Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model system for studying amyloid fibril formation. Here the authors present the 3.4 Å cryo-EM structure of the PI3K-SH3 amyloid fibril, which allows them to rationalize the effects of mutations on the kinetics of fibril for...
Guardado en:
Autores principales: | Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/0f72582fb3cd4c3f93c5943eddda0b9c |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation
por: Thibault Viennet, et al.
Publicado: (2018) -
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
por: Qiuye Li, et al.
Publicado: (2021) -
Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient
por: Paolo Swuec, et al.
Publicado: (2019) -
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
por: Marius Kollmer, et al.
Publicado: (2019) -
Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
por: Falk Liberta, et al.
Publicado: (2019)