How Important is the Role of Compact Denatured States on Amyloid Formation by Transthyretin?
Author:
Publisher
CRC Press
Link
http://www.crcnetbase.com/doi/pdf/10.1201/9781420037494.ch110
Reference7 articles.
1. Amyloid Formation by Transthyretin: From Protein Stability to Protein Aggregation
2. Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants
3. The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution
4. Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants
5. The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30–>Met variant to 1.7-A resolution.
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1. Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: Insights from molecular dynamics simulations;Protein Science;2010-02
2. Spatial Clustering of Molecular Dynamics Trajectories in Protein Unfolding Simulations;Computational Intelligence Methods for Bioinformatics and Biostatistics;2009
3. Towards Data Warehousing and Mining of Protein Unfolding Simulation Data;Journal of Clinical Monitoring and Computing;2005-10
4. Detection of Hydrophobic Clusters in Molecular Dynamics Protein Unfolding Simulations Using Association Rules;Biological and Medical Data Analysis;2005
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