ArticleActa neuropathologica communications2018
Enhancement of therapeutic potential of a naturally occurring human antibody targeting a phosphorylated Ser
Article in Acta neuropathologica communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Plasma Autoantibodies Against Neurodegeneration-Related Antigens in Dementia and Elevated Chi3Li Autoantibodies in Mild Cognitive Impairment.Biomolecules · 2026Article
- Tau is a receptor with low affinity for glucocorticoids and is required for glucocorticoid-induced bone loss.Cell research · 2025Article
- Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.Molecules (Basel, Switzerland) · 2023Review
- Proteinopathies: Deciphering Physiology and Mechanisms to Develop Effective Therapies for Neurodegenerative Diseases.Molecular neurobiology · 2022Review
- Immunotherapies for Neurodegenerative Diseases.Frontiers in neurology · 2021Review
- High-specificity antibodies and detection methods for quantifying phosphorylated tau from clinical samples.Antibody therapeutics · 2021Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Acute inhibition of the CNS-specific kinase TTBK1 significantly lowers tau phosphorylation at several disease relevant sites.PloS one · 2020Article
- Naturally occurring antibodies isolated from PD patients inhibit synuclein seeding in vitro and recognize Lewy pathology.Acta neuropathologica · 2019Article
Corrections and comments
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of tau protein and spreading of tau aggregates are pivotal pathological processes in a range of neurological disorders. Accumulating evidence suggests that immunotherapy targeting tau may be a viable therapeutic strategy. We have previously described the isolation of antibody CBTAU-22.1 from the memory B-cell repertoire of healthy human donors. CBTAU-22.1 was shown to specifically bind a disease-associated phosphorylated epitope in the C-terminus of tau (Ser
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