Development of a Proteolytically Stable Retro-Inverso Peptide Inhibitor of β-Amyloid Oligomerization as a Potential Novel Treatment for Alzheimer’s Disease-Reference-Cited by-同舟云学术

Development of a Proteolytically Stable Retro-Inverso Peptide Inhibitor of β-Amyloid Oligomerization as a Potential Novel Treatment for Alzheimer’s Disease

Published:2010-03-24 Issue:15 Volume:49 Page:3261-3272
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Taylor Mark¹,Moore Susan¹,Mayes Jennifer¹,Parkin Edward¹,Beeg Marten²,Canovi Mara²,Gobbi Marco²,Mann David M. A.³,Allsop David¹

Affiliation:

1. Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, U.K.

2. Department of Biochemistry and Molecular Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy

3. Clinical Neurosciences Research Group, University of Manchester, Hope Hospital, Salford M6 8HD, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100144m

Reference57 articles.

1. Diffusible, nonfibrillar ligands derived from A 1-42 are potent central nervous system neurotoxins

2. Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus

3. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

4. Selective neuronal degeneration induced by soluble oligomeric amyloid beta‐protein

5. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

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