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

9.2K
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,...
9.2K

You might also read

Related Articles

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

Sort by
Same author

<b>First record of the family Eriopisidae (Crustacea, Malacostraca, Amphipoda) from Southern Sea, Korea with description of one new species</b>.

Zootaxa·2026
Same author

To Explore or Not to Explore the Neck: The Role of Cervical Lymph Node Dissection in pT2-3 Esophageal Squamous Cell Carcinoma.

Annals of surgical oncology·2026
Same author

Efficacy and safety of Doxycycline versus Macrolides for <i>Mycoplasma pneumoniae</i> INfectiOn in Children (DOMINO): a protocol for a multicentre, randomised, open-label, superiority trial.

BMJ open·2026
Same author

Clinical impact of local consolidative therapy in EGFR-mutant metastatic NSCLC: A propensity-matched multicenter analysis.

Lung cancer (Amsterdam, Netherlands)·2026
Same author

Effect of Donor Lung Resection Technique on Bronchopleural Fistula in Transplantation: Pulmonary Tailoring Versus Hilar Dissection.

Yonsei medical journal·2026
Same author

Patients-specific virtual surgical navigation for lung segmentectomy: a prospective multicenter study.

Frontiers in oncology·2026

Related Experiment Video

Updated: May 23, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.2K

Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways.

Li Wang1, Sanghwan Park2, Jae Hong Choi2

  • 1Biomechanics Laboratory, College of Sport Science, Sungkyunkwan University (SKKU), Suwon, Republic of Korea.

Journal of Biomolecular Structure & Dynamics
|March 8, 2025
PubMed
Summary

Amyloid beta (Aβ) protein interactions influence Alzheimer's disease. This study reveals how Aβ40 and Aβ42 concentrations and seeds alter aggregation pathways and aggregate structures.

Keywords:
Aβ isoformCross-interactionaggregationfibril seedoligomer seed

More Related Videos

A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

11.8K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

9.7K

Related Experiment Videos

Last Updated: May 23, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.2K
A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

11.8K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

9.7K

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Amyloid beta (Aβ) protein self-aggregation is central to Alzheimer's disease pathogenesis.
  • The impact of cross-interactions between different Aβ isoforms on aggregation pathways remains poorly understood.

Purpose of the Study:

  • To investigate the cross-interaction between Aβ40 and Aβ42 during aggregation.
  • To determine how varying concentrations and seeding affect aggregation kinetics and structures.

Main Methods:

  • Studied Aβ40 and Aβ42 aggregation kinetics in mixtures.
  • Analyzed aggregate structures under varied Aβ isoform concentrations.
  • Investigated the effect of Aβ40/Aβ42 oligomer and fibril seeds on aggregation pathways.

Main Results:

  • Mixtures of Aβ40 and Aβ42 monomers exhibit concentration-dependent aggregation.
  • Different concentrations of Aβ isoforms induce distinct aggregate structures (oligomers, fibrils) with varied morphologies and flexibilities.
  • Oligomer and fibril seeds significantly influence both aggregation kinetics and resulting Aβ aggregate structures.

Conclusions:

  • Aβ isoform cross-interaction at the primary nucleation level plays a critical role in determining aggregation pathways.
  • Understanding these interactions is key to elucidating Alzheimer's disease mechanisms.