about
Novel Histone H3 Binding Protein ORF158L from the Singapore Grouper IridovirusSet2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes.The histone H3K36 demethylase Rph1/KDM4 regulates the expression of the photoreactivation gene PHR1SWI/SNF and Asf1 independently promote derepression of the DNA damage response genes under conditions of replication stressSingle cell analysis of RNA-mediated histone H3.3 recruitment to a cytomegalovirus promoter-regulated transcription site.Elongator complex influences telomeric gene silencing and DNA damage response by its role in wobble uridine tRNA modification.Promoter regulation by distinct mechanisms of functional interplay between lysine acetylase Rtt109 and histone chaperone Asf1Balancing acts of SRI and an auto-inhibitory domain specify Set2 function at transcribed chromatin.Dissecting the roles of the histone chaperones reveals the evolutionary conserved mechanism of transcription-coupled deposition of H3.3.Histone H3K36 trimethylation is essential for multiple silencing mechanisms in fission yeast.Set2 mediated H3 lysine 36 methylation: regulation of transcription elongation and implications in organismal development.Understanding the language of Lys36 methylation at histone H3.The determinants of alternative RNA splicing in human cells.Shaping the cellular landscape with Set2/SETD2 methylation.Modulation of gene expression dynamics by co-transcriptional histone methylations.Transcriptional regulation by Asf1: new mechanistic insights from studies of the DNA damage response to replication stress.Inositol phosphate kinase Vip1p interacts with histone chaperone Asf1p in Saccharomyces cerevisiae.
P2860
Q27670607-CF963C78-2509-429F-BC16-9BC298E8CDA5Q27929868-A7564C74-1474-4C46-BBF2-937C027E9C2FQ27930846-FCF0274B-9F4D-40E7-908D-C03153855577Q28478777-9CE6C42D-1E0F-409D-A1B4-B89AD70F1622Q30541321-EBF9AF31-D728-40DF-99E6-0C331E0D95EAQ34017522-FE1C9286-C182-499E-B70D-43B352461BD1Q35621349-EB010669-FF96-46E7-9050-245242415D2DQ35656826-5C04F037-0F6C-4278-A6F6-4238D1775D39Q36878418-A7FE43C8-4383-4F83-9C9C-510E33D34E34Q36914566-86C01E35-CC83-43C7-A42A-41BFC5EC96BFQ37158054-B8AD5146-AC63-4B0E-96F5-CE5AC8F6DED3Q37672319-4A29979A-7BF0-4E55-8A0C-2382CEF954E7Q38679766-067273CA-B322-457C-AEDF-8ABCC3C7A6EDQ39225775-118D11AE-6EF2-4C1E-80EA-1AAE38F20CC4Q39268159-68CEE1EB-A077-4D57-BB40-D3B4DC98F077Q42021677-C100EBB1-F5FD-49E9-A55D-AFC65190333FQ54543841-BAEC1FE1-F44D-47F5-81F6-94703CB7F27C
P2860
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Asf1 can promote trimethylation of H3 K36 by Set2.
@en
Asf1 can promote trimethylation of H3 K36 by Set2.
@nl
type
label
Asf1 can promote trimethylation of H3 K36 by Set2.
@en
Asf1 can promote trimethylation of H3 K36 by Set2.
@nl
prefLabel
Asf1 can promote trimethylation of H3 K36 by Set2.
@en
Asf1 can promote trimethylation of H3 K36 by Set2.
@nl
P2093
P2860
P356
P1476
Asf1 can promote trimethylation of H3 K36 by Set2.
@en
P2093
Gerald C Johnston
Laura V Minard
Ling-Ju Lin
Michael C Schultz
Richard A Singer
P2860
P304
P356
10.1128/MCB.01229-09
P407
P577
2010-01-04T00:00:00Z