ArticleNature communications2024
Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway.Nature communications · 2026Article
- Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.Current opinion in structural biology · 2026Review
- Structures of dye-bound transthyretin amyloid fibrils from abdominal fat biopsies.Nature communications · 2026Article
- Cryo-EM structures of light chain fibrils from abdominal fat biopsies of multiple myeloma patients.Nature communications · 2026Article
- Cryo-EM of Cardiac AL-224L Amyloid Reveals Shared Structural Motifs and Mutation-induced Differences in λ6 Light Chain Fibrils.Journal of molecular biology · 2026Article
- Biopsy-resolved cryo-EM structures of amyloid fibrils provide molecular insights into AL amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Assessment of the biochemical basis underlying the resistance against systemic amyloidosis.Scientific reports · 2026Article
- Cryo-EM structure of renal AL amyloid fibrils from a patient with λ1 light chain amyloidosis.Nature communications · 2025Article
- Identifying the quantity profiles of amyloid signature proteins in different types of renal amyloidosis.BMC nephrology · 2025Article
- An updated AL-base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2025Article
- Charting the structure-sequence landscape of light chain amyloids.Bioinformatics (Oxford, England) · 2025Article
- Clone-specific residue changes at multiple positions are associated with amyloid formation by antibody light chains.Frontiers in immunology · 2025Article
- Conformational Differences in the Light Chain Constant Domain of Immunoglobulin G and Free Light Chain May Influence Proteolysis in AL Amyloidosis.Journal of molecular biology · 2024Article
- Predicting Structural Consequences of Antibody Light Chain N-Glycosylation in AL Amyloidosis.Pharmaceuticals (Basel, Switzerland) · 2024Article
- An updated AL-Base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
12 authors.
Funding
Abstract
Systemic AL amyloidosis is one of the most frequently diagnosed forms of systemic amyloidosis. It arises from mutational changes in immunoglobulin light chains. To explore whether these mutations may affect the structure of the formed fibrils, we determine and compare the fibril structures from several patients with cardiac AL amyloidosis. All patients are affected by light chains that contain an IGLV3-19 gene segment, and the deposited fibrils differ by the mutations within this common germ line background. Using cryo-electron microscopy, we here find different fibril structures in each patient. These data establish that the mutations of amyloidogenic light chains contribute to defining the fibril architecture and hence the structure of the pathogenic agent.
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