The three-dimensional structure of human β-endorphin amyloid fibrils-Reference-Cited by-同舟云学术

The three-dimensional structure of human β-endorphin amyloid fibrils

Published:2020-10-12 Issue:12 Volume:27 Page:1178-1184
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Seuring Carolin^ORCID,Verasdonck Joeri,Gath Julia,Ghosh Dhimam,Nespovitaya Nadezhda,Wälti Marielle Aulikki,Maji Samir K.^ORCID,Cadalbert Riccardo,Güntert Peter,Meier Beat H.^ORCID,Riek Roland^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

https://www.nature.com/articles/s41594-020-00515-z.pdf

Reference48 articles.

1. Chapman, M. R. et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851–855 (2002).

2. Fowler, D. M. et al. Functional amyloid formation within mammalian tissue. PLoS Biol. 4, e6 (2006).

3. Gebbink, M. F. B. G., Claessen, D., Bouma, B., Dijkhuizen, L. & Wösten, H. A. B. Amyloids—a functional coat for microorganisms. Nat. Rev. Microbiol. 3, 333–341 (2005).

4. Maddelein, M. L., Dos Reis, S., Duvezin-Caubet, S., Coulary-Salin, B. & Saupe, S. J. Amyloid aggregates of the HET-s prion protein are infectious. Proc. Natl Acad. Sci. USA 99, 7402–7407 (2002).

5. Maji, S. K., Wang, L., Greenwald, J. & Riek, R. Structure-activity relationship of amyloid fibrils. FEBS Lett. 583, 2610–2617 (2009).

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