Breakdown of supersaturation barrier links protein folding to amyloid formation
Noji et al. test link between protein folding and misfolding upon heating and agitation. They show that folding and amyloid formation are separated by the supersaturation barrier of a protein, breakdown of which shifts the protein to the amyloid pathway. This study is useful to the field of protein...
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Nature Portfolio
2021
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oai:doaj.org-article:ed4d8eeda119466189e820b1da4455272021-12-02T14:16:33ZBreakdown of supersaturation barrier links protein folding to amyloid formation10.1038/s42003-020-01641-62399-3642https://doaj.org/article/ed4d8eeda119466189e820b1da4455272021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01641-6https://doaj.org/toc/2399-3642Noji et al. test link between protein folding and misfolding upon heating and agitation. They show that folding and amyloid formation are separated by the supersaturation barrier of a protein, breakdown of which shifts the protein to the amyloid pathway. This study is useful to the field of protein folding versus self-assembly and amyloidogenesis.Masahiro NojiTatsushi SamejimaKeiichi YamaguchiMasatomo SoKeisuke YuzuEri ChataniYoko Akazawa-OgawaYoshihisa HagiharaYasushi KawataKensuke IkenakaHideki MochizukiJózsef KardosDaniel E. OtzenVittorio BellottiJohannes BuchnerYuji GotoNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-10 (2021) |
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DOAJ |
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DOAJ |
language |
EN |
topic |
Biology (General) QH301-705.5 |
spellingShingle |
Biology (General) QH301-705.5 Masahiro Noji Tatsushi Samejima Keiichi Yamaguchi Masatomo So Keisuke Yuzu Eri Chatani Yoko Akazawa-Ogawa Yoshihisa Hagihara Yasushi Kawata Kensuke Ikenaka Hideki Mochizuki József Kardos Daniel E. Otzen Vittorio Bellotti Johannes Buchner Yuji Goto Breakdown of supersaturation barrier links protein folding to amyloid formation |
description |
Noji et al. test link between protein folding and misfolding upon heating and agitation. They show that folding and amyloid formation are separated by the supersaturation barrier of a protein, breakdown of which shifts the protein to the amyloid pathway. This study is useful to the field of protein folding versus self-assembly and amyloidogenesis. |
format |
article |
author |
Masahiro Noji Tatsushi Samejima Keiichi Yamaguchi Masatomo So Keisuke Yuzu Eri Chatani Yoko Akazawa-Ogawa Yoshihisa Hagihara Yasushi Kawata Kensuke Ikenaka Hideki Mochizuki József Kardos Daniel E. Otzen Vittorio Bellotti Johannes Buchner Yuji Goto |
author_facet |
Masahiro Noji Tatsushi Samejima Keiichi Yamaguchi Masatomo So Keisuke Yuzu Eri Chatani Yoko Akazawa-Ogawa Yoshihisa Hagihara Yasushi Kawata Kensuke Ikenaka Hideki Mochizuki József Kardos Daniel E. Otzen Vittorio Bellotti Johannes Buchner Yuji Goto |
author_sort |
Masahiro Noji |
title |
Breakdown of supersaturation barrier links protein folding to amyloid formation |
title_short |
Breakdown of supersaturation barrier links protein folding to amyloid formation |
title_full |
Breakdown of supersaturation barrier links protein folding to amyloid formation |
title_fullStr |
Breakdown of supersaturation barrier links protein folding to amyloid formation |
title_full_unstemmed |
Breakdown of supersaturation barrier links protein folding to amyloid formation |
title_sort |
breakdown of supersaturation barrier links protein folding to amyloid formation |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/ed4d8eeda119466189e820b1da445527 |
work_keys_str_mv |
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1718391699953156096 |