Small-Molecule Inhibitors of Amyloid Beta: Insights from Molecular Dynamics-Part B: Natural Compounds.

Pharmaceuticals (Basel, Switzerland)·2025

Related Experiment Video

Updated: Dec 17, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.8K

Cellular polyamines condense hyperphosphorylated Tau, triggering Alzheimer's disease.

Stefan M Ivanov1,2, Mariyana Atanasova3, Ivan Dimitrov3

  • 1Faculty of Pharmacy, Medical University of Sofia, Dunav 2 st., Sofia, 1000, Bulgaria. sivanov@ddg-pharmfac.net.

Scientific Reports
|June 24, 2020
PubMed
Summary

Positively charged Tau is not condensed by cytosolic polyanions in Alzheimer's disease. Instead, negatively charged Tau is condensed by polycations, offering new therapeutic targets for tauopathies.

More Related Videos

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia
07:18

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

8.8K
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

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

Published on: October 10, 2017

9.3K

Related Experiment Videos

Last Updated: Dec 17, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.8K
Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia
07:18

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

8.8K
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

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

Published on: October 10, 2017

9.3K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cellular Biology

Background:

  • Alzheimer's disease (AD) pathogenesis involves Tau protein dysfunction.
  • The mechanisms of Tau condensation and fibrillization remain incompletely understood.
  • Existing hypotheses on Tau aggregation may overestimate polyanion roles and underestimate polyamine influence.

Purpose of the Study:

  • To investigate the role of cytosolic polycations and polyamines in Tau condensation.
  • To propose an alternative mechanism for Tau aggregation in Alzheimer's disease.
  • To challenge the prevailing view of Tau condensation by cytosolic polyanions.

Main Methods:

  • Extensive molecular dynamics simulations were performed.
  • Analysis was conducted on physiologically relevant model systems.
  • The interactions between Tau, polyamines, and polycations were modeled.

Main Results:

  • Results suggest that unmodified, positively charged Tau is not the primary substrate for condensation by cytosolic polyanions.
  • Evidence indicates that hyperphosphorylated, negatively charged Tau is condensed by cytosolic polycations.
  • This finding challenges the established model of Tau aggregation.

Conclusions:

  • The proposed mechanism highlights the role of polycations in the condensation of hyperphosphorylated Tau.
  • This research offers a new perspective on Tauopathies, including Alzheimer's disease.
  • The findings have significant implications for developing novel therapeutic strategies targeting Tau aggregation.