ArticleThe Journal of biological chemistry2015
Tau monoclonal antibody generation based on humanized yeast models: impact on Tau oligomerization and diagnostics.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease.bioRxiv : the preprint server for biology · 2026Article
- Conformation-specific monoclonal antibodies reveal early Tau structural intermediates in Alzheimer's disease.The Journal of biological chemistry · 2026Article
- Early Alzheimer's Disease with frequent neuritic plaques harbors neocortical tau seeds distinct from primary age-related tauopathy.Nature communications · 2025Article
- Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023Review
- Non-Rodent Genetic Animal Models for Studying Tauopathy: Review ofInternational journal of molecular sciences · 2021Review
- Dangerous Liaisons: Tau Interaction with Muscarinic Receptors.Current Alzheimer research · 2020Review
- A Novel Tau Antibody Detecting the First Amino-Terminal Insert Reveals Conformational Differences Among Tau Isoforms.Frontiers in molecular biosciences · 2020Article
- The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?Acta neuropathologica communications · 2019Review
- Different tau species lead to heterogeneous tau pathology propagation and misfolding.Acta neuropathologica communications · 2018Article
- Directed evolution of a picomolar-affinity, high-specificity antibody targeting phosphorylated tau.The Journal of biological chemistry · 2018Article
- Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018Review
- NMR Meets Tau: Insights into Its Function and Pathology.Biomolecules · 2016Review
- Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells.Microbial cell (Graz, Austria) · 2016Review
- Tau in physiology and pathology.Nature reviews. Neuroscience · 2016Review
- Development of a pan-tau multivalent nanobody that binds tau aggregation motifs and recognizes pathological tau aggregates.Biotechnology progressArticle
Corrections and comments
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Authors and funding
19 authors at 8 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A link between Tau phosphorylation and aggregation has been shown in different models for Alzheimer disease, including yeast. We used human Tau purified from yeast models to generate new monoclonal antibodies, of which three were further characterized. The first antibody, ADx201, binds the Tau proline-rich region independently of the phosphorylation status, whereas the second, ADx215, detects an epitope formed by the Tau N terminus when Tau is not phosphorylated at Tyr(18). For the third antibody, ADx210, the binding site could not be determined because its epitope is probably conformational. All three antibodies stained tangle-like structures in different brain sections of THY-Tau22 transgenic mice and Alzheimer patients, and ADx201 and ADx210 also detected neuritic plaques in the cortex of the patient brains. In hippocampal homogenates from THY-Tau22 mice and cortex homogenates obtained from Alzheimer patients, ADx215 consistently stained specific low order Tau oligomers in diseased brain, which in size correspond to Tau dimers. ADx201 and ADx210 additionally reacted to higher order Tau oligomers and presumed prefibrillar structures in the patient samples. Our data further suggest that formation of the low order Tau oligomers marks an early disease stage that is initiated by Tau phosphorylation at N-terminal sites. Formation of higher order oligomers appears to require additional phosphorylation in the C terminus of Tau. When used to assess Tau levels in human cerebrospinal fluid, the antibodies permitted us to discriminate patients with Alzheimer disease or other dementia like vascular dementia, indicative that these antibodies hold promising diagnostic potential.
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