Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline Mutagenesis
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- 1 January 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 335 (3) , 833-842
- https://doi.org/10.1016/j.jmb.2003.11.008
Abstract
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This publication has 53 references indexed in Scilit:
- SCOP: A structural classification of proteins database for the investigation of sequences and structuresPublished by Elsevier ,2006
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Aggregation and neurotoxicity of mutant amyloid β (Aβ) peptides with proline replacement: importance of turn formation at positions 22 and 23Biochemical and Biophysical Research Communications, 2002
- The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formationNature Neuroscience, 2001
- Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloidJournal of Molecular Biology, 2000
- Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packingThe EMBO Journal, 1999
- Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. CohenJournal of Molecular Biology, 1997
- Fibrillogenesis of Alzheimer Aβ peptides studied by fluorescence energy transferJournal of Molecular Biology, 1997
- Physical, Morphological and Functional Differences between pH 5.8 and 7.4 Aggregates of the Alzheimer's Amyloid Peptide A βJournal of Molecular Biology, 1996
- Conformational preferences of amino acids in globular proteinsBiochemistry, 1978