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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...
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...
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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Caspase cleavage of APP contributes to amyloid beta-protein induced synaptic injury.

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Related Experiment Video

Updated: Jul 20, 2026

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

The amyloid precursor protein: beyond amyloid.

Hui Zheng1, Edward H Koo

  • 1Huffington Center on Aging and Department of Molecular & Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA. huiz@bcm.tmc.edu

Molecular Neurodegeneration
|August 26, 2006
PubMed
Summary

Amyloid precursor protein (APP) is central to Alzheimer's disease (AD) pathogenesis. This review explores APP's physiological roles beyond its link to beta-amyloid (Abeta) peptide production and amyloid plaques.

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Last Updated: Jul 20, 2026

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

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

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

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Amyloid precursor protein (APP) processing generates beta-amyloid (Abeta) peptides, implicated in Alzheimer's disease (AD) pathogenesis.
  • Mutations and duplications in APP are causal for familial Alzheimer's disease (FAD).
  • Despite its role in AD, APP possesses putative physiological functions that warrant investigation.

Purpose of the Study:

  • To review the current understanding of the physiological functions of Amyloid precursor protein (APP).
  • To explore APP's biological roles beyond its established connection to Alzheimer's disease pathology.

Main Methods:

  • Review of in vitro biochemical studies proposing models of APP function.
  • Analysis of genetic studies involving gain- and loss-of-function APP mutants in Drosophila and mouse models.
  • Synthesis of current research on APP's in vivo biological activities.

Main Results:

  • APP has diverse physiological roles that are increasingly being elucidated.
  • In vitro and in vivo studies provide insights into APP's normal biological functions.
  • APP's functions extend beyond its well-known involvement in Abeta production.

Conclusions:

  • Understanding APP's physiological functions is crucial for a comprehensive view of its role in health and disease.
  • Further research into APP's normal functions may reveal new therapeutic targets for Alzheimer's disease.
  • APP is a multifaceted protein with significant biological activities beyond its pathogenic implications.