A Biotechnological Method Provides Access to Aggregation Competent Monomeric Alzheimer's 1–42 Residue Amyloid Peptide-Reference-Cited by-同舟云学术

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A Biotechnological Method Provides Access to Aggregation Competent Monomeric Alzheimer's 1–42 Residue Amyloid Peptide

Published:1995-09 Issue:9 Volume:13 Page:988-993
ISSN:1087-0156
Container-title:Nature Biotechnology
language:en
Short-container-title:Nat Biotechnol

Author:

Döbeli Heinz,Draeger Nicholas,Huber Gerda,Jakob Peter,Schmidt Dieter,Seilheimer Bernd,Stüber Dietrich,Wipf Beat,Zulauf Martin

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Molecular Medicine,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

http://www.nature.com/articles/nbt0995-988.pdf

Reference17 articles.

1. The molecular pathology of Alzheimer's disease

2. beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.

3. Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging.

4. An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants

5. The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

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1. An expeditious and facile method of amyloid beta (1–42) purification;PLOS ONE;2024-07-11

2. The nickel-chelator dimethylglyoxime inhibits human amyloid beta peptide in vitro aggregation;Scientific Reports;2021-03-23

3. Hydrogen Peroxide Modifies Aβ–Membrane Interactions with Implications for Aβ40 Aggregation;Biochemistry;2019-06-12

4. Amyloidogenicity and Cytotoxicity of a Recombinant C-Terminal His6-Tagged Aβ1–42;ACS Chemical Neuroscience;2018-12-11

5. A facile method for expression and purification of 15 N isotope-labeled human Alzheimer’s β-amyloid peptides from E. coli for NMR-based structural analysis;Protein Expression and Purification;2015-12

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