about
Determination of enriched histone modifications in non-genic portions of the human genomeChromatin dynamics at DNA replication, transcription and repairWhat does our genome encode?Structure and catalytic mechanism of the human histone methyltransferase SET7/9Identification of novel functional TBP-binding sites and general factor repertoiresThe BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine 4 methyltransferase complexFailure of SOX9 regulation in 46XY disorders of sex development with SRY, SOX9 and SF1 mutationsRIP140 directs histone and DNA methylation to silence Ucp1 expression in white adipocytesHuman Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1Contribution of H3K4 methylation by SET-1A to interleukin-1-induced cyclooxygenase 2 and inducible nitric oxide synthase expression in human osteoarthritis chondrocytesMSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complexCoactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferasesThe human PAF complex coordinates transcription with events downstream of RNA synthesis.CENP-V is required for centromere organization, chromosome alignment and cytokinesis.CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genesHuman BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressorThe double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcriptionSolution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylationKnockdown of ALR (MLL2) reveals ALR target genes and leads to alterations in cell adhesion and growth.Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.Serum response factor binding sites differ in three human cell typesOn the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complexGlobal and Hox-specific roles for the MLL1 methyltransferaseThe tumor suppressor menin regulates hematopoiesis and myeloid transformation by influencing Hox gene expression.Centromeric chromatin exhibits a histone modification pattern that is distinct from both euchromatin and heterochromatinBtg2 enhances retinoic acid-induced differentiation by modulating histone H4 methylation and acetylationHistone modifications defining active genes persist after transcriptional and mitotic inactivationA silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatinVernalization, competence, and the epigenetic memory of winterImmunohistochemical Analysis of Histone H3 Modifications in Germ Cells during Mouse SpermatogenesisChromatin structure and gene expression programs of human embryonic and induced pluripotent stem cellsPioneer transcription factors: establishing competence for gene expressionEpigenetic alterations in agingHistone methylation regulates memory formation.Environmental studies of schizophrenia through the prism of epigeneticsIn vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferasesStructural basis for the product specificity of histone lysine methyltransferasesMicroplate-based chromatin immunoprecipitation method, Matrix ChIP: a platform to study signaling of complex genomic events
P2860
Q21283767-1A99A3CA-1A6F-4CF9-8931-0534DA7DD6F1Q22065678-77990BDB-F281-4EE1-8C1B-3C49720A9A92Q22065765-B6ADE55C-6114-438E-9188-E2BAF30891E1Q24293093-D827FE24-AD8D-4096-8039-CD5B97459FA8Q24295026-EBB417C8-B59B-4317-A2F9-4C2E0389A455Q24296996-DBCEE8EB-727D-4CF9-AE1E-93AD3E497314Q24297498-73E249CD-949E-4685-B8A7-E2542E566537Q24299066-03ABA9EC-CB4A-498B-8084-45D657A4B8D3Q24299067-1240B38D-5332-4B6D-9D93-14A5FD7F6C8BQ24300761-5F554483-F07C-45AC-ACD1-C6C4790D6549Q24303450-FB403986-6803-45B8-B442-6D069DF20E7DQ24305512-98BA05E4-8C51-43ED-A9E0-836FA155EA2BQ24305587-902AD9C3-9E5A-41C1-9388-734B17D6EE83Q24307917-227314EC-8D6B-4F2F-A3E7-6FB7AEAFE48CQ24310616-0B33C82E-7B7D-490C-B007-18DEB055563AQ24315938-3B1FA3E9-8D2D-4B3E-9AAA-6946D2BC8B4AQ24318682-712DACA3-10E7-428D-A86E-AC1C764173F5Q24319771-A7722BEB-84DE-4EDE-AB5E-82FC3B0F8B43Q24324008-EF1B4B75-3758-4019-A28D-D001C53D3BA4Q24336402-96A2BEF6-6919-49D1-B07D-70E0C0A48A11Q24337427-6F2C3C2A-C705-4BCF-AE7E-01AE23BC74E4Q24338285-DC1D3512-3EDB-4A0B-959A-4A9DEE782922Q24338662-2DF09B89-B8B9-4682-8ACB-6A25984B2F23Q24339403-F5AD2C68-3354-440A-B9C1-8DC6E7E2B113Q24529562-D84031A9-8C97-422E-BCE7-C70BDB9DB5E1Q24536084-8A3B6602-C2E4-406F-BC0B-78D87A1EDADEQ24537593-2E24996C-A541-4858-8798-0F694A6EB563Q24548977-1B92D153-C100-46F9-B580-371B967F8FA6Q24557457-B6086660-ECC5-4A00-9BEC-DCB502035504Q24561636-0BF250BC-13E1-4DD4-A863-C992D88A0A1AQ24564278-17155D7B-92DE-4952-B8E6-56ED33883DDAQ24601794-5693C887-390A-4633-9DD6-45FFEB1236C2Q24620932-230D47B2-A890-4D22-ABEB-48B0B33F2AD2Q24625373-4FBBC91F-99C1-4F24-B9C7-6E56BD112701Q24625376-AA90F5BC-B52F-400D-896E-5C851EBBABADQ24632499-E68B579D-67E8-4724-BFD3-0EF16DE6A13AQ24643547-2AADB775-61D2-4172-8903-04938CBE7B37Q24645737-EE2F94C3-0912-48CF-AD0B-DAED9C56B8FAQ24646957-1C8B3A80-D34F-41BB-A4CB-DFE8383B68B5Q24648362-C25AB4CF-2A3C-46AC-8CE3-69C3358022DB
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Active genes are tri-methylated at K4 of histone H3
@ast
Active genes are tri-methylated at K4 of histone H3
@en
type
label
Active genes are tri-methylated at K4 of histone H3
@ast
Active genes are tri-methylated at K4 of histone H3
@en
prefLabel
Active genes are tri-methylated at K4 of histone H3
@ast
Active genes are tri-methylated at K4 of histone H3
@en
P2093
P2860
P3181
P356
P1433
P1476
Active genes are tri-methylated at K4 of histone H3
@en
P2093
Bannister AJ
Bernstein BE
Kouzarides T
Santos-Rosa H
Schneider R
Schreiber SL
Sherriff J
P2860
P2888
P304
P3181
P356
10.1038/NATURE01080
P407
P577
2002-09-26T00:00:00Z
P6179
1005406259