Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance.

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Critical Role of the UBL Domain in Stimulating the E3 Ubiquitin Ligase Activity of UHRF1 toward Chromatin Chromatin structure and its chemical modifications regulate the ubiquitin ligase substrate selectivity of UHRF1

P2860

Q58560680-1F1F8EC9-0F09-4254-B40D-B281AFCD62D6 Q58784398-4C71CF7D-5D47-4C71-9AE8-FE637E954D41

P2860

Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance.

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http://www.wikidata.org/entity/Q52673715

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

@wuu

2018年学术文章

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2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Comparative biochemical analys ...... m DNA methylation maintenance.

@en

Comparative biochemical analys ...... m DNA methylation maintenance.

@nl

type

Item

label

Comparative biochemical analys ...... m DNA methylation maintenance.

@en

Comparative biochemical analys ...... m DNA methylation maintenance.

@nl

prefLabel

Comparative biochemical analys ...... m DNA methylation maintenance.

@en

Comparative biochemical analys ...... m DNA methylation maintenance.

@nl

P1476

Comparative biochemical analys ...... m DNA methylation maintenance.

@en

P2093

Bradley M Dickson

http://www.w3.org/2001/XMLSchema#string

Brian Kuhlman

http://www.w3.org/2001/XMLSchema#string

Evan M Cornett

http://www.w3.org/2001/XMLSchema#string

P2860

Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein

NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein

PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression

UHRF1 plays a role in maintaining DNA methylation in mammalian cells

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1

Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism

Structure and Hemimethylated CpG Binding of the SRA Domain from Human UHRF1

Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1

Crystal structure of PHD domain of UHRF1 and insights into recognition of unmodified histone H3 arginine residue 2

P304

4405-4416

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/NAR/GKY151

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Joseph S. Harrison

Robert M Vaughan

Scott B Rothbart

P577

2018-05-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29506131

http://www.w3.org/2001/XMLSchema#string

P921

DNA methylation

P932

5961305

http://www.w3.org/2001/XMLSchema#string

Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance.

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P2860

P2860

Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance.

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932