ArticleBiochemistry2011
Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Multi-omic phenotyping of MAPT V337M neurons reveals early changes in axonogenesis and tau phosphorylation.NPJ dementia · 2026Article
- Multi-omic phenotyping of iPSC-derived neurons harboring thebioRxiv : the preprint server for biology · 2025Article
- The six brain-specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Review
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Article
- Effect of Trehalose and Ceftriaxone on the Stability of Aggregating-Prone Tau Peptide Containing PHF6* Sequence: An SRCD Study.International journal of molecular sciences · 2022Article
- Fungally Derived Isoquinoline Demonstrates Inducer-Specific Tau Aggregation Inhibition.Biochemistry · 2021Article
- Article
- Glial contributions to neurodegeneration in tauopathies.Molecular neurodegeneration · 2017Review
- Structural evaluations of tau protein conformation: methodologies and approaches.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017Review
- Production of recombinant tau oligomers in vitro.Methods in cell biology · 2017Article
- Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.Molecular biology of the cell · 2016Article
- Analysis of isoform-specific tau aggregates suggests a common toxic mechanism involving similar pathological conformations and axonal transport inhibition.Neurobiology of aging · 2016Article
- Article
- Comparison of the neuropsychological mechanisms of 2,6-diisopropylphenol and N-methyl-D-aspartate receptor antagonist against electroconvulsive therapy-induced learning and memory impairment in depressed rats.Molecular medicine reports · 2015Article
- Azaphilones inhibit tau aggregation and dissolve tau aggregates in vitro.ACS chemical neuroscience · 2015Article
- Stages and conformations of the Tau repeat domain during aggregation and its effect on neuronal toxicity.The Journal of biological chemistry · 2014Article
- OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.Journal of the American Chemical Society · 2014Article
- Brain pathology in myotonic dystrophy: when tauopathy meets spliceopathy and RNAopathy.Frontiers in molecular neuroscience · 2014Review
- Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins.PloS one · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The microtubule-associated protein tau exists as six isoforms created through the splicing of the second, third, and tenth exons. The isoforms are classified by their number of N-terminal exons (0N, 1N, or 2N) and by their number of microtubule-binding repeat regions (3R or 4R). Hyperphosphorylated isoforms accumulate in insoluble aggregates in Alzheimer's disease and other tauopathies. These neurodegenerative diseases can be categorized based on the isoform content of the aggregates they contain. Hyperphosphorylated tau has the general characteristics of an upward electrophoretic shift, decreased microtubule binding, and an association with aggregation. Previously we have shown that a combination of seven pseudophosphorylation mutations at sites phosphorylated by GSK-3β, referred to as 7-Phos, induced several of these characteristics in full-length 2N4R tau and led to the formation of fewer but longer filaments. We sought to determine whether the same phosphorylation pattern could cause differential effects in the other tau isoforms, possibly through varied conformational effects. Using in vitro techniques, we examined the electrophoretic mobility, aggregation properties, and microtubule stabilization of all isoforms and their pseudophosphorylated counterparts. We found that pseudophosphorylation affected each isoform, but in several cases certain isoforms were affected more than others. These results suggest that hyperphosphorylation of tau isoforms could play a major role in determining the isoform composition of tau aggregates in disease.
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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.