Dataset Information
Unaligned cryo-EM micrographs of AL55 amyloid fibrils extracted from the kidney of an AL amyloidosis patient
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ABSTRACT:
SUBMITTER: Antonio Chaves-Sanjuan
PROVIDER: EMPIAR-11446 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
The Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis.
Journal of molecular biology 20230727 18
Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each patient yield distinct amyloid structures. However different tissue microenvironments may also cause identical protein precursors to adopt distinct amyloid structures. To address the impact of the tissue environment on the structural polymorphism of amyloids, we extracted fibrils from the kidney of a ...[more]