The interactome of soluble amyloid‐β across the Alzheimer's disease continuum
Interactions of Aβ with proteins involved in septins, clathrin-mediated endocytosis, and chaperone functions are diminished in AD, even in asymptomatic individuals. This observation suggests that the impaired physiological protein-binding function of soluble Aβ might represent an early pathogenic event in the development of AD.
Authors
- Klara Gawor (ORCID: https://orcid.org/0000-0001-7571-5420)
- Dietmar Rudolf Thal (ORCID: https://orcid.org/0000-0002-1036-1075)
- Joost Schymkowitz (ORCID: https://orcid.org/0000-0003-2020-0168)
- Sébastien Carpentier (ORCID: https://orcid.org/0000-0002-7389-6405)
- Anne Wiedmer (ORCID: https://orcid.org/0009-0001-4297-962X)
- Markus Otto (ORCID: https://orcid.org/0000-0003-4273-4267)
- Rik Vandenberghe
- Katerina Konstatoulea
- Jolien Schaeverbeke
- Christine A.F. von Arnim
- Xiaohang Li
- Frederic Rousseau
Institutions
- Universität Ulm (DE)
- GZA Ziekenhuizen Campus Sint-Augustinus (BE)
- Southwestern Medical Center (US)
- Universitätsmedizin Göttingen (DE)
- VIB-KU Leuven Center for Brain & Disease Research (BE)
- University Hospital Ulm (DE)
- Martin Luther University Halle-Wittenberg (DE)
- The University of Texas Southwestern Medical Center (US)
- KU Leuven (BE)
Publication Details
- Journal
- Alzheimer s & Dementia
- Published
- 2025-12-01
- DOI
- https://doi.org/10.1002/alz70855_100163
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00