Correction to Bexarotene Does Not Clear Amyloid Beta Plaques but Delays Fibril Growth: Molecular Mechanisms
نویسندگان
چکیده
منابع مشابه
Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease.
The deposition of aggregated amyloid beta-protein (Abeta) in the human brain is a major lesion in Alzheimer' disease (AD). The process of Abeta fibril formation is associated with a cascade of neuropathogenic events that induces brain neurodegeneration leading to the cognitive and behavioral decline characteristic of AD. Although a detailed knowledge of Abeta assembly is crucial for the develop...
متن کاملMolecular mechanisms initiating amyloid β-fibril formation in Alzheimer’s disease
decline characteristic of AD. Therefore, a detailed knowledge of Aβ assembly is crucial for the development of new therapeutic approaches designed to prevent fibril formation and/or to dissociate existing fibrils. Yet, our understanding of the molecular mechanisms underlying the initiation of Aβ fibrillogenesis remains very incomplete. Amyloid β-peptide is produced by specific endoproteolytic c...
متن کاملNordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association.
Nordihydroguaiaretic acid (NDGA) was observed by Ono et al. (J Neurochem 87:172-181, 2002) to decrease the fluorescence of thioflavin T associated with freshly extended amyloid beta-protein (Abeta) fibrils. They concluded that NDGA could disaggregate Abeta fibrils into aggregates that were larger than monomers or oligomers and did not bind thioflavin T. Such an effect could be of therapeutic im...
متن کاملCorrection: Early Treatment Critical: Bexarotene Reduces Amyloid-Beta Burden In Silico
[This corrects the article DOI: 10.1371/journal.pone.0153150.].
متن کاملThermodynamics of beta-amyloid fibril formation.
Amyloid fibers are aggregates of proteins. They are built out of a peptide called beta-amyloid (Abeta) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the amyloid precursor protein (APP). X-ray diffraction experiments have shown that these fibrils are rich in beta-structures, whereas the shape of the peptide displays an alp...
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ژورنال
عنوان ژورنال: ACS Chemical Neuroscience
سال: 2017
ISSN: 1948-7193,1948-7193
DOI: 10.1021/acschemneuro.7b00498