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Amyloid Fibrils

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 Fibrils

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...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Protein Folding Quality Check in the RER

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...

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Related Experiment Video

Updated: Jun 28, 2026

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Published on: October 4, 2017

Adherent monomer-misfolded SOD1.

Yasuhiro Watanabe¹, Eri Morita, Yasuyo Fukada

¹Department of Neurology, Institute of Neurological Sciences, Faculty of Medicine, Tottori University, Yonago, Japan.

|October 24, 2008

Summary

Familial amyotrophic lateral sclerosis (ALS) involves mutations in copper-zinc superoxide dismutase (SOD1). Mutant SOD1 disrupts protein interactions, potentially driving ALS pathogenesis.

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Last Updated: Jun 28, 2026

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Published on: October 4, 2017

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Area of Science:

Neuroscience
Molecular Biology
Genetics

Background:

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease impacting cellular functions.
Familial ALS (FALS) linked to Cu/Zn superoxide dismutase (SOD1) mutations presents unclear pathogenic mechanisms.

Purpose of the Study:

To investigate cellular dysfunctions caused by SOD1 mutations in FALS.
To identify proteins interacting with mutant SOD1 in the spinal cord.

Main Methods:

Utilized transgenic mouse models expressing mutant SOD1 (Leu126delTT) or wild-type SOD1.
Employed FLAG-tagging, cross-linking, and shotgun proteomic analysis on spinal cord tissues.
Compared protein interactions in symptomatic mutant SOD1 mice (DF mice) versus disease-free wild-type mice (WF mice).

Main Results:

Identified 34 SOD1-interacting proteins in mutant SOD1 (DF) mouse preparations.
Detected interactions with only 4 proteins in wild-type SOD1 (WF) mouse preparations.
Mutant SOD1 exhibited altered protein-protein interaction profiles compared to wild-type.

Conclusions:

Disease-causing mutant SOD1 disrupts normal protein-protein interactions.
Impaired protein interactions may represent an early and critical step in FALS pathogenesis.
Findings provide insights into the molecular mechanisms underlying SOD1-related ALS.