Heating during agitation of β

amyloid biophysics circular dichroism (CD) fluorescence heat denaturation phase transition protein aggregation protein folding protein stability solubility supersaturation

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
25 10 2019
Historique:
received: 27 06 2019
revised: 19 08 2019
pubmed: 10 9 2019
medline: 3 6 2020
entrez: 10 9 2019
Statut: ppublish

Résumé

Amyloidosis-associated amyloid fibrils are formed by denatured proteins when supersaturation of denatured proteins is broken. β

Identifiants

pubmed: 31495783
pii: S0021-9258(20)30342-2
doi: 10.1074/jbc.RA119.009971
pmc: PMC6816083
doi:

Substances chimiques

Amyloid 0
beta 2-Microglobulin 0
Sodium Chloride 451W47IQ8X

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

15826-15835

Informations de copyright

© 2019 Noji et al.

Références

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Auteurs

Masahiro Noji (M)

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

Kenji Sasahara (K)

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

Keiichi Yamaguchi (K)

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

Masatomo So (M)

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

Kazumasa Sakurai (K)

Institute of Advanced Technology, Kindai University, Wakayama 649-6493, Japan.

József Kardos (J)

ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. Sétány 1/C, Budapest, 1117, Hungary.

Hironobu Naiki (H)

Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan.

Yuji Goto (Y)

Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan gtyj8126@protein.osaka-u.ac.jp.

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Classifications MeSH