Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides-Reference-Cited by-同舟云学术

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Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides

Published:2013 Issue:1 Volume:4 Page:92-103
ISSN:2042-6496
Container-title:Food Funct.
language:en
Short-container-title:Food Funct.

Author:

Bharadwaj Prashant,Head Richard,Martins Ralph,Raussens Vincent,Sarroukh Rabia,Jegasothy Hema,Waddington Lynne,Bennett Louise

Publisher

Royal Society of Chemistry (RSC)

Subject

General Medicine,Food Science

Link

http://pubs.rsc.org/en/content/articlepdf/2013/FO/C2FO30111C

Reference72 articles.

2. Protective effect of colostrinin on neuroblastoma cell survival is due to reduced aggregation of β-amyloid

3. Aβ aggregation and possible implications in Alzheimer's disease pathogenesis

4. Amyloid-β Aggregation

5. Intracellular amyloid-β in Alzheimer's disease

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1. Luteoloside inhibits Aβ1–42 fibrillogenesis, disintegrates preformed fibrils, and alleviates amyloid-induced cytotoxicity;Biophysical Chemistry;2024-03

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3. Brain Hydrophobic Peptides Antagonists of Neurotoxic Amyloid β Peptide Monomers/Oligomers–Protein Interactions;International Journal of Molecular Sciences;2023-09-08

4. Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ_1–42 aggregation;Inorganic Chemistry Frontiers;2022

5. Effects of Aβ-derived peptide fragments on fibrillogenesis of Aβ;Scientific Reports;2021-09-28

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