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Updated: Feb 25, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
A review on protein misfolding, aggregation and strategies to prevent related ailments
Tooba Naz Shamsi1, Teeba Athar1, Romana Parveen1
1Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Abstract:
This review aims to highlight the fundamental mechanism of protein misfolding leading to protein aggregation and associated diseases. It also aims to anticipate novel therapeutic strategies with which to prevent or treat these highly debilitating conditions linked to these pathologies. The failure of a protein to correctly fold de novo or to remain correctly folded can have profound consequences on a living system especially when the cellular quality control processes fail to eliminate the rogue proteins. The core cause of over 20 different human diseases which have now been designated as 'conformational diseases' including neurodegenerative diseases such as Alzheimer's disease (AD), Huntington's disease (HD) and Parkinson's disease (PD) etc. A comprehensive study on protein misfolding, aggregation, and the outcomes of the effects of cytotoxic aggregates will lead to understand the aggregation-mediated cell toxicity and serves as a foundation for future research in development of promising therapies and drugs. This review has also shed light on the mechanism of protein misfolding which leads to its aggregation and hence the neurodegeneration. From these considerations, one could also envisage the possibility that protein aggregation may be exploited by nature to perform specific physiological functions in differing biological contexts.
Insights
Protein misfolding causes aggregation and diseases like Alzheimer's. Understanding this mechanism may lead to new therapies for these debilitating conformational diseases.
Area of Science:
- Molecular Biology
- Neuroscience
- Pathology
Background:
- Protein misfolding and aggregation are implicated in over 20 human diseases, termed 'conformational diseases'.
- Cellular quality control failures exacerbate the accumulation of misfolded proteins.
- Neurodegenerative diseases such as Alzheimer's, Huntington's, and Parkinson's are linked to protein aggregation.
Purpose of the Study:
- To elucidate the fundamental mechanisms of protein misfolding and aggregation.
- To explore novel therapeutic strategies for conformational diseases.
- To understand aggregation-mediated cellular toxicity and its role in neurodegeneration.
Main Methods:
- This review synthesizes current research on protein misfolding and aggregation mechanisms.
- It analyzes the consequences of cytotoxic protein aggregates on cellular function.
- The review discusses potential therapeutic interventions and drug development.
Main Results:
- Protein misfolding is a key driver of aggregation, leading to cellular dysfunction and disease.
- Understanding these processes is crucial for developing effective treatments.
- Protein aggregation might have physiological roles in specific biological contexts.
Conclusions:
- Targeting protein misfolding and aggregation pathways offers promising therapeutic avenues.
- Further research into aggregation-mediated toxicity can inform drug discovery.
- The study of conformational diseases is vital for advancing neurodegenerative disease research.
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