An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations-Reference-Cited by-同舟云学术

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An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations

Published:2016-03-21 Issue:8 Volume:17 Page:657-676
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Nagel-Steger Luitgard¹²,Owen Michael C.¹,Strodel Birgit¹³^ORCID

Affiliation:

1. Institute of Complex Systems: Structural Biochemistry (ICS-6); Forschungszentrum Jülich; 52425 Jülich Germany

2. Institut für Physikalische Biologie; Heinrich-Heine-Universität Düsseldorf; Universitätstrasse 1 40225 Düsseldorf Germany

3. Institute of Theoretical and Computational Chemistry; Heinrich Heine University Düsseldorf; Universitätstrasse 1 40225 Düsseldorf Germany

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference225 articles.

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

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

4. Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction

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3. Perspective for Molecular Dynamics Simulation Studies of Amyloid-β Aggregates;The Journal of Physical Chemistry B;2023-12-18

4. Current strategies of detecting Aβ species and inhibiting Aβ aggregation: Status and prospects;Coordination Chemistry Reviews;2023-11

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