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
- The microtubule-binding repeat region (MTBR) of tau is central to pathological aggregation and propagation in Alzheimer's disease (AD). Cryo-electron microscopy has defined residues 306-378, encompassing R3 and R4, as the ordered fibril core of AD tau; however, whether this structural core also represents the most potent seeding unit remains unclear. We generated recombinant tau fragments beginning at R1, R2, or R3 and compared their amyloid-forming and cellular seeding activities. Thioflavin T assays showed that R3-R4 and R3-378, corresponding to the AD fibril core, exhibited strong amyloid-forming activity. In contrast, FRET-based cellular assays showed maximal seeding with R2-starting fragments. Extension of R2-containing fragments into R1 markedly reduced seeding activity, indicating that R2 accessibility and sequence context, rather than the mere presence of R2, influence seed competence. These findings demonstrate a dissociation between sequence determinants of mature fibril formation and cellular tau seeding and identify exposure of R2 as a potential feature of propagation-competent tau. - Source: PubMed
Publication date: 2026/09/09
Kim Min-SeokHwang Seong-JunKim Dong-HouYoon Seung-Yong - To report a rare case of acute myeloid leukemia (AML) with abnormal chromatin clumping (ACC) in myeloblasts mimicking chronic lymphocytic leukemia (CLL), highlighting the associated diagnostic challenges. - Source: PubMed
Publication date: 2026/05/20
Horsefield Beatriz GómezGarcía David CruzGarzó Moreno AnaTuset Andujar EsperanzaSierra Leire SaizQuerol Maite Serrando - Tauopathies encompass a heterogeneous group of neurodegenerative disorders characterized by the transition of tau from a microtubule-stabilizing protein into pathogenic, seed-competent species. Increasing evidence has redefined tau from a descriptive pathological hallmark to a pharmacologically actionable target across multiple disease stages. Therapeutic opportunities are now emerging across several interconnected modules, including microtubule-associated protein tau (MAPT) gene dysregulation, 3-repeat:4-repeat (3 R:4 R) tau imbalance and pathogenic post-translational modification (PTM). Additional modules involve aggregation and seeding, liquid-liquid phase separation (LLPS), prion-like propagation, co-pathological protein interactions, and downstream injury. At the nucleic acid level, antisense oligonucleotides and splice-correcting strategies reduce total tau expression or restore pathogenic isoform balance. At the protein level, active and passive immunotherapies, proteolysis-targeting chimera (PROTAC)-based degradation, and autophagy-enhancing approaches aim to lower tau burden or eliminate pathological species. PTM-directed strategies target the transition from microtubule-bound tau to toxic soluble intermediates. However, clinical translation remains constrained by limited specificity and incomplete functional benefit. Aggregation and seeding have emerged as pharmacologically tractable processes. Key targets include the amyloidogenic motifs paired helical filament 6 (PHF6; 306-311, VQIVYK) and PHF6* (275-280, VQIINK). In parallel, LLPS and tau propagation represent additional therapeutic cascades. These involve condensate maturation, seed release, cellular uptake, glial processing, glymphatic clearance. Beyond tau-centered approaches, increasing attention has also turned to amyloid-β (Aβ) and α-synuclein co-pathology. Adjunct strategies are being developed to target neuroinflammation, synaptic dysfunction, microtubule destabilization and mitochondrial stress. Collectively, current evidence supports a paradigm shift from broad pan-tau intervention toward stage-specific, species-specific, and combination-based therapeutic strategies. - Source: PubMed
Publication date: 2026/09/04
Zhang ChengjiaMa JialiangWu XinruoWang XingyiHuang XiaohuaZheng HonghuaZhao Yingjun - Peptide and protein aggregation are hallmarks of numerous neurodegenerative diseases. However, the structural characterization of oligomeric intermediates remains challenging due to their low abundance, heterogenic nature, and complexity of coinciding and transient reaction networks. Confining reactions to microenvironments, such as picoliter droplets in droplet-based microfluidics (DBMFs), simplifies these networks, thereby enabling high-throughput analysis and controlled reaction kinetics. This study explores the integration of DBMF with ion mobility mass spectrometry (IM-MS) to probe the aggregation kinetics in droplets. We address key technical challenges, including interference from the dispersed phase, surfactant, and DBMF device material, followed by optimization strategies for droplet generation and surfactant concentration to reduce the level of contamination. Furthermore, we investigate instrumentation-based influences on ionization to improve the signal stability. Using model peptides, bradykinin, leucine-enkephalin, and the aggregation-prone segment Ac-PHF6-NH2 from the tau protein, we demonstrated the successful development of a sensitive method. Additionally, using the Ac-PHF6-NH2 peptide, oligomeric transient species were probed and characterized by their IM and m/z values. This work demonstrates the potential of DBMF-IM-MS to study peptide aggregation in confined environments, providing insights into the formation of oligomeric species and laying the groundwork for studies on larger proteins and the development of therapeutic agents targeting aggregation using multichannel devices. - Source: PubMed
Geballa-Koukoula AriadniStroganova IuliiaWillenberg HannahHes KevinKempa Emily EBarran Perdita EPiruska AigarsHuck Wilhelm T SRijs Anouk M - Copy number alterations (CNAs) drive cancer by amplifying oncogenes and deleting tumor suppressor genes. Although CNA patterns are well-studied in common cancers, they remain poorly characterized in rare tumors. - Source: PubMed
Publication date: 2026/08/14
Pavlov Vladislav SFedorova Maria SElnukaev Turpal-Ali S MKalinin Dmitry VPudova Elena AKatunina Irina VGuvatova Zulfiya GKobelyatskaya Anastasia AKaprin Andrey DKudryavtseva Anna VSnezhkina Anastasiya V