Inhibition of fibril formation and toxicity of a fragment of α-synuclein by an N-methylated peptide analogue
- 5 March 2004
- journal article
- research article
- Published by Elsevier in Neuroscience Letters
- Vol. 359 (1-2) , 89-93
- https://doi.org/10.1016/j.neulet.2003.12.077
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to TherapeuticsScience, 2002
- Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicityJournal of Molecular Biology, 2002
- Identification of the region of non‐Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicityJournal of Neurochemistry, 2001
- Inhibition of β-Amyloid(40) Fibrillogenesis and Disassembly of β-Amyloid(40) Fibrils by Short β-Amyloid Congeners ContainingN-Methyl Amino Acids at Alternate ResiduesBiochemistry, 2001
- Inhibition of Toxicity in the β-Amyloid Peptide Fragment β-(25–35) Using N-Methylated DerivativesJournal of Biological Chemistry, 2000
- Approaches to discovery and characterization of inhibitors of amyloid β-peptide polymerizationBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2000
- Toxicity of non‐Aβ component of Alzheimer's disease amyloid, and N‐terminal fragments thereof, correlates to formation of β‐sheet structure and fibrilsEuropean Journal of Biochemistry, 2000
- Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's diseaseFEBS Letters, 1998
- The N‐terminal region of non‐Aβ component of Alzheimer's Disease amyloid is responsible for its tendency to assume β‐sheet and aggregate to form fibrilsEuropean Journal of Biochemistry, 1998