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

Alzheimer's Disease: Treatment01:22

Alzheimer's Disease: Treatment

1.1K
Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
1.1K
Amyloid Fibrils03:03

Amyloid Fibrils

12.2K
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,...
12.2K

You might also read

Related Articles

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

Sort by
Same author

MRI-based axis-referenced morphometric model corresponding to lamellar organization for assessing hippocampal atrophy in dementia.

Human brain mapping·2024
Same author

Luteolin enhances drug chemosensitivity by downregulating the FAK/PI3K/AKT pathway in paclitaxel‑resistant esophageal squamous cell carcinoma.

International journal of molecular medicine·2024
Same author

[A multicenter clinical study of critically ill patients with sepsis complicated with acute kidney injury in Beijing: incidence, clinical characteristics and outcomes].

Zhonghua wei zhong bing ji jiu yi xue·2024
Same author

Interferon-α could induce liver steatosis to promote HBsAg loss by increasing triglyceride level.

Heliyon·2024
Same author

Synergistic immunochemotherapy targeted SAMD4B-APOA2-PD-L1 axis potentiates antitumor immunity in hepatocellular carcinoma.

Cell death & disease·2024
Same author

Surface engineering of zinc plate by self-growth three-dimensional-interconnected zinc silicate nanosheets effectively guiding the deposition of zinc ion for aqueous Zn metal battery.

Journal of colloid and interface science·2024

Related Experiment Video

Updated: Mar 1, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.7K

Chemical Methods to Knock Down the Amyloid Proteins.

Na Gao1, Yong-Xiang Chen2, Yu-Fen Zhao3

  • 1Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China. gaona_chocolate@126.com.

Molecules (Basel, Switzerland)
|June 8, 2017
PubMed
Summary

Novel chemical strategies are emerging to combat amyloid diseases by accelerating the clearance of harmful amyloid proteins. This review highlights cutting-edge methods like PROTAC and light-activated molecules for effective amyloid reduction.

Keywords:
amyloid proteinschemical methodsdegradation

More Related Videos

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

12.5K
Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease
08:25

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Published on: April 19, 2021

4.1K

Related Experiment Videos

Last Updated: Mar 1, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.7K
A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

12.5K
Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease
08:25

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Published on: April 19, 2021

4.1K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Medicinal Chemistry

Background:

  • Amyloid proteins are implicated in severe human diseases.
  • Current treatments for amyloid diseases are limited, necessitating new therapeutic approaches.
  • Accelerating amyloid protein clearance is a promising treatment strategy.

Purpose of the Study:

  • To review recent advancements in chemical methods for reducing amyloid proteins.
  • To explore novel strategies for treating amyloid diseases.

Main Methods:

  • Proteolysis-targeting chimera (PROTAC) strategy
  • Recognition-cleavage strategy
  • Chaperone-mediated autophagy (CMA) strategy
  • Selectively light-activatable organic and inorganic molecules
  • Other chemical strategies

Main Results:

  • The review synthesizes current chemical approaches for amyloid protein knockdown.
  • Various innovative chemical strategies are presented, offering potential therapeutic avenues.

Conclusions:

  • Chemical methods represent a promising frontier for developing effective treatments for amyloid diseases.
  • Further research into these chemical strategies could lead to breakthroughs in managing amyloid pathologies.