Amyloid fibril formationin vitrofrom halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations-Reference-Cited by-同舟云学术

Amyloid fibril formationin vitrofrom halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations

Published:2013-09-30 Issue:11 Volume:22 Page:1582-1591
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Tokunaga Yuhei¹,Matsumoto Mitsuharu²,Tokunaga Masao³,Arakawa Tsutomu⁴,Sugimoto Yasushi¹

Affiliation:

1. Laboratory of Biochemstry and Bioscience, The United Graduate School of Agricultural Sciences, Kagoshima University; Korimoto Kagoshima 890-0065 Japan

2. Joint Faculty of Veterinary Medicine; Kagoshima University; Korimoto Kagoshima 890-0065 Japan

3. Faculty of Agriculture; Kagoshima University; Korimoto Kagoshima 890-0065 Japan

4. Alliance Protein Laboratories; 6042 Cornerstone Court West, Suite A San Diego California 92121

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2359/fullpdf

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4. Designing conditions for in vitro formation of amyloid protofilaments and fibrils;Chiti;Proc Natl Acad Sci USA,1999

5. Mutational analysis of the propensity for amyloid formation by a globular protein;Chiti;Embo J,2000

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