SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity. - Wikidata - wikimedia - TriplyDB

SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.

SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.

http://www.wikidata.org/entity/Q33809955

about

DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger The current state of eukaryotic DNA base damage and repair Base Excision Repair, a Pathway Regulated by Posttranslational Modifications SUMO-mediated regulation of DNA damage repair and responses A germline polymorphism of thymine DNA glycosylase induces genomic instability and cellular transformation A TDG/CBP/RARα ternary complex mediates the retinoic acid-dependent expression of DNA methylation-sensitive genes SUMO-1 possesses DNA binding activity.Thymine DNA glycosylase is a CRL4Cdt2 substrate.E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex.Recent advances in the structural mechanisms of DNA glycosylases The SUMO pathway promotes basic helix-loop-helix proneural factor activity via a direct effect on the Zn finger protein senseless SUMO-conjugating enzyme E2 UBC9 mediates viral immediate-early protein SUMOylation in crayfish to facilitate reproduction of white spot syndrome virus.Characterizing Requirements for Small Ubiquitin-like Modifier (SUMO) Modification and Binding on Base Excision Repair Activity of Thymine-DNA Glycosylase in Vivo Thymine DNA glycosylase is a positive regulator of Wnt signaling in colorectal cancer.The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks.Monitoring regulation of DNA repair activities of cultured cells in-gel using the comet assay.SUMO-regulated transcription: challenging the dogma.Functions of SUMO in the Maintenance of Genome Stability.Sumoylation as an Integral Mechanism in Bacterial Infection and Disease Progression.Regulation of DNA demethylation by the XPC DNA repair complex in somatic and pluripotent stem cells.A click-and-release pyrrolysine analogue.SUMOylation of TDG with SUMO1 Identification of SUMO modification sites in the base excision repair protein, Ntg1.SUMO, a small, but powerful, regulator of double-strand break repair.Defining the impact of sumoylation on substrate binding and catalysis by thymine DNA glycosylase.

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P2860

SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.

http://www.wikidata.org/entity/Q33809955

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@ast

SUMO-1 regulates the conformat ...... with its DNA binding activity.

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type

label

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@ast

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@en

prefLabel

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@ast

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@en

P1433

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P1433

BMC Biochemistry

P1476

SUMO-1 regulates the conformat ...... with its DNA binding activity.

@en

P2093

Arndt Benecke

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

Hélène Léger

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

Sebastian Eilebrecht

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

P2860

Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells

The alpha/beta fold uracil DNA glycosylases: a common origin with diverse fates

T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif.

Crystal structure of a thwarted mismatch glycosylase DNA repair complex

Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition

MOLMOL: a program for display and analysis of macromolecular structures

T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha

Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription

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4

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scholarly article

P356

10.1186/1471-2091-12-4

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12

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P50

Jean-Michel Wieruszeski

Sebastian Eilebrecht

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2011-02-01T00:00:00Z

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49801781

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1030443568

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21284855

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3040724

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