Alzheimer's Disease Drug Candidates Stabilize A-β Protein Native Structure by Interacting with the Hydrophobic Core
- 16 February 2011
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 100 (4), 1076-1082
- https://doi.org/10.1016/j.bpj.2010.12.3741
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- 100 Years and Counting: Prospects for Defeating Alzheimer's DiseaseScience, 2006
- β‐Amyloid Degradation and Alzheimer′s DiseaseBioMed Research International, 2006
- 3D structure of Alzheimer's amyloid-β(1–42) fibrilsProceedings of the National Academy of Sciences, 2005
- Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s diseaseNeuroscience, 2005
- Aβ localization in abnormal endosomes: association with earliest Aβ elevations in AD and Down syndromeNeurobiology of Aging, 2004
- Familial Alzheimer Disease-linked Presenilin 1 Variants Enhance Production of Both Aβ1–40 and Aβ1–42 Peptides That Are Only Partially Sensitive to a Potent Aspartyl Protease Transition State Inhibitor of “γ-Secretase”Published by Elsevier ,2003
- The structural basis of protein folding and its links with human diseasePhilosophical Transactions Of The Royal Society B-Biological Sciences, 2001
- Amyloid fibrillogenesis: themes and variationsCurrent Opinion in Structural Biology, 2000
- Protein misfolding, evolution and diseaseTrends in Biochemical Sciences, 1999
- The Profile of Soluble Amyloid β Protein in Cultured Cell MediaJournal of Biological Chemistry, 1996