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Cellular and Molecular Life Sciences : CMLS|July 15, 2024
DAP12 interacts with RER1 and is retained in the secretory pathway before assembly with TREM2Yanxia Liu, Sandra Theil, Melanie Ibach, et al.
Acta Neuropathologica|March 26, 2013
Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's diseaseSathish Kumar, Oliver Wirths, Sandra Theil, et al.
Autophagy|August 29, 2023
Phosphorylation-state dependent intraneuronal sorting of Aβ differentially impairs autophagy and the endo-lysosomal systemAkshay Kapadia, Sandra Theil, Sabine Opitz, et al.
Glia|December 14, 2020
A reporter cell system for the triggering receptor expressed on myeloid cells 2 reveals differential effects of disease-associated variants on receptor signaling and activation by antibodies against the stalk regionMelanie Ibach, Mona Mathews, Bettina Linnartz-Gerlach, et al.
Scientific Reports|July 2, 2025
Potential role of TNFRSF12A in linking glioblastoma and alzheimer's disease via shared tumour suppressor pathwaysTing Liu, Jingjing Pu, Sandra Theil, et al.
Glia|April 4, 2017
Intramembranous processing by γ-secretase regulates reverse signaling of ephrin-B2 in migration of microgliaNadja Kemmerling, Patrick Wunderlich, Sandra Theil, et al.
Acta Neuropathologica Communications|October 19, 2021
TREM2 modulates differential deposition of modified and non-modified Aβ species in extracellular plaques and intraneuronal depositsPranav Joshi, Florian Riffel, Sathish Kumar, et al.
Cellular and Molecular Life Sciences : CMLS|August 13, 2025
RER1 regulates lipid metabolism in monocytes and macrophagesYanxia Liu, Sandra Theil, Mohamed H Yaghmour, et al.
Acta Neuropathologica|February 23, 2016
Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicitySathish Kumar, Oliver Wirths, Kathrin Stüber, et al.
Glia|August 24, 2021
Differential interaction with TREM2 modulates microglial uptake of modified Aβ speciesPranav Joshi, Florian Riffel, Kanayo Satoh, et al.
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