K4, K9 and K18 in human histone H3 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 metabolismBiotinComputer-aided Molecular Design of Compounds Targeting Histone Modifying EnzymesK12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cellsModulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesNonenzymatic 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.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.Biotin regulates the expression of holocarboxylase synthetase in the miR-539 pathway in HEK-293 cells.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.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.Quantitative proteomic approaches to studying histone modifications.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 repeatsIdentification and assessment of markers of biotin status in healthy adults.Epigenetic 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.Repression of transposable elements by histone biotinylation.Vitamin deficiencies in humans: can plant science help?Posttranslational modifications of human histone H3: an update.Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3.Epigenetics and miRNA during bacteria-induced host immune responses.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.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.
P2860
Q24295190-88F232DE-F1DF-4D37-9A20-3131D81C6242Q24318883-AEEA0A95-7938-4946-BCD0-F9A616D63CE7Q24548295-F2D340D6-EDF7-4437-A92D-67737D9E83D4Q24651550-BAAFC7A0-70F1-46B5-B9B4-3D710C005B1AQ24669960-591085BA-5C4F-4DD1-AB89-05D548057F79Q26864754-F52D01FD-E7B7-4953-8D1B-D04460A9C630Q28026625-D6F110E4-3D0B-4EBE-A589-1F1FADD37B7DQ28083849-0C036C4C-744B-4581-976B-FEBB18DFC75EQ30440966-34788BAE-9738-491C-AE2F-298BED547B39Q30570945-E5A607CC-C9D5-49EC-902F-6D8636605990Q33401809-838EBF61-85E9-4914-8CE0-51D185594AAAQ33574775-E1436209-FA94-4CB3-825B-EC3CA38869CAQ33787189-61772EC5-592B-4A9B-9DEE-2BE2CDAF510AQ33813111-B55373A8-7B53-4F91-AA78-2B97D9A9AB7CQ33849277-F418604B-EE0C-40A8-8234-00FD561A96E0Q34076084-4AB1A924-35A5-4279-8B03-F235A4F5DE29Q34093042-23577DD2-5575-472F-91C6-E4E39B404F40Q34201091-351EFD2C-B5E4-424C-8265-DA2FFEAD3897Q34990282-DE8548C6-065D-4B82-8648-E01AA90DEB64Q35113882-4AF2A8E9-824A-421E-A7CD-B4C209A987D3Q35228865-DA618366-8EFC-4188-960F-7C52F6341F49Q35587278-E3D8AD82-8E19-4DBC-9307-0D70BF93FA34Q35698874-2B6579CA-FDC0-42DA-AF92-F54F119281DAQ36377597-F480B0E2-0513-45C3-B343-6669D5CA2E2EQ36551230-FD3D0666-F2BD-424D-B791-F306DA688B48Q36551861-E75F0B59-9DA9-4A36-BBE5-9F05736B6145Q36924683-B1C635DA-06A1-4D40-BFE6-B9F1AB00C32BQ37184040-A40B4A98-C65F-43B1-B79B-AD72CF1EF7BBQ37610665-371FB08A-1E39-4744-9C5A-C4A515958F07Q37989072-DBE17426-AAA3-45B0-9F32-D57AFAE5B77CQ38232008-D7D36AA8-4C5E-4FCB-904C-B1E0CEB8310DQ38314552-5A7DE979-0E6D-4B83-B372-84D7AA88FEDBQ38639010-380326DC-B140-4547-94A2-83DADB21D0C0Q39376061-7C1F9F51-4304-48FE-B076-9530BCA86CE5Q39595968-2756720D-2B3B-454C-B40D-C2B8493ACBFBQ40022345-7DE0D099-704A-4D4D-9DE8-9BE3BB41237EQ40198999-06659E80-DD5B-4EE5-B4FB-84D254FE823CQ41436500-B99AEFB7-12BE-4535-93A1-CB021BBD0147Q41849919-E14FDC50-CAB2-4DDD-947D-88A45E614D70Q41920152-EBF03926-CA2D-456B-B9D8-275BD73FDCE6
P2860
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին 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
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@ast
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@en
type
label
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@ast
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@en
prefLabel
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@ast
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@en
P2093
P2860
P1433
P1476
K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase.
@en
P2093
Alice Kueh
Brian Rueckert
Gabriela Camporeale
Jacob B Griffin
Janos Zempleni
Keyna Kobza
P2860
P304
P356
10.1111/J.1742-4658.2005.04839.X
P407
P577
2005-08-01T00:00:00Z