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,...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

You might also read

Related Articles

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

Sort by

Same author

Nascent protein retention at polysomes reduces kinetic barriers to self-assembly.

bioRxiv : the preprint server for biology·2026

Same author

Eukaryotic domestication of a bacterial immune protein following horizontal transfer.

bioRxiv : the preprint server for biology·2026

Same author

Adaptor protein supersaturation drives innate immune signaling and cell fate.

eLife·2026

Same author

Intracellular TDP-43 amyloid nucleates from arrested nascent condensates.

bioRxiv : the preprint server for biology·2026

Same author

Impacts of stress and aging on spore health in <i>Schizosaccharomyces pombe</i>.

Microbiology spectrum·2025

Same author

Neurodegeneration emerges at a cellular tipping point between aggregate accumulation and removal.

bioRxiv : the preprint server for biology·2025

Search research articles

Related Experiment Video

Updated: Aug 5, 2025

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystal.

Tej Kandola^1,2, Shriram Venkatesan¹, Jiahui Zhang³

¹Stowers Institute for Medical Research, Kansas City, MO 64110, USA.

Biorxiv : the Preprint Server for Biology

|March 30, 2023

Summary

Researchers identified a three-glutamine (Q) residue pattern as the key to polyglutamine (polyQ) amyloid nucleus formation. This discovery elucidates the molecular basis of polyQ diseases and offers a potential therapeutic strategy.

More Related Videos

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Related Experiment Videos

Last Updated: Aug 5, 2025

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Amyloid research aims to understand the nucleation event, crucial for protein aggregation in diseases like Huntington's.
The transient nature of nucleation has hindered structural characterization using traditional methods.

Approach:

Utilized an intracellular reporter to quantify amyloid formation frequency based on polyglutamine (polyQ) concentration and sequence.
Employed molecular simulations to model the structural basis of polyQ nucleation.
Investigated strategies to inhibit amyloid formation by exploiting the nucleation mechanism.

Key Points:

Polyglutamine (polyQ) amyloid nucleation involves specific three-glutamine (Q) segments at alternating positions.
These segments form a four-stranded steric zipper with interdigitated Q side chains.
The zipper structure self-inhibits further aggregation by engaging naive polyQ polypeptides.

Conclusions:

Uncovered the physical basis of the rate-limiting nucleation event for polyQ aggregation in cells.
Elucidated the molecular etiology of polyglutamine diseases.
Demonstrated a potential therapeutic strategy by genetically inducing oligomerization to block amyloid formation.