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Introduction:

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of rare and fatal neurodegenerative disorders that affect both humans and animals. These diseases are characterized by the accumulation of misfolded prion proteins in the brain, leading to progressive neurological dysfunction and ultimately death. Prion diseases have puzzled scientists for decades due to their unique mechanism of propagation and the lack of effective treatments. Understanding the process of protein misfolding and propagation in prion diseases is crucial for developing therapeutic strategies to combat these devastating illnesses.

Table of Contents:

Chapter 1: Introduction
1.1 Introduction
1.2 Background of the study
1.3 Problem Statement
1.4 Objective of the study
1.5 Limitation of the study
1.6 Scope of the study
1.7 Significance of the study
1.8 Structure of the Thesis
1.9 Definition of Terms

Chapter 2: Literature Review
2.1 History of prion diseases
2.2 Prion protein structure and function
2.3 Mechanisms of prion protein misfolding
2.4 Transmission of prion diseases
2.5 Clinical features of prion diseases
2.6 Diagnostic methods for prion diseases
2.7 Current treatments for prion diseases
2.8 Animal models of prion diseases
2.9 Emerging research in prion diseases
2.10 Gaps in the current knowledge of prion diseases

Chapter 3: Research Methodology
3.1 Research design
3.2 Sample selection
3.3 Data collection methods
3.4 Data analysis techniques
3.5 Ethical considerations
3.6 Research limitations
3.7 Research validity and reliability
3.8 Research implications

Chapter 4: Findings
4.1 Analysis of data
4.2 Comparison of findings with existing literature
4.3 Interpretation of results
4.4 Implications of findings
4.5 Recommendations for future research
4.6 Limitations of the study
4.7 Conclusions

Chapter 5: Conclusion and Summary
5.1 Summary of key findings
5.2 Contributions to the field
5.3 Implications for clinical practice
5.4 Recommendations for further research
5.5 Conclusion

Thesis Overview on Prion diseases – protein misfolding and propagation:

Prion diseases, such as Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in animals, are fatal neurodegenerative disorders caused by the misfolding and aggregation of prion proteins. The unique feature of prion diseases is their transmissibility, as misfolded prion proteins can convert normal proteins into their pathological form. This process leads to the accumulation of protein aggregates in the brain, causing progressive neuronal damage and neurological dysfunction.

This thesis aims to provide a comprehensive overview of prion diseases, focusing on the mechanisms of protein misfolding and propagation. The literature review will cover the history of prion diseases, prion protein structure and function, transmission of prion diseases, clinical features, diagnostic methods, current treatments, animal models, and emerging research. By synthesizing the existing knowledge in this field, the thesis will highlight the gaps in understanding prion diseases and propose directions for future research.

The research methodology section will describe the design of the study, sample selection, data collection methods, analysis techniques, ethical considerations, and research limitations. The findings chapter will present the analysis of data, comparison with the literature, interpretation of results, implications, recommendations, and conclusions. Through this structured approach, the thesis aims to contribute to the advancement of knowledge on prion diseases and provide insights for the development of novel therapeutic strategies.

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