Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lynn Radamaker"'
Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM
Autor:
Lynn Radamaker, Sara Karimi-Farsijani, Giada Andreotti, Julian Baur, Matthias Neumann, Sarah Schreiner, Natalie Berghaus, Raoul Motika, Christian Haupt, Paul Walther, Volker Schmidt, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Sebastian Wiese, Clarissa Read, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains (LCs) but how post-translational modifications (PTMs) of LCs influence amyloid formation is not well understood. Here, the authors present the cryo-EM structure of an AL a
Externí odkaz:
https://doaj.org/article/0c01463d3d2340dc9ac1ed41d176f4a7
Autor:
Lynn Radamaker, Julian Baur, Stefanie Huhn, Christian Haupt, Ute Hegenbart, Stefan Schönland, Akanksha Bansal, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Systemic AL amyloidosis is a protein misfolding disease caused by the aggregation and fibrillation of immunoglobulin light chains (LCs). Here, the authors present the cryo-EM structures of λ3 LC-derived amyloid fibrils that were isolated from patien
Externí odkaz:
https://doaj.org/article/54c83fc80d47468e9d109fced8a9dd0f
Autor:
Lynn Radamaker, Yin-Hsi Lin, Karthikeyan Annamalai, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Günter Fritz, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
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 isolat
Externí odkaz:
https://doaj.org/article/b4de0969a221446794222489fd2110f9
Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM
Autor:
Sara Karimi-Farsijani, Stefanie Huhn, Marcus Fändrich, Lynn Radamaker, Julian David Baur, Giada Andreotti, Paul Walther, Matthias Neumann, Sarah Schreiner, Volker Schmidt, Clarissa Read, Matthias Schmidt, Ute Hegenbart, Christian Haupt, Stefan Schönland, Raoul Motika, Sebastian Wiese, Natalie Berghaus
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
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 in
Autor:
Stefan Schönland, Karthikeyan Annamalai, Yin-Hsi Lin, Lynn Radamaker, Matthias Schmidt, Stefanie Huhn, Günter Fritz, Marcus Fändrich, Ute Hegenbart
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Nature Communications
Nature Communications
Amyloid fibrils derived from antibody light chains are key pathogenic agents in systemic AL amyloidosis. They can be deposited in multiple organs but cardiac amyloid is the major risk factor of mortality. Here we report the structure of a λ1 AL amyl
Autor:
Stefan Schönland, Matthias Schmidt, Akanksha Bansal, Ute Hegenbart, Marcus Fändrich, Christian Haupt, Julian David Baur, Lynn Radamaker, Stefanie Huhn
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Systemic AL amyloidosis is a debilitating and potentially fatal disease that arises from the misfolding and fibrillation of immunoglobulin light chains (LCs). The disease is patient-specific with essentially each patient possessing a unique LC sequen
Autor:
Marie Müller, Francesco Tavanti, Nadine Ait-Bouziad, Paulo Jacob Silva, Sophie Vieweg, Francesco Stellacci, Maria Cristina Menziani, Zekiye Pelin Guven, Urszula Cendrowska, Marcus Fändrich, Senthil Kumar, Hilal A. Lashuel, Alfredo Alexander-Katz, Anass Chiki, Lynn Radamaker
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The ability of proteins to self-assemble into different types of fibrils with distinct morphologies has been linked to the pathological and clinical heterogeneity of amyloid diseases such as Alzheimer’s disease and Parkinson’s diseas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98ad4ae917aa1d2654c89bafd9fea266
https://doi.org/10.1101/754846
https://doi.org/10.1101/754846