Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM

  title={Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM},
  author={Lynn Radamaker and Sara Karimi-Farsijani and Giada Andreotti and Julian Baur and Matthias Neumann and Sarah Schreiner and Natalie Berghaus and Raoul Motika and Christian Haupt and Paul Walther and Volker Schmidt and Stefanie Huhn and Ute Hegenbart and Stefan O. Sch{\"o}nland and Sebastian Wiese and Clarissa Read and Matthias Schmidt and Marcus F{\"a}ndrich},
  journal={Nature Communications},
Systemic AL amyloidosis is a rare disease that is caused by the misfolding of immunoglobulin light chains (LCs). Potential drivers of amyloid formation in this disease are post-translational modifications (PTMs) and the mutational changes that are inserted into the LCs by somatic hypermutation. Here we present the cryo electron microscopy (cryo-EM) structure of an ex vivo λ1-AL amyloid fibril whose deposits disrupt the ordered cardiomyocyte structure in the heart. The fibril protein contains… 

Identification of AL proteins from 10 λ-AL amyloidosis patients by mass spectrometry extracted from abdominal fat and heart tissue.

  • Julian BaurNatalie Berghaus Christian Haupt
  • Biology
    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
  • 2022
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