UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail
about
The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia proteinNIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscapeRecognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1Dual Binding of Chromomethylase Domains to H3K9me2-Containing Nucleosomes Directs DNA Methylation in PlantsThe PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5BConserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1PHF13 is a molecular reader and transcriptional co-regulator of H3K4me2/3Dissecting the precise role of H3K9 methylation in crosstalk with DNA maintenance methylation in mammals.Topoisomerase II regulates the maintenance of DNA methylation.DNA hypomethylation induces a DNA replication-associated cell cycle arrest to block hepatic outgrowth in uhrf1 mutant zebrafish embryosA phylogenetic study of SPBP and RAI1: evolutionary conservation of chromatin binding modules.H3K9 methyltransferase G9a negatively regulates UHRF1 transcription during leukemia cell differentiationThe role of histone demethylase KDM4B in Myc signaling in neuroblastomaAn Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1.Multidimensional Proteomics Reveals a Role of UHRF2 in the Regulation of Epithelial-Mesenchymal Transition (EMT).Uhrf1 controls the self-renewal versus differentiation of hematopoietic stem cells by epigenetically regulating the cell-division modes.Systematic analysis of histone modification readout.Mind the methyl: methyllysine binding proteins in epigenetic regulation.Structural basis of molecular recognition of helical histone H3 tail by PHD finger domains.A Structural Perspective on Readout of Epigenetic Histone and DNA Methylation Marks.DNA methylation requires a DNMT1 ubiquitin interacting motif (UIM) and histone ubiquitinationHistone demethylase KDM5A is regulated by its reader domain through a positive-feedback mechanism.UHRF1 is a sensor for DNA interstrand crosslinks and recruits FANCD2 to initiate the Fanconi anemia pathway.The UHRF1 protein stimulates the activity and specificity of the maintenance DNA methyltransferase DNMT1 by an allosteric mechanism.Conformational dynamics of the TTD-PHD histone reader module of the UHRF1 epigenetic regulator reveals multiple histone-binding states, allosteric regulation, and druggability.Characteristics of a PHD Finger Subtype.An Intramolecular Interaction of UHRF1 Reveals Dual Control for Its Histone Association.Structural and mechanistic insights into UHRF1-mediated DNMT1 activation in the maintenance DNA methylation.Targeting the SET and RING-associated (SRA) domain of ubiquitin-like, PHD and ring finger-containing 1 (UHRF1) for anti-cancer drug development.Critical Role of the UBL Domain in Stimulating the E3 Ubiquitin Ligase Activity of UHRF1 toward Chromatin
P2860
Q24297944-2C446A2D-F113-4D6F-B4D2-CFAE89420C17Q26851503-0C19034F-B8A8-4DE0-ABA3-FCF158010D16Q27670916-DC4A59A8-5272-4A43-BB96-801CCE149658Q27673732-E4F6C05E-456C-4F5B-BEFA-FCC0CC354001Q27684424-6353B695-AF60-4C1A-92E6-94604CFB18F0Q28082738-B57FAAAD-414C-459B-A1A6-5E40463183D9Q28829506-4F81E890-4145-460E-9397-614D4E9515ADQ33663034-AA72966B-5210-44E2-8A60-8C437DCE58A8Q34958800-9F4545A4-4983-49E0-B9B2-90409AA0297BQ34999653-0FE561DF-7798-4BF8-A38A-B1B1C66BFEADQ35036841-F8421E15-00A2-4360-BA3C-B190A3B98D6FQ35476312-7365BBBC-CCFD-425D-B695-C58C343555FFQ36014044-C8ADD5AF-A209-44CC-86D6-51CAF944CF4EQ36021816-0A951AEB-AC99-43F2-BC53-FC56717F26BAQ37076868-6C2A758D-EE63-4BE4-90A4-9155FF647054Q37589996-353D3778-DC88-4B51-A438-FB72F350942FQ38065114-C7D00F43-F9D2-4268-B23C-7807580B55AAQ38180674-99BBF781-739B-4440-ADB3-F179153BA009Q38288565-B05D1E10-9F02-4F67-BC49-DFA38F8587EBQ38756663-2991D2D1-038F-40C7-A1B9-301E72B99BD9Q38865045-F95683B8-C270-43ED-AF3F-5FE1859BA3AAQ38909037-EA7A718C-AF2D-4FEB-ADFA-9FE7F293EC2AQ39254333-0DD3DEE1-E175-426A-80C0-B1626787AED3Q41954787-54F28187-F111-4EE1-904E-93D185516ABCQ47103361-7F2C250E-5E29-40B0-8C02-86BD31F765E2Q47281158-8C0FE6AB-B7FE-4965-BAD4-23510ABD2523Q50207902-4E9109BE-1A02-4344-AAEE-D7930B0A659FQ52374663-882B0073-BA7F-41D7-B64E-9C936EA8D88AQ55129550-8EA812A5-9EF8-4F23-91D1-440798885984Q58560680-5698A63D-BFC6-424A-9708-41AF4454C61A
P2860
UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@ast
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@en
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@nl
type
label
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@ast
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@en
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@nl
prefLabel
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@ast
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@en
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@nl
P3181
P1476
UHRF1 double tudor domain and ...... me3-containing histone H3 tail
@en
P2093
P304
P3181
P356
10.1016/J.JMB.2011.11.012
P407
P577
2011-11-12T00:00:00Z