ArticleBiochemistry2012
FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 76 citations in OpenAlex.
- Proteoform medicine: characterizing and targeting protein forms in human disease.Nature reviews. Genetics · 2026Review
- Lysosome trafficking across intracellular and intercellular networks in the brain.Frontiers in molecular neuroscience · 2026Article
- 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
- Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration.Nature communications · 2025Article
- Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- The Role of Liquid-Liquid Phase Separation in the Accumulation of Pathological Proteins: New Perspectives on the Mechanism of Neurodegenerative Diseases.Aging and disease · 2024Review
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Physiology and pharmacological targeting of phase separation.Journal of biomedical science · 2024Review
- Brain clearance of protein aggregates: a close-up on astrocytes.Molecular neurodegeneration · 2024Review
- Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation.ACS chemical neuroscience · 2023Article
- Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Tau Lysine Pseudomethylation Regulates Microtubule Binding and Enhances Prion-like Tau Aggregation.International journal of molecular sciences · 2023Article
- A Validated Method to Prepare Stable Tau Oligomers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer's Disease and Related Dementias.Cells · 2022Review
- FTD-associated mutations in Tau result in a combination of dominant and recessive phenotypes.Neurobiology of disease · 2022Article
- Tau liquid-liquid phase separation in neurodegenerative diseases.Trends in cell biology · 2022Review
- Molecular mechanisms of amyloid formation in living systems.Chemical science · 2022Review
- Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation.Neuropathology and applied neurobiology · 2022Article
- Age-dependent accumulation of tau aggregation inFrontiers in aging · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
FTDP-17 mutations in the tau gene lead to early onset frontotemporal dementias characterized by the pathological aggregation of the microtubule-associated protein tau. Tau aggregation is closely correlated with the progression and severity of localized atrophy of certain regions in the brain. These mutations are primarily located in or near the microtubule-binding repeat regions of tau and can have vastly different effects on the protein. Some mutations have been linked to effects such as increased levels of aggregation, hyperphosphorylation, defects in mRNA splicing, and weakened interaction with microtubules. Given the differential effects of the mutations, it may not be surprising that the pathology associated with FTDP-17 can vary widely as well. Despite this variety, several of the mutations are commonly used interchangeably as aggregation inducers for in vitro and in vivo models of tauopathies. We generated recombinant forms of 12 FTDP-17 mutations chosen for their predicted effects on the charge, hydrophobicity, and secondary structure of the protein. We then examined the effects that the mutations had on the properties of in vitro aggregation of the protein and its ability to stabilize microtubule assembly. The group of mutations induced very different effects on the total amount of aggregation, the kinetics of aggregation, and filament morphology. Several of the mutations inhibited the microtubule stabilization ability of tau, while others had very little effect compared to wild-type tau. These results indicate that the mechanisms of disease progression may differ among FTDP-17 mutations and that the effects of the varying mutations may not be equal in all model systems.
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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.