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Bart De Strooper

Researcher at Katholieke Universiteit Leuven

Publications -  433
Citations -  56592

Bart De Strooper is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Amyloid precursor protein & Presenilin. The author has an hindex of 117, co-authored 397 publications receiving 48516 citations. Previous affiliations of Bart De Strooper include Ghent University & Allen Institute for Brain Science.

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miR‐132 loss de‐represses ITPKB and aggravates amyloid and TAU pathology in Alzheimer's brain

TL;DR: It is shown that miR‐132 loss exacerbates both amyloid and TAU pathology via inositol 1,4,5‐trisphosphate 3‐kinase B (ITPKB) upregulation in an AD mouse model, indicating the pathological relevance of this pathway in AD.
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LifeTime and improving European healthcare through cell-based interceptive medicine

Nikolaus Rajewsky, +66 more
- 07 Sep 2020 - 
TL;DR: The LifeTime initiative is an ambitious, multidisciplinary programme that aims to improve healthcare by tracking individual human cells during disease processes and responses to treatment in order to develop and implement cell-based interceptive medicine in Europe over the next decade.
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Amyloidogenic Processing of Human Amyloid Precursor Protein in Hippocampal Neurons Devoid of Cathepsin D

TL;DR: The results rule out cathepsin D as a critical component of α-, β-, or γ-secretase and therefore as a primary target for drugs aimed at decreasing the βA4-amyloid peptide burden in Alzheimer's disease.
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DNA-Dependent Protein Kinase Is Not Required for Efficient Lentivirus Integration

TL;DR: The data suggest a protective role of DNA-PK against cellular toxicity induced by high levels of retrovirus integrase or integration, and suggest poly(ADP-ribose) polymerase (PARP) are not essential for lentivirus integration.
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Dysregulated microRNAs in neurodegenerative disorders.

TL;DR: It is proposed that studying microRNAs and their mRNA targets in the context of neurodegeneration will significantly contribute to the identification of proteins important for neuronal function and might reveal underlying molecular networks that drive these diseases.