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Related Experiment Video

Updated: Jun 10, 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

Aggregation modulating elements in mutant human superoxide dismutase 1.

Celeste M Karch¹, David R Borchelt

¹Department of Neuroscience, University of Florida, McKnight Brain Institute, Gainesville, 32610, USA. karchc@psychiatry.wustl.edu

Archives of Biochemistry and Biophysics

|August 5, 2010

Summary

This summary is machine-generated.

Mutations in superoxide dismutase 1 (SOD1) cause familial ALS. Specific SOD1 protein sequences (residues 42-50 and 109-123) were identified as critical in modulating the aggregation of mutant SOD1, a key disease process.

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4D Imaging of Protein Aggregation in Live Cells

4D Imaging of Protein Aggregation in Live Cells

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Last Updated: Jun 10, 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

4D Imaging of Protein Aggregation in Live Cells

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Area of Science:

Biochemistry
Neuroscience
Genetics

Background:

Familial amyotrophic lateral sclerosis (fALS) is linked to mutations in the superoxide dismutase 1 (SOD1) gene.
Misfolded and aggregated SOD1 proteins accumulate in affected tissues of fALS patients and mouse models.

Purpose of the Study:

To identify specific sequences within human SOD1 that influence the aggregation of fALS-associated mutant proteins.
To elucidate the structural elements involved in the modulation of SOD1 aggregation.

Main Methods:

Analysis of a panel of mutant SOD1 proteins.
Identification of critical amino acid residues modulating protein aggregation.

Main Results:

Two specific sequence elements in human SOD1, residues 42-50 (4th β-strand) and 109-123 (7th β-strand), were identified as critical modulators of aggregation.
These sequences are normally part of the core β-barrel structure in native SOD1.
Data suggest intermolecular interactions between these elements may drive mutant SOD1 aggregation.

Conclusions:

Specific sequences within SOD1 play a crucial role in the aggregation of fALS-associated mutant proteins.
Understanding these sequences may offer new therapeutic targets for fALS.
Intermolecular interactions involving residues 42-50 and 109-123 are implicated in the pathogenesis of fALS.