Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase.
about
Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locusN- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognitionEpigenetic regulation of chromatin structure and gene function by biotinBiotin and biotinidase deficiencyNuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolismBiotinLysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species in human cell cultures.K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cellsNonenzymatic biotinylation of histone H2A.Effects of Mild and Severe Vitamin B1 Deficiencies on the Meiotic Maturation of Mice OocytesK12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts.Biotin requirements are lower in human Jurkat lymphoid cells but homeostatic mechanisms are similar to those of HepG2 liver cells.Mining the TRAF6/p62 interactome for a selective ubiquitination motif.Biotinylation of K12 in histone H4 decreases in response to DNA double-strand breaks in human JAr choriocarcinoma cellsCytosine 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.H2AX: functional roles and potential applications.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Drosophila melanogaster holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan, and heat tolerance.Biotin requirements for DNA damage prevention.Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases.Feeding Drosophila a biotin-deficient diet for multiple generations increases stress resistance and lifespan and alters gene expression and histone biotinylation patternsHolocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeatsEpigenetic regulation of chromatin structure and gene function by biotin: are biotin requirements being met?Biotinylation of histones represses transposable elements in human and mouse cells and cell lines and in Drosophila melanogaster.Three promoters regulate the transcriptional activity of the human holocarboxylase synthetase gene.Repression of transposable elements by histone biotinylation.Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.Comprehensive Catalog of Currently Documented Histone Modifications.Biotinylation 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.Biotinyl-methyl 4-(amidomethyl)benzoate is a competitive inhibitor of human biotinidase.An avidin-based assay for histone debiotinylase activity in human cell nuclei.Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes.Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18.A 96-well plate assay for high-throughput analysis of holocarboxylase synthetase activity.Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.Sodium-dependent multivitamin transporter gene is regulated at the chromatin level by histone biotinylation in human Jurkat lymphoblastoma cells.The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation
P2860
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P2860
Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@ast
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@en
type
label
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@ast
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@en
prefLabel
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@ast
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@en
P2093
P2860
P1476
Lysine residues in N-terminal ...... biotinylation by biotinidase.
@en
P2093
Gabriela Camporeale
Gautam Sarath
Janos Zempleni
Yap Ching Chew
P2860
P304
P356
10.1016/J.JNUTBIO.2005.05.003
P577
2005-06-08T00:00:00Z