Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy-Reference-Cited by-同舟云学术

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

Published:2019-08-21 Issue:1 Volume:10 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Röder Christine^ORCID,Vettore Nicola^ORCID,Mangels Lena N.,Gremer Lothar^ORCID,Ravelli Raimond B. G.^ORCID,Willbold Dieter^ORCID,Hoyer Wolfgang^ORCID,Buell Alexander K.^ORCID,Schröder Gunnar F.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-019-11320-8.pdf

Reference61 articles.

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3. Kayed, R. et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486–489 (2003).

4. Cohen, S. I. A. et al. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. PNAS 110, 9758–9763 (2013).

5. Pepys, M. B. et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362, 553 (1993).

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