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

12.1K
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,...
12.1K
Amyloid Fibrils03:03

Amyloid Fibrils

6.5K
6.5K

You might also read

Related Articles

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

Sort by
Same author

Infection of Rhesus Macaques with O'nyong-nyong virus UVRI-0804 recapitulates key aspects of human clinical disease.

PLoS neglected tropical diseases·2026
Same author

Jamestown Canyon virus rapidly adapts to mosquito cells through multiple M segment mutations.

bioRxiv : the preprint server for biology·2026
Same author

Emulating the gingival-tooth interface during bacterial, fungal, and viral infection in a microphysiological model of the human oral cavity.

bioRxiv : the preprint server for biology·2026
Same author

La Crosse virus, but not Jamestown Canyon virus, is dependent on the host translation termination factor eRF1 due to changes in the nonstructural protein NSm.

mBio·2026
Same author

Hantavirus disease and the need for pathogenesis-guided therapy.

The Journal of experimental medicine·2026
Same author

Distinct virus-derived circular RNA molecule influences host response during SARS-CoV-2 infection.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Feb 20, 2026

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
07:07

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Published on: August 3, 2021

3.2K

A RHIM with a View: FLYing with Functional Amyloids.

Sunny Shin1, Sara Cherry1

  • 1Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104, USA.

Immunity
|October 19, 2017
PubMed
Summary

Proteins in the insect immune deficiency (IMD) pathway form functional amyloids, similar to mammalian RIPK proteins, which regulate immune responses. This amyloid formation presents a potential regulatory point in biological processes.

Area of Science:

  • * Innate immunity
  • * Molecular biology
  • * Cellular signaling

Background:

  • * The Drosophila immune deficiency (IMD) pathway recognizes bacterial peptidoglycan.
  • * This recognition activates NF-κB, initiating an immune response.
  • * The molecular mechanisms underlying IMD pathway activation require further elucidation.

Purpose of the Study:

  • * To investigate the structural and functional properties of proteins within the Drosophila IMD pathway.
  • * To identify novel regulatory mechanisms governing innate immune signaling.

Main Methods:

  • * Bioinformatic analysis to identify conserved protein motifs.
  • * In vitro assays to assess protein aggregation and amyloid formation.
  • * Genetic manipulation in Drosophila to study pathway function.

More Related Videos

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.4K
Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
13:31

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

9.3K

Related Experiment Videos

Last Updated: Feb 20, 2026

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
07:07

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Published on: August 3, 2021

3.2K
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.4K
Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
13:31

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

9.3K

Main Results:

  • * Proteins in the IMD pathway self-assemble into functional amyloids.
  • * A cryptic motif, similar to the RHIM motif in mammalian RIPK proteins, mediates this amyloid formation.
  • * Amyloid formation is subject to negative regulation.

Conclusions:

  • * Functional amyloid formation is a key feature of the Drosophila IMD pathway.
  • * This process, involving a RHIM-like motif, is conserved across species.
  • * Negative regulation of amyloid formation offers a novel control point for immune responses.