Stem-Forming Regions That Are Essential for the Amyloidogenesis of Prion Proteins-Reference-Cited by-同舟云学术

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Stem-Forming Regions That Are Essential for the Amyloidogenesis of Prion Proteins

Published:2012-02-16 Issue:8 Volume:51 Page:1566-1576
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Saiki Masatoshi¹²³,Hidaka Yuji¹,Nara Masayuki⁴,Morii Hisayuki²

Affiliation:

1. School of Science and Engineering, Kinki University, Kowakae, Higashi-Osaka, Osaka 577-8502, Japan

2. National Institute of Advanced Industrial Science and Technology (AIST), Central 6, Tsukuba, Ibaraki 305-8566, Japan

3. Faculty of Engineering, Tokyo University of Science, Yamaguchi, Sanyo-Onoda, Yamaguchi 756-0884, Japan

4. Laboratory of Chemistry, Tokyo Medical and Dental University, Ichikawa, Chiba 272-0827, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201688r

Reference40 articles.

1. NMR structure of the mouse prion protein domain PrP(121–231)

2. Prion protein NMR structures of chickens, turtles, and frogs

3. Scrapie prions aggregate to form amyloid-like birefringent rods

4. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein.

5. The most infectious prion protein particles

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1. Design of Peptides for Inhibiting Amyloidogenesis by Blocking Hydrophobic Interactions;2022-10-11

2. Protective Effects of a Neurohypophyseal Hormone Analogue on Prion Aggregation, Cellular Internalization, and Toxicity;ACS Chemical Neuroscience;2019-08-13

3. Replica Exchange Molecular Dynamics Study of Dimerization in Prion Protein: Multiple Modes of Interaction and Stabilization;The Journal of Physical Chemistry B;2016-07-22

4. Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-β region;FEBS Letters;2015-10-20

5. Evaluation of the structural stability of amyloid fibrils by dynamic light scattering;Journal of Biorheology;2015

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