Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM
Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains (LCs) but how post-translational modifications (PTMs) of LCs influence amyloid formation is not well understood. Here, the authors present the cryo-EM structure of an AL amyloid fibril derived from the heart tissue of a p...
Guardado en:
Autores principales: | Lynn Radamaker, Sara Karimi-Farsijani, Giada Andreotti, Julian Baur, Matthias Neumann, Sarah Schreiner, Natalie Berghaus, Raoul Motika, Christian Haupt, Paul Walther, Volker Schmidt, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Sebastian Wiese, Clarissa Read, Matthias Schmidt, Marcus Fändrich |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/0c01463d3d2340dc9ac1ed41d176f4a7 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
por: Lynn Radamaker, et al.
Publicado: (2021) -
Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis
por: Lynn Radamaker, et al.
Publicado: (2019) -
Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
por: Matthias Schmidt, 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) -
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
por: Marius Kollmer, et al.
Publicado: (2019)