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anti-Human HIST4H4 Antikörper:
anti-Rat (Rattus) HIST4H4 Antikörper:
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ata show that PP32 and SET/TAF-Ibeta proteins block HAT1-mediated H4 acetylation.
Data suggest post-translational modifications of histones, trimethylation of lysine 36 in H3 (H3K36me3) and acetylation of lysine 16 in H4 (H4K16ac), have roles in DNA damage repair; H3K36me3 stimulates H4K16ac upon DNA double-strand break; SETD2, LEDGF, and KAT5 are required for these epigenetic changes. (SETD2 = SET domain containing 2; LEDGF = lens epithelium-derived growth factor; KAT5 = lysine acetyltransferase 5)
Data suggest that O-GlcNAc transferase 1 (OGT1) specifically binds to, O-GlcNAcylates, and stabilizes nonspecific lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16.
Data show that Omomyc protein co-localized with proto-oncogene protein c-myc (c-Myc), protein arginine methyltransferase 5 (PRMT5) and histone H4 H4R3me2s-enriched chromatin domains.
H4K12ac is regulated by estrogen receptor-alpha and is associated with BRD4 function and inducible transcription
Systemic lupus erythematosus appears to be associated with an imbalance in histone acetyltransferases and histone deacetylase enzymes favoring pathologic H4 acetylation.
Data indicate that MEP50 WD repeat protein is essential for methylation of histones H4 and H2A by PRMT5 arginine methyltransferase.
Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions.
Acetylation at lysine 5 of histone H4 associated with lytic gene promoters during reactivation of Kaposi's sarcoma-associated herpesvirus.
An increase in histone H4 acetylation caused by hypoxia in human neuroblastoma cell lines corresponds to increased levels of N-myc transcription factor in these cells.
Human PIH1 domain-containing protein 1 (PIH1) interacts directly with histone H4 and recruits the Brg1-SWI/SNF complex via SNF5 to human rRNA genes.
Data indicate that G1-phase histone assembly is restricted to CENP-A and H4.
This study focused on the distribution of a specific histone modification, namely H4K12ac, in human sperm and characterized its specific enrichment sites in promoters throughout the whole human genome.
SRP68/72 heterodimers as major nuclear proteins whose binding of histone H4 tail is inhibited by H4R3 methylation.
TNF-alpha inhibition of AQP5 expression in human salivary gland acinar cells is due to the epigenetic mechanism by suppression of acetylation of histone H4.
our data suggest that global histone H3 and H4 modification patterns are potential markers of tumor recurrence and disease-free survival in non-small cell lung cancer
HAT1 differentially impacts nucleosome assembly of H3.1-H4 and H3.3-H4.
phosphorylation of histone H4 Ser 47 catalyzed by the PAK2 kinase, promotes nucleosome assembly of H3.3-H4 and inhibits nucleosome assembly of H3.1-H4 by increasing the binding affinity of HIRA to H3.3-H4 and reducing association of CAF-1 with H3.1-H4
The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer
the imatinib-induced hemoglobinization and erythroid differentiation in K562 cells are associated with global histone H4
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H4 family. Transcripts from this gene lack polyA tails\\\\; instead, they contain a palindromic termination element.
, histone 4, H4