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Title
Enhanced processivity of Dnmt1 by monoubiquitinated histone H3
Authors
Keywords
-
Journal
GENES TO CELLS
Volume 25, Issue 1, Pages 22-32
Publisher
Wiley
Online
2019-11-04
DOI
10.1111/gtc.12732
References
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Related references
Note: Only part of the references are listed.- Structural and mechanistic insights into UHRF1-mediated DNMT1 activation in the maintenance DNA methylation
- (2018) Tao Li et al. NUCLEIC ACIDS RESEARCH
- Critical Role of the UBL Domain in Stimulating the E3 Ubiquitin Ligase Activity of UHRF1 toward Chromatin
- (2018) Benjamin M. Foster et al. MOLECULAR CELL
- Stella safeguards the oocyte methylome by preventing de novo methylation mediated by DNMT1
- (2018) Yingfeng Li et al. NATURE
- RFTS-dependent negative regulation of Dnmt1 by nucleosome structure and histone tails
- (2017) Yuichi Mishima et al. FEBS Journal
- DNMT1 mutations found in HSANIE patients affect interaction with UHRF1 and neuronal differentiation
- (2017) Martha Smets et al. HUMAN MOLECULAR GENETICS
- Synthesis of ubiquitylated histone H3 using a thiirane linker for chemical ligation
- (2017) Toru Kawakami et al. JOURNAL OF PEPTIDE SCIENCE
- Structure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance
- (2017) Satoshi Ishiyama et al. MOLECULAR CELL
- Usp7-dependent histone H3 deubiquitylation regulates maintenance of DNA methylation
- (2017) Luna Yamaguchi et al. Scientific Reports
- Identification of a methylation profile for DNMT1-associated autosomal dominant cerebellar ataxia, deafness, and narcolepsy
- (2016) Kristin D. Kernohan et al. Clinical Epigenetics
- DNA methylation requires a DNMT1 ubiquitin interacting motif (UIM) and histone ubiquitination
- (2015) Weihua Qin et al. CELL RESEARCH
- Regulation of maintenance DNA methylation via histone ubiquitylation
- (2015) Atsuya Nishiyama et al. JOURNAL OF BIOCHEMISTRY
- Crystal Structure of Human DNA Methyltransferase 1
- (2015) Zhi-Min Zhang et al. JOURNAL OF MOLECULAR BIOLOGY
- Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation
- (2015) Jingdong Cheng et al. Nature Communications
- Dual Functions of the RFTS Domain of Dnmt1 in Replication-Coupled DNA Methylation and in Protection of the Genome from Aberrant Methylation
- (2015) Ronald Garingalao Garvilles et al. PLoS One
- The UHRF1 Protein Stimulates the Activity and Specificity of the Maintenance DNA Methyltransferase DNMT1 by an Allosteric Mechanism
- (2013) Pavel Bashtrykov et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The DNA Methyltransferase Dnmt1 Directly Interacts with the SET and RING Finger-associated (SRA) Domain of the Multifunctional Protein Uhrf1 to Facilitate Accession of the Catalytic Center to Hemi-methylated DNA
- (2013) Ahmet Can Berkyurek et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Uhrf1-dependent H3K23 ubiquitylation couples maintenance DNA methylation and replication
- (2013) Atsuya Nishiyama et al. NATURE
- DNMT1-interacting RNAs block gene-specific DNA methylation
- (2013) Annalisa Di Ruscio et al. NATURE
- Mutations in DNMT1 cause autosomal dominant cerebellar ataxia, deafness and narcolepsy
- (2012) Juliane Winkelmann et al. HUMAN MOLECULAR GENETICS
- Functions of DNA methylation: islands, start sites, gene bodies and beyond
- (2012) Peter A. Jones NATURE REVIEWS GENETICS
- Structure-Based Mechanistic Insights into DNMT1-Mediated Maintenance DNA Methylation
- (2012) J. Song et al. SCIENCE
- Mutations in DNMT1 cause hereditary sensory neuropathy with dementia and hearing loss
- (2011) Christopher J Klein et al. NATURE GENETICS
- Structural insight into maintenance methylation by mouse DNA methyltransferase 1 (Dnmt1)
- (2011) K. Takeshita et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Cyclin-dependent kinase-like 5 binds and phosphorylates DNA methyltransferase 1
- (2008) Isamu Kameshita et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
- (2008) Kyohei Arita et al. NATURE
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