Phosphorylation of histone H3 correlates with transcriptionally active loci
about
MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14The human CDK8 subcomplex is a histone kinase that requires Med12 for activity and can function independently of mediatorTumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complexGenome-wide review of transcriptional complexity in mouse protein kinases and phosphatases.A tale of histone modifications.Epigenetics of cervical cancer. An overview and therapeutic perspectivesGlucocorticoids, epigenetic control and stress resilienceTranscriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylationPhosphorylation of histone H3 during transcriptional activation depends on promoter structureDistinct epigenetic and gene expression changes in rat hippocampal neurons after Morris water maze training.Exercise improves cognitive responses to psychological stress through enhancement of epigenetic mechanisms and gene expression in the dentate gyrus.14-3-3 mediates histone cross-talk during transcription elongation in Drosophila.Regulation of iNOS gene transcription by IL-1β and IFN-γ requires a coactivator exchange mechanism.Methyl-CpG binding domain proteins inhibit interspecies courtship and promote aggression in Drosophila.Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms.Protein composition of interband regions in polytene and cell line chromosomes of Drosophila melanogaster.Akirin links twist-regulated transcription with the Brahma chromatin remodeling complex during embryogenesis.Protein modules that manipulate histone tails for chromatin regulation.An embarrassment of niches: the many covalent modifications of histones in transcriptional regulation.The Rb/chromatin connection and epigenetic control: opinion.Phosphorylation of histone variant regions in chromatin: unlocking the linker?Chromatin decondensation and nuclear reprogramming by nucleoplasminSelective repression of low-density lipoprotein receptor expression by SP600125: coupling of histone H3-Ser10 phosphorylation and Sp1 occupancySurvivin selectively modulates genes deregulated in human leukemia stem cells.The chromosomal association/dissociation of the chromatin insulator protein Cp190 of Drosophila melanogaster is mediated by the BTB/POZ domain and two acidic regionsHistone variants and histone modifications: a structural perspective.The Drosophila P68 RNA helicase regulates transcriptional deactivation by promoting RNA release from chromatinDNA hypermethylation in Drosophila melanogaster causes irregular chromosome condensation and dysregulation of epigenetic histone modifications.BIR-1, a Caenorhabditis elegans homologue of Survivin, regulates transcription and development.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Signal Transduction Pathways Leading to Heat Shock Transcription.Epigenetic regulation of stress responses in plants.Functional role of RNA polymerase II and P70 S6 kinase in KCl withdrawal-induced cerebellar granule neuron apoptosis.MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation.Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulatedProtein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster.Regulation of Torpor in the Gray Mouse Lemur: Transcriptional and Translational Controls and Role of AMPK SignalingLessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.The cloning and characterization of the histone acetyltransferase human homolog Dmel\TIP60 in Drosophila melanogaster: Dmel\TIP60 is essential for multicellular developmentHistone modifications at the ABCG2 promoter following treatment with histone deacetylase inhibitor mirror those in multidrug-resistant cells.
P2860
Q24303450-5ADA57FB-7333-41CD-979D-2D318C274924Q24320150-A45AA830-FAAD-4DE3-A217-5BC2370C9C00Q24534882-55CD948E-4CEB-4B73-83D7-7544A00E7961Q24548067-03EC76C8-25EA-431F-AF76-0C2CE12E3E7AQ24805396-74E2D700-CB54-44FB-86A7-C1821B2F9FB2Q24812104-403C0D55-1497-45FB-9CB5-1E25810141A8Q28088692-25BB681B-E14E-4D2E-B524-4239171EF6ABQ28363102-71956E11-D08F-40D8-82D1-66B9891E94BBQ30450451-203E9433-AFC9-4FD0-A3A4-6C817765D6CBQ30654504-8A5F6934-F327-4D4F-AD18-C32C52068893Q33404079-17C6ADF6-DCDD-4845-A6FC-6A5CB4814B7BQ33598533-7B5D2816-121D-4E1F-AADC-40BDF6342CF1Q33669239-95EE1197-C4EB-4660-A9D5-8FDF94C0505BQ33905565-9736A666-6260-4A63-85E0-61583BA283F2Q33930752-6DC553D1-17C0-4E06-BCCD-9BA193B2BC4AQ34077027-205EDE6B-2DBA-4B8A-80A0-82495E8B616BQ34187034-42973BAA-AC42-474E-8EB2-4DDA26BD564CQ34271581-E66D8E66-307C-45F1-B78F-E4E900907DBDQ34290234-A7A235D4-F0A6-461B-9E71-3265FC139360Q34290306-B078243B-BE0B-47B2-AD50-41463121DE9EQ34316278-8B4B3239-73F1-4E2A-82CA-7DE49539FB4CQ34353713-FD962A50-1009-4A3F-B50C-F29C291C74ADQ34353731-3C2F2AA6-3C3D-41CD-8DEA-DE01FF8B83A9Q34495409-53FFCAE8-BEAB-4EF4-AE7D-7BC071D7D7B3Q34499292-F7DB7A06-8C96-444E-9705-555EB67180AEQ34500001-2EBDCBE3-7F5E-4DE5-BBB4-217E97125324Q34649267-DB5EC4F1-D82E-4484-B6E2-057E4ADF6D95Q34784614-A8678ABC-AB74-439F-86F7-A8A64F9A6AAFQ34982547-D48C7BCB-1110-4775-A555-A9085A28A9D1Q34990282-2006D998-0C83-467D-9143-DB2B8616F80AQ35047254-F7EFCD25-4494-4C74-8818-72EA314E4088Q35114858-AD2E4F1A-251A-4E7C-A4F8-FD75CBD42892Q35126559-A3247041-B76D-463A-83EE-52421BF6D211Q35163934-B3DE2F26-EFEF-4D1D-ACFF-CD4C5E34838EQ35423830-457FF858-22F8-4031-BC88-324FEABB6F91Q35661433-567C4F9C-C147-4C57-8E6C-4EF7E585D95FQ35669187-3880795E-A4EB-463D-81F7-BD453C452CBCQ35684970-E05B6DD7-97AA-4EBB-9D22-18400F0F98BFQ35730122-6DE54F04-F5A0-4A21-BA6D-CF97245D7A2CQ35837565-819C5D8C-8428-4369-ACC2-EA0EC04A6648
P2860
Phosphorylation of histone H3 correlates with transcriptionally active loci
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Phosphorylation of histone H3 correlates with transcriptionally active loci
@ast
Phosphorylation of histone H3 correlates with transcriptionally active loci
@en
type
label
Phosphorylation of histone H3 correlates with transcriptionally active loci
@ast
Phosphorylation of histone H3 correlates with transcriptionally active loci
@en
prefLabel
Phosphorylation of histone H3 correlates with transcriptionally active loci
@ast
Phosphorylation of histone H3 correlates with transcriptionally active loci
@en
P2860
P356
P1433
P1476
Phosphorylation of histone H3 correlates with transcriptionally active loci
@en
P2093
V G Corces
P2860
P304
P356
10.1101/GAD.848800
P577
2000-12-01T00:00:00Z