A Comparative Study of the Relationship Between Protein Structure and β-Aggregation in Globular and Intrinsically Disordered Proteins
- 1 September 2004
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 342 (1), 345-353
- https://doi.org/10.1016/j.jmb.2004.06.088
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- Protein-misfolding diseases: Getting out of shapeNature, 2002
- Predicting Changes in the Stability of Proteins and Protein Complexes: A Study of More Than 1000 MutationsJournal of Molecular Biology, 2002
- Natively unfolded proteins: A point where biology waits for physicsProtein Science, 2002
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002
- The structural basis of protein folding and its links with human diseasePhilosophical Transactions Of The Royal Society B-Biological Sciences, 2001
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Conformational Analysis of Peptides Corresponding to β-Hairpins and a β-Sheet that Represent the Entire Sequence of the α-Spectrin SH3 DomainJournal of Molecular Biology, 1996
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural PeptidesJournal of Molecular Biology, 1995