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

Amyloid Fibrils03:03

Amyloid Fibrils

10.2K
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,...
10.2K
Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism01:21

Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism

412
Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
412
Polymer Classification: Crystallinity01:21

Polymer Classification: Crystallinity

3.2K
Unlike ionic or small covalent molecules, polymers do not form crystalline solids due to the diffusion limitations of their long-chain structures. However, polymers contain microscopic crystalline domains separated by amorphous domains.
Crystalline domains are the regions where polymer chains are aligned in an orderly manner and held together in proximity by intermolecular forces. For example, chains in the crystalline domains of polyethylene and nylon are bound together by van der Waals...
3.2K
Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

705
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...
705
Protein and Protein Structure02:15

Protein and Protein Structure

82.3K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
82.3K

You might also read

Related Articles

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

Sort by
Same author

Large-scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation.

FEBS open bio·2026
Same author

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies.

Molecular systems biology·2026
Same author

Generation and characterization of human induced pluripotent stem cells from neuropathologically confirmed multiple system atrophy patient-derived fibroblasts.

Frontiers in immunology·2026
Same author

Design, Synthesis and Evaluation of the First 2-Alkynyl(aza)indole <sup>18</sup>F Probe Targeting α-Synuclein Aggregates.

Pharmaceuticals (Basel, Switzerland)·2025
Same author

Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation.

The EMBO journal·2025
Same author

In vivo validation of novel non-invasive PHP.eB AAVs as a potential therapeutic approach for alpha-synucleinopathies.

Acta neuropathologica communications·2025

Related Experiment Video

Updated: Sep 27, 2025

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

6.3K

Amyloid polymorphs and pathological diversities.

Ronald Melki1

  • 1Institut Francois Jacob (MIRCen), CEA and Laboratory of Neurodegenerative Diseases, CNRS, 18 Route du Panorama, 92265, Fontenay-Aux-Roses cedex, France.

Neurochemistry International
|April 8, 2022
PubMed
Summary
This summary is machine-generated.

Protein aggregates in the brain cause neurodegenerative diseases. This review explores how one protein can cause diverse pathologies through different molecular mechanisms.

More Related Videos

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

3.3K
Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

13.6K

Related Experiment Videos

Last Updated: Sep 27, 2025

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

6.3K
Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

3.3K
Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

13.6K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Protein aggregates in the central nervous system are linked to neurodegenerative diseases.
  • Distinct diseases often involve distinct protein aggregates.
  • The aggregation of a single protein type leading to varied pathologies is puzzling.

Purpose of the Study:

  • To review the molecular and mechanistic basis for pathological diversity arising from single protein aggregation.
  • To connect molecular processes with observed pathological outcomes in neurodegenerative conditions.

Main Methods:

  • Literature review focusing on molecular mechanisms of protein aggregation.
  • Analysis of studies linking specific protein aggregation pathways to distinct disease pathologies.

Main Results:

  • Identified diverse molecular pathways driving the aggregation of specific proteins.
  • Correlated distinct aggregation mechanisms with different pathological manifestations in the central nervous system.

Conclusions:

  • Molecular and mechanistic variations explain how a single protein can cause diverse neurodegenerative pathologies.
  • Understanding these diverse pathways is crucial for developing targeted therapies for proteinopathies.