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Updated: Jun 25, 2025

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
Published on: July 27, 2016
Each big journey starts with a first step: Importance of oligomerization
Mansoureh Mirza Agha1, Fatemeh Aziziyan1, Vladimir N Uversky2
1Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
Abstract:
Protein oligomers, widely found in nature, have significant physiological and pathological functions. They are classified into three groups based on their function and toxicity. Significant advancements are being achieved in the development of functional oligomers, with a focus on various applications and their engineering. The antimicrobial peptides oligomers play roles in death of bacterial and cancer cells. The predominant pathogenic species in neurodegenerative disorders, as shown by recent results, are amyloid oligomers, which are the main subject of this chapter. They are generated throughout the aggregation process, serving as both intermediates in the subsequent aggregation pathways and ultimate products. Some of them may possess potent cytotoxic properties and through diverse mechanisms cause cellular impairment, and ultimately, the death of cells and disease progression. Information regarding their structure, formation mechanism, and toxicity is limited due to their inherent instability and structural variability. This chapter aims to provide a concise overview of the current knowledge regarding amyloid oligomers.
Insights
Protein oligomers have critical roles in health and disease. This chapter focuses on amyloid oligomers, key players in neurodegenerative disorders, exploring their formation, structure, and toxicity.
Area of Science:
- Biochemistry and Molecular Biology
- Neuroscience
- Cell Biology
Background:
- Protein oligomers are ubiquitous in biological systems, exhibiting diverse physiological and pathological functions.
- They are categorized based on function and toxicity, with ongoing research into engineered functional oligomers.
- Antimicrobial peptide oligomers demonstrate roles in bacterial and cancer cell death.
Purpose of the Study:
- To provide a concise overview of current knowledge on amyloid oligomers.
- To highlight their significance as pathogenic species in neurodegenerative disorders.
- To address the challenges in studying their structure, formation, and toxicity.
Main Methods:
- Literature review and synthesis of existing research on amyloid oligomers.
- Analysis of data pertaining to oligomer formation during protein aggregation.
- Examination of studies on the cytotoxic mechanisms and cellular impacts of amyloid oligomers.
Main Results:
- Amyloid oligomers are identified as predominant pathogenic species in neurodegenerative diseases.
- They arise during protein aggregation, acting as intermediates and final products.
- Certain amyloid oligomers exhibit potent cytotoxicity, leading to cellular impairment and disease progression.
Conclusions:
- Understanding amyloid oligomers is crucial for neurodegenerative disease research.
- Their inherent instability and variability present significant research challenges.
- Further investigation into their structure, formation, and toxicity is warranted.
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