Revealing Well-Defined Soluble States during Amyloid Fibril Formation by Multilinear Analysis of NMR Diffusion Data-Reference-Cited by-同舟云学术

Revealing Well-Defined Soluble States during Amyloid Fibril Formation by Multilinear Analysis of NMR Diffusion Data

Published:2019-11-08 Issue:47 Volume:141 Page:18649-18652
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Jensen Kristine Steen¹,Linse Sara²^ORCID,Nilsson Mathias³^ORCID,Akke Mikael¹^ORCID,Malmendal Anders²⁴^ORCID

Affiliation:

1. Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden

2. Biochemistry and Structural Biology, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden

3. School of Chemistry, University of Manchester, Oxford Road, Manchester M13 9PL, U.K.

4. Department of Science and Environment, Roskilde University, P.O. Box 260, DK-4000 Roskilde, Denmark

Funder

Engineering and Physical Sciences Research Council

Vetenskapsr?det

Det Frie Forskningsr?d

H2020 European Research Council

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.9b07952

Reference25 articles.

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

2. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

3. Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization

4. Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways

5. Reaction Kinetics Studied Using Diffusion-Ordered Spectroscopy and Multiway Chemometrics

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