Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
about
Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patternsActivation of androgen receptor function by a novel nuclear protein kinaseDynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: analysis at c-fos and c-jun.Histone acetylation: novel target for the treatment of acute lymphoblastic leukemiaFunctional Role of G9a Histone Methyltransferase in CancerMultiple levels of epigenetic control for bone biology and pathologyTranscriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylationDynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylationCR Cistrome: a ChIP-Seq database for chromatin regulators and histone modification linkages in human and mouseMultivalent engagement of chromatin modifications by linked binding modulesPhosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activationDistinct epigenetic and gene expression changes in rat hippocampal neurons after Morris water maze training.Phosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation.Nickel compounds induce phosphorylation of histone H3 at serine 10 by activating JNK-MAPK pathway.Phosphorylation of histone H3 is functionally linked to retinoic acid receptor beta promoter activationSensing core histone phosphorylation - a matter of perfect timing.Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3.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.Mitogen and stress activated kinases act co-operatively with CREB during the induction of human cytomegalovirus immediate-early gene expression from latency.Phosphorylation of histone H3 correlates with transcriptionally active lociProtein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster.Hypoxia-induced and stress-specific changes in chromatin structure and function.The Ras-MAPK signal transduction pathway, cancer and chromatin remodeling.Inducible covalent posttranslational modification of histone H3.JIL-1, a chromosomal kinase implicated in regulation of chromatin structure, associates with the male specific lethal (MSL) dosage compensation complex.Histone H3 phosphorylation - a versatile chromatin modification for different occasions.Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells.14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activationHistone H3 tails containing dimethylated lysine and adjacent phosphorylated serine modifications adopt a specific conformation during mitosis and meiosis.Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena.Exposure to estrogen and ionizing radiation causes epigenetic dysregulation, activation of mitogen-activated protein kinase pathways, and genome instability in the mammary gland of ACI rats.Histone H3 phosphorylation, immediate-early gene expression, and the nucleosomal response: a historical perspective.Computational and experimental methods to decipher the epigenetic codeBeyond transcription factors: how oncogenic signalling reshapes the epigenetic landscape.Elucidating combinatorial histone modifications and crosstalks by coupling histone-modifying enzyme with biotin ligase activity.Cooperation between phosphorylation and acetylation processes in transcriptional control.Activation of the mouse histone deacetylase 1 gene by cooperative histone phosphorylation and acetylation.cAMP-response element-binding protein (CREB) controls MSK1-mediated phosphorylation of histone H3 at the c-fos promoter in vitro.Cascade of distinct histone modifications during collagenase gene activation.
P2860
Q24322623-A3DDC323-98FD-46C2-A270-B587F7691428Q24644935-EA1B0464-5920-4ECB-88CA-17C8265D8ADEQ24814990-735EF7C8-A4C4-4F84-AECE-39647BFFE339Q26778780-918C218D-54A4-4498-855A-CB1AD8445678Q26781247-2392BE58-00E4-4F7E-902D-88AF03ECB3FAQ28083715-922B4F09-603B-494E-A375-ABC780F2681DQ28363102-CC956851-3A54-41DC-B406-B737EB8338A9Q28593817-C35A159F-E71F-4745-A662-B941390D193DQ28660713-82FF3833-DA21-4677-8ED2-4FC61C7EE7FDQ29617236-EFE68957-5B97-4293-B824-DACB47D8C32CQ30449899-BEFE40FE-AC0D-45D3-8731-A1A660EDC812Q30654504-B6A80899-036A-4F97-8873-2EA5F7A0EE74Q30671436-2DA8575B-1F31-4D2A-BC12-23DEF884AA13Q33693529-18890DFF-7853-42A0-A53F-B8EFA22BC1F8Q33757737-94E0DF65-33BA-4C23-A5C6-FEE98917275EQ33920071-F2B4DE2B-FE9E-45CF-A993-85487B6294B0Q33947096-DFED2FF9-BB71-4EFD-8679-0645AFE93B7DQ35126559-516CC247-0030-4F24-9A2D-98A7A14F97A5Q35163934-EF8C6BCC-C619-4D19-A286-EADF8B6CC78EQ35191037-5ACA41F3-0694-449C-B4AA-E7BFEF93CA42Q35208366-692DF78F-936C-4F64-A1F7-A6CBA0E44171Q35661433-60472BB0-C2B7-4A3D-9F67-5547D2B55209Q35901931-031D7450-9215-40D0-829B-639A76C3CE68Q36061535-C204ADCE-5795-445B-B63E-F326935D6A4AQ36108372-1DE04CF4-D3D6-4791-B50C-6C580930930BQ36327550-44308B76-2C11-4B4B-9715-8F3E68DD1CC4Q36345651-DD94A032-30C9-475A-AAC9-76E2395C1508Q36380877-24D0F869-3305-4D50-A3D1-BADE7920B076Q36392006-99E86D58-53F7-4471-9B17-CE5A421C0356Q36483487-126C5143-5D9E-4F4B-805B-CC9443328BF4Q36492308-37FD476C-DE7D-4546-BA1F-762D2A22F2B7Q37092668-58DA60D7-4830-45BC-AD42-79A5ACA852DFQ37976424-3DD07FF1-DA08-42DC-B9C5-F7831E13B05CQ38258085-BD28E2D3-0DD6-4B54-B9FE-3C2222B68C0AQ38843250-F06AA0C3-A0EC-4932-9C4F-BFC97A18372EQ39222596-F98D2C71-279A-4036-B3A3-465257039D4DQ39445547-5E5D6017-A925-47EA-8818-57546920CD0EQ39677863-ECE063ED-131A-499A-A0EF-2DE74F520831Q39737970-66B0B54B-DF77-4DDE-BB74-6EB9BEB36A1DQ39740383-30B79951-FC54-4F23-A610-5511937732A0
P2860
Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
name
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@ast
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@en
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@nl
type
label
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@ast
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@en
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@nl
prefLabel
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@ast
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@en
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@nl
P2093
P2860
P356
P1476
Mitogen-stimulated phosphoryla ...... acetylation-sensitive fraction
@en
P2093
C A Hazzalin
L C Mahadevan
M J Barratt
P2860
P304
P356
10.1073/PNAS.91.11.4781
P407
P577
1994-05-24T00:00:00Z