| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Williams, Robert
University of Bath
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (5/5 displayed)
- 2021The impact of oxidised powder particles on the microstructure and mechanical properties of Ti-6Al-4 V processed by laser powder bed fusioncitations
- 2018Advanced glycation end products modulate amyloidogenic APP processing and Tau phosphorylation: a mechanistic link between glycation and the development of Alzheimer’s diseasecitations
- 2017Increased Foxo3a nuclear translocation and activity is an early neuronal response to βγ-secretase mediated processing of the Amyloid-β-Protein Precursor Protein: Utility of an AβPP-GAL4 reporter assaycitations
- 2016Theory, practice and results of food crop variety evaluation and release in Timor Leste 2001-2015
- 2016Comparative analysis of structure and hardness of cast and direct metal laser sintering produced Co-Cr alloys used for dental devicescitations
Places of action
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article
Advanced glycation end products modulate amyloidogenic APP processing and Tau phosphorylation: a mechanistic link between glycation and the development of Alzheimer’s disease
Abstract
<p>Advanced glycation end products (AGEs) are implicated in the pathology of Alzheimer's disease (AD), as they induce neurodegeneration following interaction with the receptor for AGE (RAGE). This study aimed to establish a mechanistic link between AGE-RAGE signaling and AD pathology. AGE-induced changes in the neuro2a proteome were monitored by SWATH-MS. Western blotting and cell-based reporter assays were used to investigate AGE-RAGE regulated APP processing and tau phosphorylation in primary cortical neurons. Selected protein expression was validated in brain samples affected by AD. The AGE-RAGE axis altered proteome included increased expression of cathepsin B and asparagine endopeptidase (AEP), which mediated an increase in Aβ<sub>1-42</sub> formation and tau phosphorylation, respectively. Elevated cathepsin B, AEP, RAGE, and pTau levels were found in human AD brain, coincident with enhanced AGEs. This study demonstrates that the AGE-RAGE axis regulates Aβ<sub>1-42</sub> formation and tau phosphorylation via increased cathepsin B and AEP, providing a new molecular link between AGEs and AD pathology.</p>