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H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
DAXX gene plays a role in the pathogenesis of neuroendocrine pancreatic neoplasms.
The widespread dynamic nature of DAXX methylation in association with trophoblast differentiation and placenta-associated pathologies is consistent with an important role for this gene in proper placental development and function.
findings reveal a previously unappreciated cross-talk between two crucial tumor suppressor genes, MEN1 and DAXX, thought to work by independent pathways
The interaction of Daxx C-terminal domain and androgen receptor (show AR Proteins) suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor (show AR Proteins).
HDAC1 (show HDAC1 Proteins) and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67 (show GAD1 Proteins).
We provide an overview of the individual components (ATRX, DAXX and/or H3.3) tested in each study and propose a model where the ATRX/DAXX chaperone complex deposits H3.3 to maintain the H3K9me3 modification at heterochromatin throughout the genome.
Daxx and Atrx (show ATRX Proteins) safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Proteins) levels are low.
Studies of the dynamics of the response of PML (show PML Proteins) nuclear body components and IFI16 (show IFI16 Proteins) to invading herpes simplex virus 1 genomes demonstrated that human Daxx (hDaxx) and IFI16 (show IFI16 Proteins) respond more rapidly than PML (show PML Proteins).
identifying Daxx as a broad cellular inhibitor of reverse-transcription. Altogether, these findings unravel a novel antiviral function for PML (show PML Proteins) and PML (show PML Proteins) nuclear body-associated protein Daxx
This study provides important details regarding the expression and post-translational modifications of DAXX in aging in the entire organism and provides reference data for the deregulation observed in age-associated diseases.
This is a promising novel therapeutic approach because it appears to be effective in a model producing severe injury by interfering with an array of proximal signals and effectors of the ischemic cascade, upstream of JNK (show MAPK8 Proteins), caspases, and BIM (show BCL2L11 Proteins) and BAX (show BAX Proteins) activation.
The protein levels of Daxx is reduced in Stella (show DPPA3 Proteins)-null oocytes and embryos.
Daxx selectively represses IL-6 (show IL6 Proteins) transcription through HDAC1 (show HDAC1 Proteins)-mediated histone deacetylation
Overall, these data imply a regulatory role for Daxx in reovirus-induced apoptosis, depending on its location in the nucleus or cytoplasm.
phosphorylation of Daxx by RIP3 comprises an important part of ischemic necrosis in rat retinal ganglion cells
DAXX is associated with regulatory regions of selected activity-regulated genes, where it promotes H3.3 loading upon membrane depolarization. DAXX loss not only affects H3.3 deposition but also impairs transcriptional induction of these genes.
Daxx, a HIPK kinase substrate in the apoptosis pathway, was phosphorylated by HIPK3 (show HIPK3 Proteins) at Ser (show SIGLEC1 Proteins)-669 in response to cAMP stimulation.
Neither Daxx nor PML (show PML Proteins), the main players of ND10-based immunity, are required for the block to viral gene expression in the S/G2 (show STRN3 Proteins) phase.
This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, the encoded protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. Alternative splicing results in multiple transcript variants.
28S ribosomal protein S29, mitochondrial
, death associated protein 3
, 28S ribosomal protein S29, mitochondrial-like
, CENP-C binding protein
, ETS1-associated protein 1
, Fas-binding protein
, death domain-associated protein 6
, death-associated protein 6
, fas death domain-associated protein
, Fas death domain-associated protein
, death-domain associated protein