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
- Plant Homeodomain Finger Protein 6 (PHF6) gene mutations are rare in acute myeloid leukemia (AML), with unclear mechanisms and uncertain prognostic value. They may compromise risk stratification and treatment decisions. This study analyzed clinical features and survival outcomes in PHF6-mutated AML patients, evaluating the impact of allogeneic hematopoietic stem cell transplantation (HSCT) and co-mutations on prognosis. Precise stratification helps optimize prognostic models and guide individualized therapy. - Source: PubMed
Wang DongmeiPan HanzhangWang YunguiXu HuanLiu LinXu YutingTong Hongyan - Analogues of a tau protein subunit (VQIVYK, or PHF6) containing a medium-sized or bulky α,β-dehydroamino acid (ΔAA) were synthesized and evaluated for their ability to inhibit aggregation of the parent peptide. The ΔAAs were constructed via the dehydration of the corresponding β-hydroxyamino acids. Some analogues were assembled by solid-phase peptide synthesis, but a solution-phase strategy was required in two cases due to the failure of a key azlactone ring-opening amidation. The ΔAA-containing peptides are 2-20 times more stable to proteolysis than related proline-containing PHF6 analogues. Transmission electron microscopy and Thioflavin T (ThT) assays revealed that the ΔAA-containing analogues are potent inhibitors of PHF6 aggregation. The impact of the analogues on the morphology of the preformed PHF6 fibrils was also investigated. This study validates the use of medium-sized or bulky ΔAAs as tools for increasing the proteolytic stability of functional peptides. - Source: PubMed
Publication date: 2026/04/28
Garcia Stephanie GAlmardini Ahmad AbdullatifPereira Aramis JXing HuihuaKnox Logan JJimenez Julie VWebster-Ford Joshua CMoyá Diego APayne Joshua CDawes Courtney KConda-Sheridan MartinCastle Steven L - The pathological conversion of intrinsically disordered proteins into β-sheet-rich amyloid filaments is a hallmark of numerous neurodegenerative disorders. In the case of tau protein, misfolding into aggregation-prone species can be promoted by truncation, motivating the present study. We employed an integrative approach combining established experimental techniques, including AFM and ThT fluorescence assay, with MD simulations to study amyloidogenic propensities of five tau truncation variants in the presence of aggregation inducers in vitro. The experimental observations were further validated by CD and NMR spectroscopy. Our experiments demonstrated that tau variants exhibit distinct amyloidogenic propensities. Tau variant spanning residues 321-391 (numbered according to the longest CNS tau isoform 1-441) represents the minimal E391-truncated construct capable of amyloid aggregation in vitro, whereas the shorter 326-391 variant failed to form fibrillar assemblies, even in the presence of aggregation inducers. All-atom (AA) MD simulations highlighted the importance of hairpin-like structural motifs during the early stages of aggregation, which appear to template subsequent fibril growth and are preferentially adopted by the Tau321-391 variant. In contrast, coarse-grained (CG) simulations revealed a pronounced α-helical propensity in Tau321-391, particularly at the N-terminal region. This elevated N-terminal helicity constitutes the most prominent structural distinction between the aggregation-competent and aggregation-incompetent variants. In both AA and CG MD simulations, the structural transitions of tau were driven by amyloid-nucleating sequence motifs, including the G-motif, PHF6**, and PAM4. Despite sharing these amyloidogenic regions, the Tau326-391 variant lacks the intrinsic amyloid propensity required to undergo productive self-assembly into ordered amyloid fibrils. - Source: PubMed
Publication date: 2026/04/17
Njemoga StefanaMajerova PetraPiestansky JurajGazova ZuzanaKaderavek PavelBarrera Exequiel EBednarikova ZuzanaCehlar Ondrej - Contemporary risk models in chronic myelomonocytic leukemia (CMML) focus on the prognostic relevance of individual rather than concurrent mutations. In the current study of 605 Mayo Clinic patients with CMML, we applied machine-learning algorithms in order to examine the influence of cooperative mutational interactions on blast transformation (BT). A hierarchical clustering algorithm was developed and tailored for patient stratification using survival outcomes and co-occurrence of genomic alterations. Five molecular clusters were identified with 3-year blast BT rates ranging from 0% to 100% (AUC at 3 years 0.78). A subsequent Cox regression analysis confirmed independent detrimental impact of specific mutations or their combinations including NPM1 (HR 26.7; p < 0.01), "NRAS + SETBP1" (HR 12.6; p < 0.01), "ASXL1 + BCOR" (HR 8.4; p < 0.01), "ASXL1 + RUNX1" (HR 2.2, p < 0.01), JAK2 (HR 2.1; p < 0.01), and "ASXL1 + TET2" (HR 1.7; p = 0.02) while "PHF6+wild-type ASXL1" (HR 5.61e-10; p < 0.01) had a favorable impact. Furthermore, compared to NPM1 wild-type cases, NPM1-mutated patients were less likely to have co-occurring mutations involving ASXL1 (0% vs. 43%, p < 0.01), RUNX1 (0% vs. 17%, p = 0.02), and SRSF2 (7% vs. 39%, p < 0.01) and were more likely DNMT3A (71% vs. 7%, p < 0.01). The prognostic relevance of "NRAS + SETBP1", "ASXL1 + RUNX1", NPM1 and BCOR was validated in an external cohort from Italy (N = 501). Taken together, these observations highlight i) the possibility of prognostic interaction of mutations in CMML that should be considered in the development of future risk models and ii) the distinct genotypic and prognostic characteristics of NPM1-mutated CMML. - Source: PubMed
Publication date: 2026/04/12
Fathima SaubiaRokach LiorYousuf MuhammadFaldu PriyanshAlsugair AliCsizmar CliffordNakhleh MerryMangaonkar Abhishek APardanani AnimeshLanino LucaCampagna AlessiaMaggioni GiuliaFarnoud NoushinRampal RaajitReichard Kaaren KHe RongGangat NaseemaPatnaik Mrinal MDella Porta Matteo GTefferi Ayalew - T-cell lymphoblastic lymphoma (T-LBL) and T-cell acute lymphoblastic leukemia (T-ALL) originate from thymic T-cell precursors, with ongoing debate on whether they are variants of the same disease or distinct entities. For 211 patients, including pediatric and adult T-ALL and T-LBL cases, targeted next-generation sequencing and SNP-arrays were performed, and single-nucleotide variants, indels and copy-number variants (CNVs) were analyzed. We aimed to assess genetic differences between T-ALL and T-LBL across age. Generally, mutational landscape analysis identified mutated PHF6 being associated with higher, NOTCH1 with lower age at diagnosis for both T-LBL and T-ALL. Association of CNVs with higher age was evident for T-ALL, but not T-LBL. Analysis of clonal evolution revealed that CNVs - especially deletions and LOH in chromosome 9 (LOH_in_9p) - were observed as first mutational event in both pediatric T-ALL and T-LBL. The sequence of genetic events, starting with LOH_in_9p followed by mutations in NOTCH1, was significantly more frequent in pediatric T-ALL and T-LBL. Detailed evaluation of the patients' individual clonal evolution indicated that the proportion of malignant cells without NOTCH determines the risk of relapse (hazard ratio 1.032, p = 4.65*10). In T-ALL, aside from MRD, validated molecular markers for risk-group stratification remain limited. Our data suggest that molecular metrics analogous to those in T-LBL may help refining risk stratification in T-ALL as well. - Source: PubMed
Publication date: 2026/04/02
Sandmann SarahTe Vrugt MarcelRandau GerritBeder ThomasNeumann MartinLange ToniAlfert AmelieMueller StephanieHotfilder MarcRossi CorinneEckert CorneliaMoericke AnjaHorns Johanna MariaZimmermann MartinVarghese JulianBrüggemann MonikaBurkhardt Birgit