Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

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 Fibrils

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...

You might also read

Related Articles

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

Sort by

Same author

Black Hole Spectroscopy and Tests of General Relativity with GW250114.

Physical review letters·2026

Same author

GW250114: Testing Hawking's Area Law and the Kerr Nature of Black Holes.

Physical review letters·2025

Same author

Pathological Conditions of the Oral Cavity: Clinical and Therapeutic Perspectives.

La Clinica terapeutica·2025

Same author

Frequency-Dependent Squeezed Vacuum Source for the Advanced Virgo Gravitational-Wave Detector.

Physical review letters·2023

Same author

Search for Subsolar-Mass Binaries in the First Half of Advanced LIGO's and Advanced Virgo's Third Observing Run.

Physical review letters·2022

Same author

Constraints on Cosmic Strings Using Data from the Third Advanced LIGO-Virgo Observing Run.

Physical review letters·2021

Same journal

Erratum: Bacterial Turbulence at Compressible Fluid Interfaces [Phys. Rev. Lett. 136, 138301 (2026)].

Physical review letters·2026

Same journal

Unveiling Light-Quark Yukawa Flavor Structure via Dihadron Fragmentation at Lepton Colliders.

Physical review letters·2026

Same journal

Adaptable Route to Fast Coherent State Transport via Bang-Bang-Bang Protocols.

Physical review letters·2026

Same journal

Topological Transition and Emergence of Elasticity of Dislocation in Skyrmion Lattice: Beyond Kittel's Magnetic-Polar Analogy.

Physical review letters·2026

Same journal

Pound-Drever-Hall Method for Superconducting-Qubit Readout.

Physical review letters·2026

Same journal

Coupling a ^{73}Ge Nuclear Spin to an Electrostatically Defined Quantum Dot in Silicon.

Physical review letters·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 8, 2026

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

Simplified exactly solvable model for β-amyloid aggregation.

M Zamparo¹, A Trovato, A Maritan

¹Dipartimento di Fisica G. Galilei and CNISM, Università di Padova, v. Marzolo 8, PD-35131 Padova, Italy. marco.zamparo@pd.infn.it

Physical Review Letters

|September 28, 2010

Summary

This summary is machine-generated.

This study presents a statistical mechanical model for beta-amyloid aggregation, accounting for monomer concentration and peptide chain details. The model

More Related Videos

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Related Experiment Videos

Last Updated: Jun 8, 2026

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Area of Science:

Statistical mechanics
Biophysics
Computational biology

Background:

Beta-amyloid aggregation is implicated in neurodegenerative diseases.
Understanding the thermodynamics of this process is crucial.
Existing models often simplify the microscopic details of peptide chains.

Purpose of the Study:

To develop an exactly solvable statistical mechanical model for beta-amyloid aggregation.
To incorporate monomer concentration and microscopic peptide degrees of freedom.
To generalize existing protein folding models.

Main Methods:

Developed a simplified statistical mechanical model.
Explicitly included monomer concentration.
Considered microscopic degrees of freedom in both folded and fibrillar states.

Main Results:

The model is exactly solvable.
The phase diagram of the aggregation process was studied.
Qualitatively reproduced experimental outcomes of fibril formation.

Conclusions:

The proposed model provides a framework for understanding beta-amyloid thermodynamics.
The model captures key aspects of fibril formation.
This approach offers insights into the relationship between molecular details and macroscopic behavior.