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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...
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,...
Mitochondria01:37

Mitochondria

Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

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Related Experiment Video

Updated: Jun 3, 2026

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

Amyloid-Beta interaction with mitochondria.

Lucia Pagani1, Anne Eckert

  • 1Neurobiology Laboratory for Brain Aging and Mental Health, Psychiatric University Clinics, University of Basel, Wilhelm Klein-Straße 27, 4012 Basel, Switzerland.

International Journal of Alzheimer'S Disease
|April 5, 2011
PubMed
Summary
This summary is machine-generated.

Alzheimer's disease involves amyloid-beta (Aβ) damaging neurons. This study shows Aβ directly harms mitochondria, impacting energy production and increasing oxidative stress, supporting a revised Alzheimer cascade mitochondrial hypothesis.

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Quantitative Analysis of Mitochondria-Associated Endoplasmic Reticulum Membrane (MAM) Stabilization in a Neural Model of Alzheimer's Disease (AD)
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Quantitative Analysis of Mitochondria-Associated Endoplasmic Reticulum Membrane (MAM) Stabilization in a Neural Model of Alzheimer's Disease (AD)

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Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
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Last Updated: Jun 3, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Quantitative Analysis of Mitochondria-Associated Endoplasmic Reticulum Membrane (MAM) Stabilization in a Neural Model of Alzheimer's Disease (AD)
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Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Mitochondrial dysfunction is central to Alzheimer's disease (AD) neurotoxicity.
  • Amyloid-beta (Aβ) and its precursor (AβPP) are increasingly studied within cells, including mitochondria.

Purpose of the Study:

  • To explore the intracellular localization of Aβ and AβPP.
  • To investigate how Aβ accesses mitochondria.
  • To summarize evidence linking Aβ to mitochondrial dysfunction in AD.

Main Methods:

  • Review of current literature on Aβ/AβPP intracellular localization.
  • Analysis of evidence from postmortem AD brains, cell models, and animal models.
  • Focus on Aβ interactions with various mitochondrial compartments and proteins.

Main Results:

  • Aβ can access and accumulate within mitochondria.
  • Aβ disrupts mitochondrial function via impaired oxidative phosphorylation and increased reactive oxygen species (ROS).
  • Aβ alters mitochondrial dynamics and interacts with key mitochondrial proteins.

Conclusions:

  • Aβ directly induces mitochondrial dysfunction, contributing to neuronal toxicity in AD.
  • Aβ interacts with multiple mitochondrial targets, from the outer membrane to the matrix.
  • A modified Alzheimer cascade mitochondrial hypothesis is proposed based on these findings.