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Related Concept Videos

Amyloid Fibrils03:03

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...
Amyloid Fibrils03:03

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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Related Experiment Video

Updated: Jul 17, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Novel modulators of amyloid-beta precursor protein processing.

Bor Luen Tang1, Yih Cherng Liou

  • 1Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore. bchtbl@nus.edu.sg

Journal of Neurochemistry
|January 24, 2007
PubMed
Summary

New molecules regulate amyloid precursor protein (APP) processing, reducing amyloid-beta (Abeta) production. Understanding these modulators offers potential therapeutic targets for Alzheimer's disease, a neurodegenerative disorder.

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Related Experiment Videos

Last Updated: Jul 17, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

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

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

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) pathogenesis involves amyloid precursor protein (APP) processing by secretases.
  • Genetic factors like APP mutations and apolipoprotein E4 influence AD risk.
  • Amyloid-beta (Abeta) production is central to the amyloidogenic pathway.

Purpose of the Study:

  • To review novel cellular modulators of APP processing and Abeta secretion.
  • To explore the mechanisms by which these molecules impact Abeta generation.
  • To identify potential therapeutic strategies for Alzheimer's disease.

Main Methods:

  • Literature review of studies on APP processing modulators.
  • Analysis of molecular interactions between proteins and APP or secretases.
  • Investigation of signaling pathways, including Rho GTPases.

Main Results:

  • Several novel modulators identified: Mints/X11s, RTN-3, RTN-4/Nogo-B, NgR, Pin1, and Rho GTPases.
  • Direct binding of Mints and NgR to APP; RTN3 and Nogo-B interact with BACE1.
  • Interactions generally lead to reduced Abeta generation in vitro and in vivo.
  • Inhibition of Rho/ROCK and Rac1 activity correlates with reduced Abeta production.

Conclusions:

  • Novel modulators significantly impact APP processing and Abeta production.
  • Understanding these mechanisms provides insight into AD pathophysiology.
  • Targeting these pathways offers promising therapeutic avenues for Alzheimer's disease.