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Ansgar B. Siemer
Researcher at University of Southern California
Publications - 37
Citations - 3573
Ansgar B. Siemer is an academic researcher from University of Southern California. The author has contributed to research in topics: Fibril & Amyloid. The author has an hindex of 18, co-authored 34 publications receiving 3131 citations. Previous affiliations of Ansgar B. Siemer include Salk Institute for Biological Studies & ETH Zurich.
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Journal ArticleDOI
The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis
Jixi Li,Thomas McQuade,Ansgar B. Siemer,Johanna Napetschnig,Kenta Moriwaki,Yu-Shan Hsiao,Ermelinda Damko,David Moquin,Thomas Walz,Thomas Walz,Ann E. McDermott,Francis Ka-Ming Chan,Hao Wu +12 more
TL;DR: Insight is provided into the structural changes that occur when RIP kinases are triggered to execute different signaling outcomes and the realm of amyloids is expanded to complex formation and signaling.
Journal ArticleDOI
Amyloid fibrils of the HET-s(218–289) prion form a β-solenoid with a triangular hydrophobic core.
Christian Wasmer,Adam Lange,Hélène Van Melckebeke,Ansgar B. Siemer,Roland Riek,Beat H. Meier +5 more
TL;DR: A structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina is presented.
Journal ArticleDOI
Correlation of structural elements and infectivity of the HET-s prion.
Christiane Ritter,Marie-Lise Maddelein,Ansgar B. Siemer,Thorsten Lührs,Matthias Ernst,Beat H. Meier,Sven J. Saupe,Roland Riek +7 more
TL;DR: It is shown that the structure-based mutagenesis approach shows that this conformation is the functional and infectious entity of the HET-s prion, and correlate distinct structural elements with prion infectivity.
Journal ArticleDOI
The structure of the necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex
Miguel Mompeán,Wenbo Li,Jixi Li,Ségolène Laage,Ansgar B. Siemer,Gunes Bozkurt,Hao Wu,Hao Wu,Ann E. McDermott +8 more
TL;DR: The RIPK1-RIPK3 core is the first detailed structure of a hetero-amyloid and provides a potential explanation for the specificity ofhetero- over-homo-AMyloid formation and a structural basis for understanding the mechanisms of signal transduction.
Journal ArticleDOI
Observation of highly flexible residues in amyloid fibrils of the HET-s prion.
Ansgar B. Siemer,Alexandre A. Arnold,Christiane Ritter,Thomas Westfeld,Matthias Ernst,Roland Riek,Beat H. Meier +6 more
TL;DR: The observation of undetected residues of the prion protein fragment HET-s(218-289) which give rise to well-resolved (13)C, (15)N, and (1)H NMR resonances under high-resolution magic-angle spinning (HRMAS) conditions is reported.