Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis
Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains and is one of the most frequently occurring forms of systemic amyloidosis. Here the authors present the 3.3 Å cryo-EM structure of a λ1 AL amyloid fibril that was isolated from an explanted human heart.
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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
20 March 2019
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| In: |
Nature Communications
Year: 2019, Volume: 10 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-019-09032-0 |
| Online Access: | Verlag, Volltext: https://doi.org/10.1038/s41467-019-09032-0 Verlag, Volltext: https://www.nature.com/articles/s41467-019-09032-0 
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| Author Notes: | Lynn Radamaker, Yin-Hsi Lin, Karthikeyan Annamalai, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Günter Fritz, Matthias Schmidt & Marcus Fändrich |
| Summary: | Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains and is one of the most frequently occurring forms of systemic amyloidosis. Here the authors present the 3.3 Å cryo-EM structure of a λ1 AL amyloid fibril that was isolated from an explanted human heart. |
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| Item Description: | Gesehen am 14.06.2019 |
| Physical Description: | Online Resource |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-019-09032-0 |