Conformational Properties Relevant to the Amyloidogenicity of β2-Microglobulin Analyzed Using Pressure- and Salt-Dependent Chemical Shift Data-Reference-Cited by-同舟云学术

Conformational Properties Relevant to the Amyloidogenicity of β2-Microglobulin Analyzed Using Pressure- and Salt-Dependent Chemical Shift Data

Published:2019-01-03 Issue:4 Volume:123 Page:836-844
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Sakurai Kazumasa¹²^ORCID,Maeno Akihiro³,Lee Young-Ho²⁴,Akasaka Kazuyuki⁵

Affiliation:

1. High Pressure Protein Research Center, Institute of Advanced Technology, Kindai University, 930 Nishimitani, Kinokawa, Wakayama 649-6493, Japan

2. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan

3. Laboratory of Medical Chemistry, Kansai Medical University, 2-5-1 Shin-machi, Hirakata, Osaka 573-1010, Japan

4. Protein Structure Research Group, Division of Bioconvergence Analysis, Korea Basic Science Institute, Cheongju, Chungcheongbuk-do 28119, South Korea

5. Kyoto Prefectural University of Medicine, 465 Kajii-cho, Kamigyo-ku, Kyoto 602-8566, Japan

Funder

Ministry of Education, Culture, Sports, Science and Technology

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b11408

Reference40 articles.

1. Aspects on human amyloid forms and their fibril polypeptides

2. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin

3. Amyloid formation by globular proteins under native conditions

4. Conformational constraints for amyloid fibrillation: the importance of being unfolded

5. Critical Balance of Electrostatic and Hydrophobic Interactions Is Required for β2-Microglobulin Amyloid Fibril Growth and Stability

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