Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptides
- 15 December 2006
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 353 (2) , 443-449
- https://doi.org/10.1016/j.bbrc.2006.12.043
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid FormationJournal of the American Chemical Society, 2004
- A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activityNature, 2001
- Temperature-dependent β-sheet formation in β-amyloid Aβ1–40 peptide in water: uncoupling β-structure folding from aggregationBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
- Translating cell biology into therapeutic advances in Alzheimer's diseaseNature, 1999
- Temperature dependence of amyloid β-protein fibrillizationProceedings of the National Academy of Sciences, 1998
- MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid ProteinsAnnual Review of Biochemistry, 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
- Selective Inhibition of Aβ Fibril FormationJournal of Biological Chemistry, 1996
- Evidence that Aβ42 is the real culprit in alzheimer's diseaseAnnals of Neurology, 1995
- The molecular pathology of Alzheimer's diseaseNeuron, 1991