Patrick Wunderlich
University of Bonn
10 Papers
79 Citations
Patrick Wunderlich is an academic researcher from University of Bonn. The author has contributed to research in topics: Microglia & Amyloid precursor protein. The author has an hindex of 9, co-authored 10 publications.
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Papers
Sequential Proteolytic Processing of the Triggering Receptor Expressed on Myeloid Cells-2 (TREM2) Protein by Ectodomain Shedding and γ-Secretase-dependent Intramembranous Cleavage
Patrick Wunderlich,Konstantin Glebov,Nadja Kemmerling,Nguyen T. Tien,Harald Neumann,Jochen Walter +5 more
TL;DR: In this article, the C-terminal fragment (CTF) of TREM2 generated by ectodomain shedding is cleaved by γ-secretase, which results in accumulation of CTF at the plasma membrane that also interacts with the signaling adaptor protein DAP12.
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Statins Promote the Degradation of Extracellular Amyloid β-Peptide by Microglia via Stimulation of Exosome-associated Insulin-degrading Enzyme (IDE) Secretion
Irfan Y. Tamboli,Esther Barth,Leonie Christian,Martin Siepmann,Sathish Kumar,Sandesh Singh,Karen Tolksdorf,Michael T. Heneka,Dieter Lütjohann,Patrick Wunderlich,Jochen Walter +10 more
TL;DR: It is shown that statins potently stimulate the degradation of extracellular Aβ by microglia, demonstrating a novel pathway for the nonconventional secretion of IDE via exosomes and suggesting that modulation of this pathway could provide a new strategy to enhance theextracellular clearance of Aβ.
203
Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity.
Sathish Kumar,Oliver Wirths,Kathrin Stüber,Patrick Wunderlich,Philipp Koch,Sandra Theil,Nasrollah Rezaei-Ghaleh,Markus Zweckstetter,Markus Zweckstetter,Markus Zweckstetter,Thomas A. Bayer,Oliver Brüstle,Oliver Brüstle,Dietmar Rudolf Thal,Jochen Walter +14 more
TL;DR: An Aβ variant phosphorylated at Ser26 residue (pSer26Aβ) is identified in transgenic mouse models of AD and in human brain that shows contrasting spatio-temporal distribution as compared to non-phosphorylated Aβ (npAβ), and could represent a critical species in the neurodegeneration during AD pathogenesis.
Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.
Marit Stirnberg,Eva Maurer,Angelika Horstmeyer,Sonja Kolp,Stefan Frank,Tobias Bald,Katharina Arenz,Andreas Janzer,Kai Prager,Patrick Wunderlich,Jochen Walter,Michael Gütschow +11 more
TL;DR: The subcellular localization of the monomeric and multimeric form of matriptase-2 was characterized and it was identified as a defining point in its proteolytic processing, indicating a transactivation and trans-shedding mechanism.
γ-Secretase in microglia – implications for neurodegeneration and neuroinflammation
TL;DR: The involvement of γ‐secretase in the regulation of microglial functions, and the potential relevance of these processes under physiological and pathophysiological conditions are discussed.
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