Advancements in Understanding and Predicting Transthyretin Amyloidosis ID: 2020-047

This study provides groundbreaking insights into the mechanisms of Transthyretin (TTR) amyloidosis and introduces novel methodologies for its prediction and assessment.

Technology Overview

The document examines the condition of Transthyretin (TTR) amyloidosis, where misfolding of the TTR protein leads to the formation of amyloid deposits, contributing to degenerative diseases. It highlights the role of TTR in plasma, the impact of mutations or aging on TTR stability, and the potential role of glycosylation in amyloidosis initiation. The study presents a model to predict amyloidosis risk and discusses advanced methods for assessing TTR stability and amyloidosis risk, including mass spectrometry and stability assessments.

Key Advantages

• Provides a detailed understanding of the biochemical processes leading to TTR amyloidosis
• Introduces a predictive model for assessing individual risk of amyloidosis
• Highlights novel methodologies for the detection and assessment of TTR monomers in plasma
• Offers potential pathways for the development of therapeutic interventions

Problems Addressed

• Challenges in predicting and diagnosing Transthyretin amyloidosis
• Lack of understanding of the molecular mechanisms behind TTR misfolding and aggregation
• Difficulty in assessing the stability of TTR proteins in plasma

Market Applications

• Clinical diagnostics for early detection of amyloidosis
• Development of targeted therapies for treating TTR amyloidosis
• Research tools for studying protein misfolding diseases

Additional Information

Technology ID: 2020-047
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Date Published: 28 March, 2025