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Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Related Experiment Video

Updated: Mar 1, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

Direct interaction between selenoprotein R and Aβ42.

Chao Wang¹, Ping Chen², Xiaohong He³

¹Shenzhen Center for Disease Control and Prevention, 518055, Shenzhen, China.

Biochemical and Biophysical Research Communications

|June 6, 2017

Summary

This summary is machine-generated.

Selenoprotein R (SelR) interacts with amyloid-beta 42 (Aβ42), potentially modulating its aggregation. This discovery offers new insights into Alzheimer's disease (AD) prevention strategies involving SelR.

Keywords:

Alzheimer's disease (AD)Amyloid-β (Aβ) peptide Protein interaction SelR

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Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Amyloid-beta (Aβ) peptide aggregation is central to Alzheimer's disease (AD) progression.
The redox state of methionine at position 35 (Met35) in Aβ influences its biological activity and aggregation pathway.
Selenoprotein R (SelR), an antioxidative selenoenzyme, reduces oxidized methionine (MetO) to methionine (Met), maintaining cellular redox balance.

Purpose of the Study:

To investigate the relationship between Selenoprotein R (SelR) and amyloid-beta (Aβ) in the context of Alzheimer's disease.
To determine if SelR directly interacts with Aβ42 and modulates its aggregation.

Main Methods:

Fluorescence resonance energy transfer (FRET) assays to detect direct interaction.
Co-immunoprecipitation (co-IP) to confirm binding.
Pull-down assays to further validate the interaction between SelR and Aβ42.

Main Results:

Direct interaction between SelR and Aβ42 was confirmed using FRET, co-IP, and pull-down assays.
SelR's ability to modulate Aβ42 aggregation was demonstrated.
The findings highlight SelR's potential role in the biological functions within the human brain relevant to AD.

Conclusions:

Selenoprotein R directly interacts with Aβ42.
SelR has the capacity to modulate Aβ42 aggregation, suggesting a potential role in Alzheimer's disease pathogenesis.
This study opens a novel research avenue for exploring SelR's mechanism in AD prevention.