Minimalist Protein Model as a Diagnostic Tool for Misfolding and Aggregation
- 13 October 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 363 (1) , 297-308
- https://doi.org/10.1016/j.jmb.2006.07.088
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Amyloid Formation from HypF-N under Conditions in which the Protein is Initially in its Native StateJournal of Molecular Biology, 2005
- In the Footsteps of AlchemistsScience, 2004
- Protein folding and misfoldingNature, 2003
- Myoglobin forms amyloid fibrils by association of unfolded polypeptide segmentsProceedings of the National Academy of Sciences, 2003
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Emerging ideas on the molecular basis of protein and peptide aggregationCurrent Opinion in Structural Biology, 2003
- Unraveling the secrets of Alzheimer's β-amyloid fibrilsProceedings of the National Academy of Sciences, 2003
- Molecular Dynamics Simulation of the SH3 Domain Aggregation Suggests a Generic Amyloidogenesis MechanismJournal of Molecular Biology, 2002
- Mechanisms of cooperativity underlying sequence-independent β-sheet formationThe Journal of Chemical Physics, 2002
- Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assemblyProceedings of the National Academy of Sciences, 2000