@article{8a9ce23f895d43b4887da1bee499d6eb,
title = "NMR characterization of the interaction of GroEL with amyloid β as a model ligand",
abstract = "Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.",
keywords = "Amyloid β, Chaperonin, GroEL, NMR, NOE",
author = "Maho Yagi-Utsumi and Tomoko Kunihara and Takashi Nakamura and Yoshinori Uekusa and Koki Makabe and Kunihiro Kuwajima and Koichi Kato",
note = "Funding Information: We thank Ms. Hiroko Mizuki ( National Institute of Natural Sciences ), Ms. Kiyomi Senda, and Ms. Kumiko Hattori ( Nagoya City University ) for their help with the preparation of recombinant proteins. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas ( 20107004 , 20107009 ) and for Research Activity Start-up ( 23870043 ) from the Ministry of Education, Culture, Sports, Science and Technology of Japan and Research Funding for Longevity Sciences ( 22-14 ) from the National Center for Geriatrics and Gerontology, Japan . ",
year = "2013",
month = jun,
day = "5",
doi = "10.1016/j.febslet.2013.04.007",
language = "English",
volume = "587",
pages = "1605--1609",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "11",
}