Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Disrupting the ATRX (show ATRX Proteins)/DAXX complex and inhibiting telomerase activity in telomerase-positive cancer cells lead to the alternative lengthening of telomeres switch.
Study found that enhanced nuclear accumulation of Daxx correlated with the malignant phenotype in gastric mucosa.
ATRX (show ATRX Proteins) or DAXX loss was proved to be an independent predictor for OS of PanNETs in a multivariate Cox (show COX8A Proteins) regression analysis including well-established risk factors; tumor stage and tumor grade.
Both primary Alternative lengthening of telomeres(ALT) -positive and ATRX (show ATRX Proteins)/DAXX-negative PanNETs are independently associated with aggressive clinicopathologic behavior and displayed reduced recurrence-free survival. In contrast, ALT activation and loss of ATRX (show ATRX Proteins)/DAXX are both associated with better overall survival in patients with metastases
Whole-exome sequencing has identified recurrent mutations in the genes DAXX and ATRX (show ATRX Proteins), which correlate with loss of protein expression and alternative lengthening of telomeres (ALT).ALT and DAXX/ATRX (show ATRX Proteins) loss in PanNETs was associated with shorter disease-free survival (DFS (show FST Proteins)) and disease-specific survival (DSS (show NR0B1 Proteins)) and likely plays a significant role in driving metastatic disease
We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX (show ATRX Proteins))/death-domain associated protein (DAXX) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin.
Structural and biochemical characterization of DAXX-ATRX (show ATRX Proteins) interaction.
Structural basis for DAXX interaction with ATRX (show ATRX Proteins).
Given the high frequency of ATRX (show ATRX Proteins) and DAXX mutations in cancer, these chromatin regulators likely play a key role in pathogenesis [review]
H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
PML (show PML Proteins) protein organizes heterochromatin domains where it regulates histone H3.3 (show H3F3A Proteins) deposition by ATRX (show ATRX Proteins) and DAXX.
data support a model in which activation of myogenic differentiation results in PML (show PML Proteins) NB loss, chromatin reorganization and DAXX relocalization, and provides a paradigm for understanding the consequence of PML (show PML Proteins) loss in other cellular contexts, such as during cancer development and progression
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.
Daxx and Atrx (show ATRX Proteins) safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Proteins) levels are low.
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 mRNA was detected in embryonic development from 6 h to 120 h and in all 11 selected zebrafish tissues, and Daxx expression first increased and then decreased during megalocytivirus infectious spleen and kidney necrosis virus infection.
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.
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
, death-domain associated protein
, death associated protein 3
, Fas death domain-associated protein
, LOW QUALITY PROTEIN: death domain-associated protein 6
, death-associated protein 6 L homeolog