Andreas A. Deeg
Ludwig Maximilian University of Munich
9 Papers
10 Citations
Andreas A. Deeg is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Confocal & Protein aggregation. The author has an hindex of 7, co-authored 9 publications.
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Papers
Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson’s disease
Jens Wagner,Sergey Ryazanov,Sergey Ryazanov,Andrei Leonov,Andrei Leonov,Johannes Levin,Song Shi,Felix Schmidt,Catharina Prix,Francisco J Pan-Montojo,Uwe Bertsch,Gerda Mitteregger-Kretzschmar,Markus Geissen,Martin Eiden,Fabienne Leidel,Thomas Hirschberger,Andreas A. Deeg,Julian J. Krauth,Wolfgang Zinth,Paul Tavan,Jens Pilger,Jens Pilger,Markus Zweckstetter,Markus Zweckstetter,Markus Zweckstetter,Tobias Frank,Mathias Bähr,Jochen H. Weishaupt,Manfred Uhr,Henning Urlaub,Henning Urlaub,Ulrike Teichmann,Matthias Samwer,Kai Bötzel,Martin H. Groschup,Hans A. Kretzschmar,Christian Griesinger,Christian Griesinger,Armin Giese +38 more
TL;DR: The findings suggest that pathological oligomers in neurodegenerative diseases share structural features, although the main protein component is disease-specific, indicating that compounds such as anle138b that modulate oligomer formation by targeting structure-dependent epitopes can have a broad spectrum of activity in the treatment of different protein aggregation diseases.
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Isomerization- and temperature-jump-induced dynamics of a photoswitchable β-hairpin.
Andreas A. Deeg,Michael S. Rampp,Alexander Popp,Bert M. Pilles,Tobias E. Schrader,Tobias E. Schrader,Luis Moroder,Karin Hauser,Wolfgang Zinth +8 more
TL;DR: The combination of the two techniques allows a detailed model for folding and unfolding to be presented, which shows that the peptide dynamics induced by T-jump and isomerization are both determined by the same mechanism and exclude a downhill-folding process.
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Photophysics of diphenyl-pyrazole compounds in solutions and α-synuclein aggregates.
Anne Reiner,Felix Schmidt,Sergey Ryazanov,Andrei Leonov,Daniel Weckbecker,Andreas A. Deeg,Christian Griesinger,Armin Giese,Wolfgang Zinth +8 more
TL;DR: The binding site of the DPP anle138b in protein aggregates is characterized and contribute to the understanding of the therapeutic mode of action of this compound.
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Amyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly
TL;DR: In this paper, the light-driven disassembly process of amyloid-like structures formed by azobenzene model peptides is studied by time-resolved mid-IR spectroscopy from nanoseconds to minutes.
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