ArticleAngewandte Chemie (International ed. in English)2019
Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- Modifications of Lysine Residues 294 and 311 Within the Microtubule-Binding Region Alter Tau Aggregation and Tubulin Binding Equilibria.Angewandte Chemie (International ed. in English) · 2026Article
- Site-specific phosphorylation of Ser352 drives aggregation of Tau R4 under acidosis conditions.Chemical science · 2026Article
- Reversal of protein chemical aging by enzymatic deglycation.Nature communications · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Convergent Assembly of Homo- and Heterotypic Ubiquitin Chains from Functionalized, Expressed Monomers via Thiol-Ene Chemistry.Angewandte Chemie (International ed. in English) · 2025Article
- Chemical Synthesis Reveals Pathogenic Role ofJournal of the American Chemical Society · 2025Article
- Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases.RSC chemical biology · 2025Review
- Post-Translational Modifications Control Phase Transitions of Tau.ACS central science · 2024Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Post-Translational Modifications Control Phase Transitions of Tau.bioRxiv : the preprint server for biology · 2024Article
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Chemical Synthesis of Microtubule-Associated Protein Tau.Journal of the American Chemical Society · 2023Article
- Total synthesis of interleukin-2Chemical science · 2023Article
- Chemical tools for study and modulation of biomolecular phase transitions.Chemical science · 2022Review
- Consequences of post-translational modifications on amyloid proteins as revealed by protein semisynthesis.Current opinion in chemical biology · 2021Review
- Methylation as a key regulator of Tau aggregation and neuronal health in Alzheimer's disease.Cell communication and signaling : CCS · 2021Review
- Semisynthetic Modification of Tau Protein with Di-Ubiquitin Chains for Aggregation Studies.International journal of molecular sciences · 2020Article
- Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau.The Journal of biological chemistry · 2020Article
- Chemical modification of proteins by insertion of synthetic peptides using tandem protein trans-splicing.Nature communications · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
A variety of methods have been employed to study the impact of posttranslational modifications on Tau protein function. Here, a semisynthesis strategy is described that enables selective modification within the central repeat domain of Tau4 (residues 291-321), comprising a major interaction motive with tubulin as well as one of the key hexapeptides involved in Tau aggregation. This strategy has led to the preparation of four semisynthetic Tau variants with phosphoserine residues in different positions and one with a so far largely ignored carboxymethyllysine modification that results from a non-enzymatic posttranslational modification (nPTM). The latter modification inhibits tubulin polymerization but exhibits an aggregation behavior very similar to unmodified Tau. In contrast, phosphorylated Tau variants exhibit similar binding to tubulin as unmodified Tau4 but show lower tendencies to aggregate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.