PHF6 Antibody
- Known as:
- PHF6 Antibody
- Catalog number:
- 35894
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- PHF6 Antibody
Ask about this productRelated genes to: PHF6 Antibody
- Gene:
- PHF6 NIH gene
- Name:
- PHD finger protein 6
- Previous symbol:
- BFLS, BORJ
- Synonyms:
- KIAA1823, MGC14797, CENP-31
- Chromosome:
- Xq26.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-28
- Date modifiied:
- 2019-04-23
Related products to: PHF6 Antibody
Related articles to: PHF6 Antibody
- Pathogenic microtubule-associated protein tau (MAPT) mutations play an important role in tauopathies by altering tau assembly and early aggregation. The V337M mutation, located within the aggregation-prone PHF6** motif of tau, is known to accelerate tau assembly, while its molecular mechanism is unclear. Here, we employ multiscale molecular dynamics simulations, combining replica-exchange, conventional and coarse-grained approaches, to elucidate how the V337M mutation reshapes the conformational ensemble and aggregation behavior of PHF6** peptides. Replica-exchange molecular dynamics simulations demonstrate that the V337M mutation enhances the β-structure and shifts PHF6** oligomers toward more compact aggregates. Interaction analyses show that the V337M mutation facilitates the formation of hydrogen bonds and salt-bridges and strengthens the residue-residue association, with the most pronounced enhancements involving residue 337 and its neighboring residues. Conventional molecular dynamics simulations reveal that the V337M mutation promotes persistent oligomerization and stabilizes β-sheet assemblies in larger PHF6** systems. Coarse-grained simulations establish that β-structure formation is a prerequisite for PHF6** oligomerization and the V337M mutation stabilizes interpeptide association, leading to earlier oligomer formation and more extensively interconnected oligomers. This study provides mechanistic insights into mutation-enhanced tau oligomerization, which may be helpful for an in-depth understanding of the pathogenesis of mutation-linked tauopathies. - Source: PubMed
Publication date: 2026/05/29
Xia PengxuanChen YujieTang JiaxingGuan LuluFeng DushuoZou Yu - Tauopathies are neurodegenerative diseases all characterized by tau lesions in the brain. Nevertheless, a clinical and pathophysiological heterogeneity is present among them. This includes the dominant tau isoform found within aggregates (3R and/or 4R tau) along with different brain regions being affected. For some tauopathies, especially in Alzheimer's disease, a specific spatio-temporal staging of tau lesions is present. This staging has been the basis for the prion-like propagation hypothesis, which describes a cell-to-cell transfer of pathological tau species resulting in new aggregates formation in recipient neurons. Human extracellular vesicles isolated from the brain-derived fluid (BD-EVs) of Alzheimer's disease patients contain seeds that contribute to this tau pathology spreading. However, the nature of these tau species responsible for this nucleation activity remains unknown. Additionally, heterogeneity in seeding activity of BD-EVs of Alzheimer's disease, progressive supranuclear palsy and Pick's disease patients is known. - Source: PubMed
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