Lynn Radamaker
University of Ulm
6 Papers
3 Citations
Lynn Radamaker is an academic researcher from University of Ulm. The author has contributed to research in topics: Fibril & Amyloid. The author has an hindex of 3, co-authored 6 publications.
Chat about Author
Papers
Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis
Lynn Radamaker,Yin-Hsi Lin,Karthikeyan Annamalai,Stefanie Huhn,Ute Hegenbart,Stefan Schönland,Günter Fritz,Günter Fritz,Matthias Schmidt,Marcus Fändrich +9 more
TL;DR: The structure of a λ1 AL amyloid fibril from an explanted human heart at a resolution of 3.3 Å provides insight into the mechanism of protein misfolding and the role of patient-specific mutations in pathogenicity.
Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
Lynn Radamaker,Julian David Baur,Stefanie Huhn,Christian Haupt,Ute Hegenbart,Stefan Schönland,Akanksha Bansal,Matthias Schmidt,Marcus Fändrich +8 more
TL;DR: In this paper, the authors presented two ex vivo fibril structures of a λ3 LC-derived amyloid fibrils that were extracted from the explanted heart of a patient (FOR005).
Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM
Lynn Radamaker,Sara Karimi-Farsijani,Giada Andreotti,Julian David Baur,Matthias Neumann,Sarah Schreiner,Natalie Berghaus,Raoul Motika,Christian Haupt,Paul Walther,Volker Schmidt,Stefanie Huhn,Ute Hegenbart,Stefan Schönland,Sebastian Wiese,Clarissa Read,Matthias Schmidt,Marcus Fändrich +17 more
TL;DR: In this article, the authors present the structure of an ex vivo λ 1-AL amyloid fibril whose deposits disrupt the ordered cardiomyocyte structure in the heart.
60
Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM.
Urszula Cendrowska,Paulo Jacob Silva,Nadine Ait-Bouziad,Marie Müller,Zekiye Pelin Guven,Sophie Vieweg,Anass Chiki,Lynn Radamaker,Senthil Kumar,Marcus Fändrich,Francesco Tavanti,Maria Cristina Menziani,Alfredo Alexander-Katz,Francesco Stellacci,Hilal A. Lashuel +14 more
TL;DR: NPs that efficiently label amyloid fibrils produced in vitro or isolated from postmortem tissues, under hydrating conditions and in such a way as to unmask their polymorphism and morphological features are described, consistent with the emerging view that the physiologic milieu is a key determinant of amyloids fibril strains.
60
Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
Lynn Radamaker,Julian David Baur,Stefanie Huhn,Christian Haupt,Ute Hegenbart,Stefan Schönland,Akanksha Bansal,Matthias Schmidt,Marcus Fändrich +8 more
TL;DR: The first ex vivo fibril structures of a λ3 LC are presented, which imply that a 180° rotation around the disulfide bond and a major unfolding step are necessary for fibrils to form.