The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers-Reference-Cited by-同舟云学术

The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers

Published:2006-09-01 Issue:9 Volume:39 Page:568-575
ISSN:0001-4842
Container-title:Accounts of Chemical Research
language:en
Short-container-title:Acc. Chem. Res.

Author:

Eisenberg David¹,Nelson Rebecca¹,Sawaya Michael R.¹,Balbirnie Melinda¹,Sambashivan Shilpa¹,Ivanova Magdalena I.¹,Madsen Anders Ø.¹,Riekel Christian¹

Affiliation:

1. Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 KBH, Denmark, and European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France

Publisher

American Chemical Society (ACS)

Subject

General Medicine,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ar0500618

Reference64 articles.

1. New Model for Crystalline Polyglutamine Assemblies and Their Connection with Amyloid Fibrils

2. Structures for amyloid fibrils

3. β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers

4. Structural insights into a yeast prion illuminate nucleation and strain diversity

Cited by 166 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cutaneous Amyloidoses;Rook's Textbook of Dermatology;2024-03-19

2. Prediction of Protein Aggregation Propensity via Data-Driven Approaches;ACS Biomaterials Science & Engineering;2023-10-16

3. The Effect of Ultrasonication on the Fibrillar/ Oligomeric Structures of Aβ1−42 at Different Concentrations;The Protein Journal;2023-08-27

4. Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils;Protein Science;2023-07-24

5. Peptide Self‐Assembly into Amyloid Fibrils at Hard and Soft Interfaces—From Corona Formation to Membrane Activity;Macromolecular Bioscience;2023-03-10