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The protein encoded by ATRX contains an ATPase/helicase domain, and thus it belongs to the SWI/SNF family of chromatin remodeling proteins. Additionally we are shipping ATRX Antibodies (127) and many more products for this protein.
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The results of this study support an important role for ATRX loss and acquisition of ALT in the biology of NF1 (show NF1 Proteins)-associated gliomas, particularly diffuse and high-grade tumors developing in adults.
We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX (show DAXX Proteins)) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin.
Structural and biochemical characterization of DAXX (show DAXX Proteins)-ATRX interaction.
Structural basis for DAXX (show DAXX Proteins) interaction with ATRX.
Review of research progress of TERT (show TERT Proteins)-mediated and ATRX-mediated telomere maintenance and neuroblastoma (show ARHGEF16 Proteins), especially high-risk tumors
This study demonstrated the ATRX loss in glioneuronal tumors with neuropil-like islands.
6 cases of diffuse glioma that presented a diagnostic challenge due to conflicting IDH1 (show IDH1 Proteins)/IDH2 (show IDH2 Proteins), ATRX, and 1p/19q results.
The chromatin remodeling enzyme ATRX is a regulator of therapy induced senescence and drives cells into this state via multiple mechanisms.
The present study explored the structural consequences influenced by two observed mutations V194I and C220R on ADD domain of ATRX protein by applying all atom molecular dynamics (MD) simulation.
Study demonstrate that the retention of ATRX expression in all oligodendroglial tumor nuclei strongly supports the diagnosis of oligodendroglioma. Conversely, its loss in tumor astrocytic nuclei favors the diagnosis of astrocytoma.
Gene expression changes in the Atrx-null retina indicate defective synaptic structure and neuronal circuitry, suggest excitotoxic mechanisms of neurodegeneration, and demonstrate that common targets of ATRX in the forebrain and retina may contribute to similar neuropathological processes underlying cognitive impairment and visual dysfunction in ATR-X syndrome.
mosaic loss of ATRX expression in the central nervous system leads to endocrine defects and decreased body size and has a negative impact on learning and memory.
The results suggest that ATRX is required to limit replication stress during cellular proliferation, whereas upregulation of PARP-1 (show PARP1 Proteins) activity functions as a compensatory mechanism to protect stalled forks, limiting genomic damage, and facilitating late-born neuron production.
Our study highlights the importance of the cooperation between Rad54 (show RAD54L Proteins) and Mus81 (show MUS81 Proteins) for mediating DNA DSB repair and restraining chromosome missegregation.
The long noncoding RNA, TERRA (show DMRT2 Proteins) can bind both in cis (show CISH Proteins) to telomeres and in trans to genic targets; a large network of interacting proteins was defined, including epigenetic factors, telomeric proteins, and the RNA helicase, ATRX. TERRA (show DMRT2 Proteins) and ATRX share hundreds of target genes and are functionally antagonistic at these loci: whereas TERRA (show DMRT2 Proteins) activates, ATRX represses gene expression.
The changes of ATRX distribution occur and partially correlate with the main stages of zygotic genome activation during mouse early development, butthese changes seem to be determined by other processes of structural and functional rearrangements of blastomere nuclei.
ATRX mutation is associated with increased mutation rate at the single-nucleotide variant (SNV) level.
Daxx (show DAXX Proteins) and Atrx safeguard the genome by silencing repetitive elements when DNA methylation (show HELLS Proteins) levels are low.
A direct role of Atrx in the establishment and robust maintenance of heterochromatin is demonstrated.
We propose a model whereby ATRX-dependent deposition of H3.3 into heterochromatin is normally required to maintain the memory of silencing at imprinted loci.
The protein encoded by this gene contains an ATPase/helicase domain, and thus it belongs to the SWI/SNF family of chromatin remodeling proteins. The mutations of this gene are associated with an X-linked mental retardation (XLMR) syndrome most often accompanied by alpha-thalassemia (ATRX) syndrome. These mutations have been shown to cause diverse changes in the pattern of DNA methylation, which may provide a link between chromatin remodeling, DNA methylation, and gene expression in developmental processes. This protein is found to undergo cell cycle-dependent phosphorylation, which regulates its nuclear matrix and chromatin association, and suggests its involvement in the gene regulation at interphase and chromosomal segregation in mitosis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported.
ATP-dependent helicase ATRX
, DNA dependent ATPase and helicase
, X-linked helicase II
, X-linked nuclear protein
, Zinc finger helicase
, alpha thalassemia/mental retardation syndrome X-linked (RAD54 homolog, S. cerevisiae)
, helicase 2, X-linked
, transcriptional regulator ATRX
, alpha thalassemia/mental retardation syndrome X-linked homolog
, helicase II
, HP1 alpha-interacting protein
, alpha thalassemia/mental retardation syndrome (X-linked)
, heterochromatin protein 2
, DNA repair and recombination protein RAD54-like
, RAD54 homolog