288 related articles for article (PubMed ID: 22500635)
1. Calcium-dependent dephosphorylation of the histone chaperone DAXX regulates H3.3 loading and transcription upon neuronal activation.
Michod D; Bartesaghi S; Khelifi A; Bellodi C; Berliocchi L; Nicotera P; Salomoni P
Neuron; 2012 Apr; 74(1):122-35. PubMed ID: 22500635
[TBL] [Abstract][Full Text] [Related]
2. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres.
Lewis PW; Elsaesser SJ; Noh KM; Stadler SC; Allis CD
Proc Natl Acad Sci U S A; 2010 Aug; 107(32):14075-80. PubMed ID: 20651253
[TBL] [Abstract][Full Text] [Related]
3. HIRA and Daxx constitute two independent histone H3.3-containing predeposition complexes.
Elsaesser SJ; Allis CD
Cold Spring Harb Symp Quant Biol; 2010; 75():27-34. PubMed ID: 21047901
[TBL] [Abstract][Full Text] [Related]
4. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.
Drané P; Ouararhni K; Depaux A; Shuaib M; Hamiche A
Genes Dev; 2010 Jun; 24(12):1253-65. PubMed ID: 20504901
[TBL] [Abstract][Full Text] [Related]
5. H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.
Zink LM; Delbarre E; Eberl HC; Keilhauer EC; Bönisch C; Pünzeler S; Bartkuhn M; Collas P; Mann M; Hake SB
Nucleic Acids Res; 2017 Jun; 45(10):5691-5706. PubMed ID: 28334823
[TBL] [Abstract][Full Text] [Related]
6. Structural and mechanistic insights into ATRX-dependent and -independent functions of the histone chaperone DAXX.
Hoelper D; Huang H; Jain AY; Patel DJ; Lewis PW
Nat Commun; 2017 Oct; 8(1):1193. PubMed ID: 29084956
[TBL] [Abstract][Full Text] [Related]
7. PML is recruited to heterochromatin during S phase and represses DAXX-mediated histone H3.3 chromatin assembly.
Shastrula PK; Sierra I; Deng Z; Keeney F; Hayden JE; Lieberman PM; Janicki SM
J Cell Sci; 2019 Mar; 132(6):. PubMed ID: 30796101
[TBL] [Abstract][Full Text] [Related]
8. PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX/DAXX.
Delbarre E; Ivanauskiene K; Spirkoski J; Shah A; Vekterud K; Moskaug JØ; Bøe SO; Wong LH; Küntziger T; Collas P
Genome Res; 2017 Jun; 27(6):913-921. PubMed ID: 28341773
[TBL] [Abstract][Full Text] [Related]
9. DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.
Elsässer SJ; Huang H; Lewis PW; Chin JW; Allis CD; Patel DJ
Nature; 2012 Nov; 491(7425):560-5. PubMed ID: 23075851
[TBL] [Abstract][Full Text] [Related]
10. Death domain-associated protein 6 (Daxx) selectively represses IL-6 transcription through histone deacetylase 1 (HDAC1)-mediated histone deacetylation in macrophages.
Yao Z; Zhang Q; Li X; Zhao D; Liu Y; Zhao K; Liu Y; Wang C; Jiang M; Li N; Cao X
J Biol Chem; 2014 Mar; 289(13):9372-9. PubMed ID: 24550390
[TBL] [Abstract][Full Text] [Related]
11. DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin.
Delbarre E; Ivanauskiene K; Küntziger T; Collas P
Genome Res; 2013 Mar; 23(3):440-51. PubMed ID: 23222847
[TBL] [Abstract][Full Text] [Related]
12. CENP-B protects centromere chromatin integrity by facilitating histone deposition via the H3.3-specific chaperone Daxx.
Morozov VM; Giovinazzi S; Ishov AM
Epigenetics Chromatin; 2017 Dec; 10(1):63. PubMed ID: 29273057
[TBL] [Abstract][Full Text] [Related]
13. DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network.
Carraro M; Hendriks IA; Hammond CM; Solis-Mezarino V; Völker-Albert M; Elsborg JD; Weisser MB; Spanos C; Montoya G; Rappsilber J; Imhof A; Nielsen ML; Groth A
Mol Cell; 2023 Apr; 83(7):1075-1092.e9. PubMed ID: 36868228
[TBL] [Abstract][Full Text] [Related]
14. Single-cell analysis of Daxx and ATRX-dependent transcriptional repression.
Newhart A; Rafalska-Metcalf IU; Yang T; Negorev DG; Janicki SM
J Cell Sci; 2012 Nov; 125(Pt 22):5489-501. PubMed ID: 22976303
[TBL] [Abstract][Full Text] [Related]
15. Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
Liu CP; Xiong C; Wang M; Yu Z; Yang N; Chen P; Zhang Z; Li G; Xu RM
Nat Struct Mol Biol; 2012 Dec; 19(12):1287-92. PubMed ID: 23142979
[TBL] [Abstract][Full Text] [Related]
16. Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek.
Hollenbach AD; McPherson CJ; Mientjes EJ; Iyengar R; Grosveld G
J Cell Sci; 2002 Aug; 115(Pt 16):3319-30. PubMed ID: 12140263
[TBL] [Abstract][Full Text] [Related]
17. The histone chaperone function of Daxx is dispensable for embryonic development.
Sun C; Qi Y; Fowlkes N; Lazic N; Su X; Lozano G; Wasylishen AR
Cell Death Dis; 2023 Aug; 14(8):565. PubMed ID: 37633949
[TBL] [Abstract][Full Text] [Related]
18. DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.
DeNizio JE; Elsässer SJ; Black BE
Nucleic Acids Res; 2014 Apr; 42(7):4318-31. PubMed ID: 24493739
[TBL] [Abstract][Full Text] [Related]
19. Promyelocytic leukemia (PML) nuclear bodies (NBs) induce latent/quiescent HSV-1 genomes chromatinization through a PML NB/Histone H3.3/H3.3 Chaperone Axis.
Cohen C; Corpet A; Roubille S; Maroui MA; Poccardi N; Rousseau A; Kleijwegt C; Binda O; Texier P; Sawtell N; Labetoulle M; Lomonte P
PLoS Pathog; 2018 Sep; 14(9):e1007313. PubMed ID: 30235352
[TBL] [Abstract][Full Text] [Related]
20. A Molecular Prospective for HIRA Complex Assembly and H3.3-Specific Histone Chaperone Function.
Ricketts MD; Marmorstein R
J Mol Biol; 2017 Jun; 429(13):1924-1933. PubMed ID: 27871933
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
