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

9.7K
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,...
9.7K
Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

615
Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
615

You might also read

Related Articles

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

Sort by
Same author

Pathology and Therapeutic Significance of Fibroblast Growth Factors.

Targets (Basel)·2026
Same author

Incorporation of unnatural amino acid into human acidic fibroblast growth factor 1 (FGF1) protein with increased thermal, chemical stability and enhanced bioactivity.

Archives of biochemistry and biophysics·2025
Same author

Signaling of Mitogenic and Metabolic Activities by Fibroblast Growth Factors.

Journal of cellular signaling·2025
Same author

Oxime-Ether Group Transfer to Unpolarized C(sp3)─H Bonds via Light-Induced HAT Catalysis.

Chemistry, an Asian journal·2025
Same author

Fibroblast Growth Factors: Roles and Emerging Therapeutic Applications.

Current drug targets·2025
Same author

Overexpression and biophysical and functional characterization of a recombinant FGF21.

Biophysical reports·2025

Related Experiment Video

Updated: Aug 19, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.2K

Amyloidogenesis: What Do We Know So Far?

Zeina Alraawi1, Nayan Banerjee2, Srujana Mohanty3

  • 1Department of Chemistry and Biochemistry, Fulbright College of Art and Science, University of Arkansas, Fayetteville, AR 72701, USA.

International Journal of Molecular Sciences
|November 26, 2022
PubMed
Summary
This summary is machine-generated.

Protein aggregation and amyloidosis are key in neurodegenerative diseases like Alzheimer's and Parkinson's. This review explores amyloid formation, biophysical techniques, and therapeutic challenges, including COVID-19's potential impact.

Keywords:
Aβ peptideCOVID-19 and amyloidosisamyloid precursor proteinamyloid related diseasesamyloid structure analysisamyloidsfibril formationphysical techniques in amyloid analysisprotein aggregation

More Related Videos

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease
06:52

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

Published on: July 6, 2019

9.4K
Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

10.7K

Related Experiment Videos

Last Updated: Aug 19, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.2K
Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease
06:52

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

Published on: July 6, 2019

9.4K
Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

10.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Protein aggregation, particularly amyloidosis, is implicated in neurodegenerative diseases such as Alzheimer's and Parkinson's.
  • Despite extensive research, the precise mechanisms of protein aggregate formation remain incompletely understood.
  • A comprehensive understanding is crucial for developing effective therapeutic strategies.

Observation:

  • This review provides a chronological overview of amyloid discovery and research.
  • It details various biophysical techniques used to analyze amyloid structure, formation mechanisms, and kinetics.
  • The role of the biophysicochemical and cellular environment in protein aggregation is examined.

Findings:

  • Aggregation may not be limited to specific proteins but influenced by environmental factors.
  • Therapeutic strategies for neurodegenerative diseases involving protein aggregation have shown limited success in clinical trials.
  • The potential for viral infections, like COVID-19, to trigger amyloidosis is discussed.

Implications:

  • Further research into protein aggregation mechanisms is needed to overcome therapeutic failures.
  • Understanding environmental influences could lead to novel diagnostic or therapeutic targets.
  • Exploring amyloid applications as biomaterials presents new avenues for innovation.