-
berrant histone methylation of IFN-gamma associating H3K4me3 and H3K27me3 caused by over-binding of Ash2L and Jmjd3 might be involved in immune dysfunction and vascular damage in Kawasaki disease in the acute phase.
-
our results suggest that ASH2L contributes to leukemogenesis by cooperating with other proteins that aberrantly upregulate cellular growth and proliferation pathways.
-
different cancer mutations in MLL1 lead to a loss or increase in activity, illustrating the complex and tumor-specific role of MLL1 in carcinogenesis.
-
Overall, epigenetic modulation is a promising approach to evaluate the role of chromatin structure for the radioresponsiveness of glioma cell lines.
-
Data suggest an interplay between megakaryocytic leukemia 1 (MKL1) and ASH2 protein to promote tumor necrosis factor alpha (TNF-alpha) induced proinflammatory transcription in macrophages.
-
the histone methyltransferase core enzyme ASH2L was bound at EGFR in the germinal matrix and in gliomas where levels of H3K4me3 are high, and the histone acetyltransferase P300 was bound in samples with H3K27ac enrichment
-
Ash2L acts in concert with P53 promoter occupancy to activate RNA Polymerase II by aiding formation of a stable transcription pre-initiation complex required for its activation.
-
ASH2L enhances ERalpha expression as a coactivator of GATA3 in breast cancers
-
Non active site mutations in the MLL1 SET domain render the protein defective for H3K4 dimethylation by the MLL1 core complex, which is associated with a loss of the ability of MLL1 to interact with WRAD or with the RbBP5/Ash2L heterodimer.
-
Data indicate that MLL1 methylates Ash2L in the absence of histone H3, but only when assembled within a complex with WDR5 and RbBP5.
-
H2B dependent regulation of MLL family histone methylatransferases depends on the N-terminal WH motif of ASH2L.
-
crystal structure of the C-terminal SPRY domain of human Ash2L
-
The structure shows that Ash2L contains an atypical PHD finger that does not have histone tail-binding activity.
-
ASH2L binds DNA using a forkhead-like helix-wing-helix (HWH) domain.
-
NF-Y acts upstream of H3K4me3 deposition by recruiting Ash2L
-
Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes.
-
Data suggest that both Ash2L/RbBP5 and the MLL1 SET domain make direct contacts with the substrates and contribute to the formation of a joint catalytic center.
-
Results show that Depletion of CHD8 enhances HOXA2 expression and a loss of the WDR5/Ash2L/RbBP5 subcomplex.
-
Ash2l and Saf-A are recruited to the inactive X chromosome at the onset of stable X inactivation.
-
high dimethylation of histone H3 at lysine 4 expression is rare in hepatocellular carcinoma compared with other carcinomas, possibly due to complex epigenetic regulation involving Ash2
