Related Experiment Video
Updated: Aug 5, 2025

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
Published on: April 28, 2022
Structural basis of bioenergetic protein complexes in Alzheimer's disease pathogenesis
Lindsay McGregor1, Montserrat Soler-López1
1Structural Biology Group, European Synchrotron Radiation Facility (ESRF), CS 40220, 38043 Grenoble Cedex 9, France.
Abstract:
Alzheimer's disease (AD) is a progressive neurodegenerative disease with no cure where the underlying causes remain elusive. Mitochondrial dysfunction has become a prime suspect in AD pathogenesis since bioenergetic deficits precede the pathology. With advancing structural biology techniques at synchrotrons and cryo-electron microscopes, it is becoming possible to determine the structures of key proteins suspected to contribute to the initiation and propagation of AD, and investigate their interactions. In this review, we provide an overview of the recent developments concerning the structural aspects of mitochondrial protein complexes and their assembly factors involved the production of energy, in pursuit of therapies to halt or even reverse this disease in the early stages when mitochondria are most sensitive to amyloid toxicity.
Related Concept Videos
Alzheimer's Disease: Overview
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Alzheimer's Disease: Treatment
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
ATP Synthase: Mechanism

