Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation-Reference-Cited by-同舟云学术

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Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation

Published:2013-07-02 Issue:28 Volume:135 Page:10202-10205
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Apostol Marcin I.¹,Perry Kay²,Surewicz Witold K.¹

Affiliation:

1. Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106, United States

2. NE-CAT, Department of Chemistry and Chemical Biology, Cornell University, Argonne National Laboratory, Argonne, Illinois 60439, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja403001q

Reference29 articles.

1. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

2. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases

3. The most infectious prion protein particles

4. Structure of the cross-β spine of amyloid-like fibrils

5. Atomic structures of amyloid cross-β spines reveal varied steric zippers

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3. Probing differences among Aβ oligomers with two triangular trimers derived from Aβ;Proceedings of the National Academy of Sciences;2023-05-22

4. Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils;Frontiers in Molecular Biosciences;2023-02-09

5. The interactions of amyloid β aggregates with phospholipid membranes and the implications for neurodegeneration;Biochemical Society Transactions;2023-01-11

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