ATRX localizes to pericentromeric heterochromatin and the short arms of human acrocentric chromosomes; this supports chromosomal localization rather than an enzymatic assignment.

ATRX phosphorylation and association with chromatin and the nuclear matrix vary across the cell cycle; the reported correlation does not define a complete causal phosphorylation mechanism.

Human ATRX mutations are associated with altered DNA methylation patterns at repetitive regions; the result does not establish intrinsic DNA methyltransferase activity.

ATRX forms a DAXX-associated nuclear remodeling complex with ATP-dependent DNA translocation and nucleosome effects, and a subset localizes to PML bodies. Selected original assays did not detect conventional duplex unwinding with the tested substrates.

A variant PxVxL motif in ATRX supports binding to the HP1 chromoshadow domain, providing a more informative molecular interaction than generic protein binding.

MeCP2 interacts with ATRX and affects its heterochromatin targeting. The inspected interaction design includes human ATRX prey and rat MeCP2 bait, with distinct mouse-cell localization experiments.

ATRX and DAXX associate with H3.3 chromatin and support its telomeric localization in mouse embryonic stem cells; human HeLa histone-complex experiments are a separate assay context.

DAXX has intrinsic H3.3/H4 chaperone activity, whereas the ATRX–DAXX complex supports ATP-dependent nucleosome remodeling and H3.3 deposition; mouse embryonic stem-cell experiments support telomeric targeting.

The ATRX ADD domain recognizes H3K9-trimethylated histone tails in the context of the H3K4 methylation state, and tested disease-associated ADD variants impair binding and heterochromatin localization.

The EBV tegument protein BNRF1 disrupts the DAXX–ATRX restriction system and promotes viral early transcription; the abstract does not by itself establish a purified binary BNRF1–ATRX interaction.

ATRX associates with macroH2A1 and restricts its chromatin accumulation, including at alpha-globin loci in human erythroleukemic cells; this is distinct from assigning ATRX macroH2A-deposition activity.

Atrx loss causes replication defects in primary mouse-cell models, while human HeLa coimmunoprecipitation supports ATRX association with the MRN complex. The mouse-focused title does not exclude the human experiment.

This systematic interaction study is the source cited for a generic ATRX–DAXX interaction row. The exact pair-level matrix entry and score were not independently inspected; separate targeted studies establish the association.

Selected Results support ATRX association with PRC2 and Xist RNA. Isolated EZH2 contact, complete construct-species details and the contents of two linked corrections remain unverified.

In human telomerase-positive glioma cells, ATRX localizes to subtelomeric chromatin and its loss reduces telomeric cohesin and TERRA; ATRX inactivation alone did not initiate ALT in that model.

In hypomethylated mouse embryonic stem cells, DAXX/Atrx-associated chromatin protects tandem repeats and supports H3K9 trimethylation through the chromatin machinery; this is not ATRX methyltransferase catalysis.

The ATRX–macroH2A1.1–tankyrase axis regulates timely resolution of sister-telomere cohesion and recombination in ALT-cell contexts; cohesion resolution is distinct from the amount of chromatin-bound cohesin.

This interaction-network source underlies a generic ATRX–DAXX annotation. Exact pair-level assay details were not independently verified; targeted ATRX/DAXX literature supplies separate biological support.

Human-cell chromatin experiments connect ATRX with TRIM28, SETDB1 and ZNF274 at atypical zinc-finger gene chromatin domains and H3K9me3 preservation; coimmunoprecipitation is not proof of each purified binary interface.

This proteome-scale interaction source is cited for ATRX–DAXX association. Its precise matrix entry and score were not independently inspected, so reference-level verification is limited despite independent targeted support.

Pathogenic variants in the human ATRX locus establish its association with X-linked intellectual disability and alpha-thalassemia; the early predicted regulatory mechanism is not itself a catalytic assay.

The historical human XH2 cloning study identifies the locus later named ATRX. Its early sequence and putative-helicase interpretation do not replace the current full-length sequence or direct biochemical evidence.

The normal human event describes ATRX binding DAXX in a chromatin-remodeling assembly.

The human event places ATRX–DAXX at subtelomeric chromatin and links it to cohesin recruitment and TERRA regulation.

The event describes ATRX/DAXX-dependent telomeric H3.3 deposition, distinguishing DAXX histone handling from HIRA-associated deposition pathways.

This disease event describes defective ATRX variants and their DAXX association, distinguishing fragment assays from inferred loss-of-function candidate variants; it is not a negation for normal ATRX.

This disease event concerns defective DAXX variants in ATRX association and distinguishes fragment experiments from full-length mutant testing; it does not establish universal failure of the normal complex.

A conserved truncated ATRX product lacks the SWI/SNF motifs and differs from full-length ATRX in PML-body localization. The human/mouse transcript mechanism does not by itself map the reported product to a particular current UniProt isoform.

Human ATRX-deficient cells show impaired replication restart and a reduced origin-firing readout after hydroxyurea; the authors caution that inefficient CldU incorporation during recovery may contribute to the latter observation. The authors conclude that ATRX does not regulate replication rate from unchanged fiber lengths after release. MRN copurifies with ATRX; cotransfection pull-down recovers NBS1 rather than the other tested MRN components.

Atrx loss in mouse neural progenitors produces replication-associated damage with ATM activation and downstream p53-dependent apoptosis; combined p53 loss increases persistence of damaged cells.

Purified human ATRX fragments map macroH2A-H2B recognition to the ADD domain, with discrimination from canonical H2A in the tested assays. The same study distinguishes direct CHD4 peptide binding from broader NuRD associations.

Human-cell separation-of-function experiments distinguish PIP-dependent protection against genome-wide replication stress from ATPase-dependent suppression of telomeric single-stranded DNA, with endpoint-specific dependence on the ATRX-DAXX interaction.