K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts.

K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts.

Item
http://www.wikidata.org/entity/Q33787189
Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolismLysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species in human cell cultures.The role of histone H4 biotinylation in the structure of nucleosomes.Biotin requirements are lower in human Jurkat lymphoid cells but homeostatic mechanisms are similar to those of HepG2 liver cells.Cytosine methylation in miR-153 gene promoters increases the expression of holocarboxylase synthetase, thereby increasing the abundance of histone H4 biotinylation marks in HEK-293 human kidney cells.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Biotin requirements for DNA damage prevention.Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeatsBiotinylation is a natural, albeit rare, modification of human histones.Identification of holocarboxylase synthetase chromatin binding sites in human mammary cell lines using the DNA adenine methyltransferase identification technology.Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes.Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.Holocarboxylase synthetase synergizes with methyl CpG binding protein 2 and DNA methyltransferase 1 in the transcriptional repression of long-terminal repeats.K16-biotinylated histone H4 is overrepresented in repeat regions and participates in the repression of transcriptionally competent genes in human Jurkat lymphoid cellsThe role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events.Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation.
P2860

K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts.

Item
http://www.wikidata.org/entity/Q33787189
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
@ast
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
@en
type
label
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
@ast
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
@en
prefLabel
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
@ast
K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
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K12-biotinylated histone H4 is ...... human lung IMR-90 fibroblasts.
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10.1016/J.JNUTBIO.2009.01.010
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P5875
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P932