Characterization of Aβ aggregation mechanism probed by congo red-Reference-Cited by-同舟云学术

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Characterization of Aβ aggregation mechanism probed by congo red

Published:2012-06 Issue:2 Volume:30 Page:160-169
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Wang Chih-Ching,Huang Hsien-bin,Tsay Huey-Jen,Shiao Ming-Shi,Wu Wen-Jin Winston,Cheng Yi-Chen,Lin Ta-Hsien

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883

Reference36 articles.

1. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

2. A Model for Structure-Dependent Binding of Congo Red to Alzheimer β-Amyloid Fibrils

3. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]

4. Aβ40(L17A/F19A) mutant diminishes the aggregation and neurotoxicity of Aβ40

5. Solution Structure of Amyloid β-Peptide(1−40) in a Water−Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is?,

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4. Shear-induced aggregation of amyloid β (1–40) in a parallel plate geometry;Journal of Biomolecular Structure and Dynamics;2020-07-27

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