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...

Fibril-associated Collagen

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

Chemistry of Carbohydrates

Chemistry of Carbohydrates

Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...

Fibrous Proteins

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

Polymers

Polymers

The word polymer is derived from the Greek words “poly” which means “many” and “mer” which means “parts”. Polymers are long chains of molecules composed of repeating units of smaller molecules, known as monomers. They either occur naturally, such as DNA and proteins, or can be constructed synthetically, like plastics. They have varied structural characteristics, such as linear chains, branched chains, or complex networks, that contribute to the properties that they exhibit. Additionally,...

You might also read

Related Articles

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

Sort by

Same author

Hypochlorous Acid-Gated Hydrolysis of a Phosphinate Ester Dye in Living Cells.

Journal of the American Chemical Society·2025

Same author

A Modular Platform for the Optogenetic Control of Small GTPase Activity in Living Cells Reveals Long-Range RhoA Signaling.

bioRxiv : the preprint server for biology·2025

Same author

Split-Small GTPase Reassembly as a Method to Control Cellular Signaling with User-Defined Inputs.

ACS chemical biology·2025

Same author

Methods for Controlling Small GTPase Activity.

Chembiochem : a European journal of chemical biology·2025

Same author

Acoustic loudness factor as an experimental parameter for benchmarking small molecule photoacoustic probes.

Nature communications·2025

Same author

Split-Small GTPase Reassembly as a Method to Control Cellular Signaling with User-Defined Inputs.

bioRxiv : the preprint server for biology·2025

Search research articles

Related Experiment Video

Updated: Jul 13, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

When conjugated polymers meet amyloid fibrils.

Cliff I Stains¹, Indraneel Ghosh

¹Department of Chemistry, University of Arizona, Tucson, Arizona 85721, USA.

ACS Chemical Biology

|August 22, 2007

Summary

Alzheimer's disease (AD) involves protein aggregation, but the toxic species remains unclear. New diagnostic agents can differentiate protein structures, aiding AD research.

Area of Science:

Neurology
Biochemistry
Molecular Biology

Background:

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by abnormal protein aggregation.
Protein aggregation is implicated in various diseases, including AD, Parkinson's disease, and amyloidosis.

Discussion:

The precise toxic molecular species in AD pathogenesis is still under investigation.
Distinguishing between different aggregated protein morphologies is crucial for understanding disease mechanisms.

Key Insights:

Recent advancements have led to diagnostic agents capable of differentiating protein aggregate structures.
These agents offer new possibilities for studying the complex molecular basis of AD.

Outlook:

More Related Videos

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Related Experiment Videos

Last Updated: Jul 13, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Further research utilizing these agents may clarify the toxic species in AD.

Improved diagnostics could lead to more targeted therapeutic strategies for neurodegenerative diseases.