PHF6 antibody Host rabbit
- Known as:
- PHF6 (anti-) Host host: rabbit
- Catalog number:
- 'ARP51237_T100
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- PHF6 antibody Host rabbit
Related genes to: PHF6 antibody Host rabbit
- 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 Host rabbit
Related articles to: PHF6 antibody Host rabbit
- To evaluate time to diagnosis in infants with very early-onset genetic epilepsies, identify contributing factors to diagnostic delay, and assess the impact of a definite diagnosis on clinical management. - Source: PubMed
Publication date: 2026/08/10
Pizzuto ChiaraMorabito ValeriaCarapancea EvelinaCilio Maria Roberta - Mammalian large tumor suppressor 2 (LATS2) is an evolutionarily conserved Ser/Thr kinase that regulates the Hippo signaling pathway and cell cycle checkpoints. In this study, we demonstrate that ultraviolet (UV) irradiation causes the phosphorylation of LATS2 at S835, leading to localization of a portion of it to the nuclear speckle, which is a membraneless organelle enriched in pre-mRNA splicing factors in the nucleoplasm. This phosphorylation can potentially enhance LATS2 kinase activity and induce subsequent phosphorylation of plant homeodomain finger protein 6 (PHF6) at S183. We also show that LATS2 promotes ribosomal RNA (rRNA) transcription in the absence of UV irradiation and that PHF6 is translocated from the nucleolus to the nucleoplasm after UV damage. Some of the phosphorylated PHF6 localizes in the nuclear speckles after UV irradiation, eventually preventing LATS2-mediated rRNA transcription. These results suggest that the nuclear speckle functions as a sequestration site for transcriptional regulators and as a crucible that promotes biochemical reactions in the DNA damage response. Therefore, a strategy targeting the LATS2-PHF6 axis could facilitate the development of new therapies for critical diseases caused by abnormal rRNA synthesis, such as ribosomopathies and cancers. - Source: PubMed
Publication date: 2026/08/13
Suzuki HirokazuMukai SatomiKato YorikaSakashita EijiEndo HitoshiNojima HiroshiYabuta Norikazu - Mixed phenotype acute leukemia (MPAL) is a rare and biologically heterogeneous category characterized by discrete admixed populations of myeloid and lymphoid blasts (bilineal or mixed lineage) or with coexpression of lymphoid and myeloid markers in a single blast population (biphenotypic or mixed phenotype). Despite advances in diagnostic criteria, MPAL remains a significant diagnostic and therapeutic challenge due to its immunophenotypic complexity and genetic diversity. Accurate classification relies heavily on multiparameter flow cytometry immunophenotyping, integrated with cytogenetic and molecular studies. The current World Health Organization classification and International Consensus Classification recognize specific genetic subtypes, including MPAL with t(9; 22)(q34.1; q11.2)/BCR::ABL1 and MPAL with KMT2A rearrangement, reflecting the increasing importance of genomic profiling in disease characterization. Recent genomic studies have revealed additional recurrent alterations involving transcription factors, epigenetic regulators, signaling pathways, and lineage-specifying genes, including ZNF384 rearrangements, BCL11B alterations, mutations involving PHF6, WT1, FLT3, and RUNX1, and mutations affecting chromatin remodeling and cytokine signaling pathways. Importantly, distinct genetic lesions appear to correlate with specific immunophenotypic patterns, suggesting biologically meaningful disease subsets and providing insights into mechanisms of lineage plasticity and leukemogenesis. This review summarizes the current understanding of the immunophenotypic and genetic landscape of MPAL, emphasizing the integration of morphologic, immunophenotypic, cytogenetic, and molecular findings into diagnosis and subclassification. - Source: PubMed
Publication date: 2026/06/25
Leventaki VasilikiWang Sa A - Neurofibrillary tangles, composed of aggregated Tau proteins, are a pathological hallmark of Alzheimer's disease (AD). Within these tangles, the amyloid core is primarily formed by the microtubule-binding (MTB) repeats. Although site-specific acetylation has been implicated in the regulation of Tau aggregation, the atomic-level mechanisms by which individual acetylation events modulate the structure and interactions of amyloid-forming motifs remain incompletely understood. In particular, whether dual acetylation events may act cooperatively during early Tau assembly is still unclear. In this study, we used microsecond-scale all-atom molecular dynamics simulations to systematically examine the dimerization dynamics of the four Tau MTB repeat homodimers (R1-R4). Our simulations suggest that the relatively higher aggregation propensity of R3 and R4 may be associated with amyloidogenic, β-sheet-prone core sequences, in which the key lysine residues K311 and K353 are located. Further analysis indicates that acetylation at these sites attenuates early Tau dimerization: K353 acetylation appears to moderately destabilize the R4 dimer through steric effects and the disruption of intrachain salt bridges, resulting in a more disordered conformational ensemble. K311 acetylation shows a more pronounced inhibitory effect on R3 dimerization by neutralizing the positive charge of K311 and weakening key interchain salt bridges and π-cation interactions associated with the PHF6 motif. Notably, dual acetylation of K311 and K353 in the R3-R4 dimer produces a stronger-than-additive reduction in β-sheet formation. This potential synergistic effect arises from the combined disruption of the hydrophobic core and distal electrostatic interaction networks. In summary, our results provide a molecular-level explanation for how acetylation at K311 and K353 cooperatively modulates Tau dimerization and early amyloid nucleation, offering mechanistic insight into the role of lysine acetylation in Tau aggregation. - Source: PubMed
Publication date: 2026/06/20
Wu JiaxuanHe XinyuFu MinghuaLiu YueSu WanLi RuopengXu MingmingChan Kevin ChunHuang DaiyunWu Sijin - Characterizing the conformational landscapes of intrinsically disordered proteins is essential for elucidating their roles in health and disease, but remains challenging due to their structural heterogeneity. In this study, we introduce an enhanced algorithmic framework for the Energy Landscape Visualization Method (ELViM) that enables the simultaneous mapping of monomeric and oligomeric conformational spaces within a unified metric space. Unlike traditional reaction-coordinate-based approaches, this extended ELViM implementation employs a distance-based similarity metric and force projection embedding to generate low-dimensional representations that preserve high-dimensional structural relationships without predefined bias. We expanded the standard workflow by integrating a density-guided Local Conformational Signature analysis coupled with a new consensus interchain contact mapping protocol. This development allows for the systematic disentanglement of intrachain folding dynamics from the interchain assembly interactions that drive protein aggregation. Using replica exchange molecular dynamics data for a 19-residue fragment of the tau protein, we demonstrate the method's utility by comparing the conformational landscapes of the wild type and the aggregation-associated P301L mutant. ELViM effectively captures continuous conformational transitions and highlights key structural motifs, including the aggregation-prone PHF6 segment (VQIVYK). The analysis reveals how the P301L mutation acts as a structural stabilizer, shifting conformational preferences toward compact, preorganized ensembles with more persistent interchain contacts around PHF6. By providing a quantitative yet intuitive framework for exploring heterogeneous ensembles, this enhanced ELViM workflow offers broad applicability to studying folding landscapes, protein-protein interactions, and complex aggregation pathways. - Source: PubMed
Publication date: 2026/06/18
Sanches Murilo NGanguly PritamShea Joan-EmmaLeite Vitor B P