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

Subviral Agents

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...

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...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

You might also read

Related Articles

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

Sort by

Same author

Pancreatic Cancer Early Detection Biomarkers for High-Risk Individuals: Insights From the PRECEDE Consortium.

International journal of cancer·2026

Same author

Author Correction: High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs.

Nature chemistry·2026

Same author

Neuroinflammation and neurodegeneration trigger a specific splice form of ribosomal protein S24.

Brain : a journal of neurology·2026

Same author

A model-based prion vaccine protects a transgenic mouse line carrying a Gerstmann-Sträussler-Scheinker disease mutation.

Acta neuropathologica·2026

Same author

Creutzfeldt-Jakob disease is an Alzheimer's disease-related dementia.

Trends in molecular medicine·2026

Same author

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease model.

bioRxiv : the preprint server for biology·2026

Search research articles

Related Experiment Video

Updated: May 26, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Purification and Refolding to Amyloid Fibrils of (His)₆-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

Protease-resistant prions selectively decrease Shadoo protein.

Joel C Watts¹, Jan Stöhr, Sumita Bhardwaj

¹Institute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, United States of America.

|December 14, 2011

Summary

This summary is machine-generated.

Shadoo (Sho) protein levels decrease in prion-infected brains across multiple species. This inverse relationship with protease-resistant PrP(Sc) suggests Sho is a specific marker for prion disease.

More Related Videos

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Prion Safety Laboratory Swipe Test

Prion Safety Laboratory Swipe Test

Published on: February 14, 2025

Related Experiment Videos

Last Updated: May 26, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Purification and Refolding to Amyloid Fibrils of (His)₆-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Prion Safety Laboratory Swipe Test

Prion Safety Laboratory Swipe Test

Published on: February 14, 2025

Area of Science:

Neuroscience
Prion Biology
Protein Biochemistry

Background:

Prion diseases involve the misfolding of cellular prion protein (PrP(C)) into infectious PrP(Sc).
The precise mechanisms of PrP(Sc)-induced neuronal dysfunction are not fully understood.
Reduced Shadoo (Sho) levels were observed in prion-infected mouse brains, hinting at a potential diagnostic role.

Purpose of the Study:

To investigate whether Shadoo (Sho) protein levels serve as a reliable indicator of prion disease.
To explore the relationship between Sho levels and the presence of protease-resistant PrP(Sc) across various experimental models.

Main Methods:

Quantitative analysis of Sho protein levels in brain tissues from multiple prion-infected animal models (mice, hamsters, voles, sheep).
Examination of Sho levels in prion-infected transgenic mice overexpressing Sho and infected neuroblastoma cell lines.
Time-course studies to correlate Sho levels with protease-resistant PrP(Sc) accumulation.
Investigation of factors influencing the Sho-PrP(Sc) relationship, including membrane anchoring and PrP N-terminal domain.

Main Results:

Sho protein levels were consistently decreased in the brains of diverse species infected with various prion strains.
This reduction in Sho was observed in both natural and experimental prion infections, including in transgenic models and cell cultures.
Sho levels showed an inverse correlation with the amount of protease-resistant PrP(Sc).
Membrane anchoring and the N-terminal domain of PrP modulated the inverse relationship between Sho and PrP(Sc).

Conclusions:

Shadoo (Sho) is identified as the first non-PrP protein marker specifically associated with prion disease.
The inverse correlation between Sho and PrP(Sc) provides a potential biomarker for prion disease diagnosis.
Further research utilizing the Sho-PrP(Sc) paradigm may elucidate cellular pathways affected by prion infection.