Zeitschriftenartikel (31)
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Oligodendrocytes produce amyloid-β and contribute to plaque formation alongside neurons in Alzheimer’s disease model mice. Nature Neuroscience 27, S. 1668 - 1674 (2024)
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APP family member dimeric complexes are formed predominantly in synaptic compartments. Cell & Bioscience 13, 141 (2023)
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Differential effects of familial Alzheimer’s disease-causing mutations on amyloid precursor protein (APP) trafficking, proteolytic conversion, and synaptogenic activity. Acta Neuropathologica Communications 11, 87 (2023)
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The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease. Cells 11 (21), 3421 (2022)
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Brothers in arms: proBDNF/BDNF and sAPPα/Aβ-signaling and their common interplay with ADAM10, TrkB, p75NTR, sortilin, and sorLA in the progression of Alzheimer’s disease. Biological Chemistry 403 (1), S. 43 - 71 (2022)
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The role of mycotoxins in neurodegenerative diseases: current state of the art and future perspectives of research. Biological Chemistry 403 (1), S. 3 - 26 (2022)
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Heterologous production of a cyanobacterial bacteriocin with potent antibacterial activity. Current Research in Biotechnology 3, S. 281 - 287 (2021)
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The Rab5 activator RME-6 is required for amyloid precursor protein endocytosis depending on the YTSI motif. Cellular and Molecular Life Sciences 77, S. 5223 - 5242 (2020)
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Forschungskolleg “NeurodegX”. Neuroforum 26 (3), S. 185 - 186 (2020)
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Copper and zinc ions govern the trans‐directed dimerization of APP family members in multiple ways. Journal of Neurochemistry 151 (5), S. 626 - 641 (2019)
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Trafficking in Alzheimer’s Disease: Modulation of APP Transport and Processing by the Transmembrane Proteins LRP1, SorLA, SorCS1c, Sortilin, and Calsyntenin. Molecular Neurobiology 55, S. 5809 - 5829 (2018)
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Dimerization leads to changes in APP (amyloid precursor protein) trafficking mediated by LRP1 and SorLA. Cellular and Molecular Life Sciences 75, S. 301 - 322 (2018)
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APLP1 Is a Synaptic Cell Adhesion Molecule, Supporting Maintenance of Dendritic Spines and Basal Synaptic Transmission. The Journal of Neuroscience 37 (21), S. 5345 - 5365 (2017)
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Fe65-PTB2 Dimerization Mimics Fe65-APP Interaction. Frontiers in Molecular Neuroscience 10, 140 (2017)
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LRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric State. Frontiers in Molecular Neuroscience 10, 118 (2017)
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Shedding of APP limits its synaptogenic activity and cell adhesion properties. Frontiers in Cellular Neuroscience 8, 410 (2014)
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Amyloid Precursor Protein Dimerization and Synaptogenic Function Depend on Copper Binding to the Growth Factor-Like Domain. The Journal of Neuroscience 34 (33), S. 11159 - 11172 (2014)
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Age-dependent increases in tau phosphorylation in the brains of type 2 diabetic rats correlate with a reduced expression of p62. Experimental Neurology 248, S. 441 - 450 (2013)
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A New Mint1 Isoform, but Not the Conventional Mint1, Interacts with the Small GTPase Rab6. PLoS One 8 (5), S. e64149 (2013)
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Early BDNF Treatment Ameliorates Cell Loss in the Entorhinal Cortex of APP Transgenic Mice. The Journal of Neuroscience 33 (39), S. 15596 - 15602 (2013)
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Amyloid precursor protein (APP) regulates synaptic structure and function. Molecular and Cellular Neuroscience 51 (1-2), S. 43 - 52 (2012)
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Structural aspects and physiological consequences of APP/APLP trans-dimerization. Experimental Brain Research 217, S. 389 - 395 (2012)
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APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms. Cellular and Molecular Life Sciences 69, S. 1353 - 1375 (2012)
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Deletion of the amyloid precursor-like protein 2 (APLP2) does not affect hippocampal neuron morphology or function. Molecular and Cellular Neuroscience 49 (4), S. 448 - 455 (2012)
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Lysine 624 of the Amyloid Precursor Protein (APP) Is a Critical Determinant of Amyloid β Peptide Length. Journal of Biological Chemistry 286 (46), S. 39804 - 39812 (2011)
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Induced Dimerization of the Amyloid Precursor Protein Leads to Decreased Amyloid-β Protein Production. Journal of Biological Chemistry 284 (42), S. 28943 - 28952 (2009)
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PAT1a Modulates Intracellular Transport and Processing of Amyloid Precursor Protein (APP), APLP1, and APLP2. Journal of Biological Chemistry 281 (52), S. 40114 - 40123 (2006)
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Homo- and heterodimerization of APP family members promotes intercellular adhesion. The EMBO Journal 24, S. 3624 - 3634 (2005)
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The Proteolytic Processing of the Amyloid Precursor Protein Gene Family Members APLP-1 and APLP-2 Involves α-, β-, γ-, and ϵ-Like Cleavages. Journal of Biological Chemistry 279 (18), S. 18146 - 18156 (2004)
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γ-Secretase Cleavage and Binding to FE65 Regulate the Nuclear Translocation of the Intracellular C-Terminal Domain (ICD) of the APP Family of Proteins. Biochemistry 42 (22), S. 6664 - 6673 (2003)
31.
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A Novel ε-Cleavage within the Transmembrane Domain of the Alzheimer Amyloid Precursor Protein Demonstrates Homology with Notch Processing. Biochemistry 41 (8), S. 2825 - 2835 (2002)
Preprint (1)
32.
Preprint
Oligodendrocytes and neurons contribute to amyloid-β deposition in Alzheimer’s disease. bioRxiv (2023)