SUMO-1 conjugation to human DNA topoisomerase II isozymes - Test2 - elhamkhani - TriplyDB

SUMO-1 conjugation to human DNA topoisomerase II isozymes

SUMO-1 conjugation to human DNA topoisomerase II isozymes

http://www.wikidata.org/entity/Q28138899

about

Stabilization and activation of p53 by the coactivator protein TAFII31 Highlight: BRCA1 and BRCA2 proteins in breast cancer SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair.Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha SUMO-2/3 regulates topoisomerase II in mitosis Role of desumoylation in the development of prostate cancer Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates Topoisomerase II can unlink replicating DNA by precatenane removal Aberrant lamination in the cerebral cortex of mouse embryos lacking DNA topoisomerase IIbeta Alternate exon insertion controls selective ubiquitination and degradation of different AUF1 protein isoforms The SUMO pathway is required for selective degradation of DNA topoisomerase IIbeta induced by a catalytic inhibitor ICRF-193(1)RNA helicase A interacts with dsDNA and topoisomerase IIalpha Meiosis and small ubiquitin-related modifier (SUMO)-conjugating enzyme, Ubc9.The impact of the human DNA topoisomerase II C-terminal domain on activity.Identification and molecular properties of SUMO-binding proteins in Arabidopsis.Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxia SUMO: of branched proteins and nuclear bodies.A stress inducible SUMO conjugating enzyme gene (SaSce9) from a grass halophyte Spartina alterniflora enhances salinity and drought stress tolerance in Arabidopsis.Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport.Versatile protein tag, SUMO: its enzymology and biological function.Novel mechanism by which histone deacetylase inhibitors facilitate topoisomerase IIα degradation in hepatocellular carcinoma cells The topoisomerase IIbeta circular clamp arrests transcription and signals a 26S proteasome pathway All tangled up: how cells direct, manage and exploit topoisomerase function.SUMOylation of the C-terminal domain of DNA topoisomerase IIα regulates the centromeric localization of Claspin.A genome-wide RNAi screen identifies core components of the G₂-M DNA damage checkpoint.Analysis of SUMOylation of topoisomerase IIalpha with Xenopus egg extracts.SUMOylation of DNA topoisomerase IIα regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis.DNA topoisomerase IIα controls replication origin cluster licensing and firing time in Xenopus egg extracts Quality control of a transcriptional regulator by SUMO-targeted degradation SUMO modification of DNA topoisomerase II: trying to get a CENse of it all Ubiquitin-family modifications of topoisomerase I in camptothecin-treated human breast cancer cells.DNA topoisomerases: harnessing and constraining energy to govern chromosome topology.DNA topoisomerase II and its growing repertoire of biological functions.Targets and consequences of protein SUMOylation in neurons.Genome-wide ChIP-seq analysis of human TOP2B occupancy in MCF7 breast cancer epithelial cells.Non-SMC Element 2 (NSMCE2) of the SMC5/6 Complex Helps to Resolve Topological Stress.System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability.SUMOylation regulates AKT1 activity.Natural Compounds as Anticancer Agents Targeting DNA Topoisomerases.Conjugation of Smt3 to dorsal may potentiate the Drosophila immune response.

P2860

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P2860

SUMO-1 conjugation to human DNA topoisomerase II isozymes

http://www.wikidata.org/entity/Q28138899

description

2000 nî lūn-bûn

@nan

2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

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2000年论文

@wuu

name

SUMO-1 conjugation to human DNA topoisomerase II isozymes

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SUMO-1 conjugation to human DNA topoisomerase II isozymes

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SUMO-1 conjugation to human DNA topoisomerase II isozymes

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type

label

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@ast

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@en

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@nl

prefLabel

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@ast

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@en

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@nl

P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

SUMO-1 conjugation to human DNA topoisomerase II isozymes

@en

P2093

L F Liu

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

S D Desai

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

Y Mao

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

P2860

In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1

Differential regulation of sentrinized proteins by a novel sentrin-specific protease

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9

SUMO-1 modification activates the transcriptional response of p53

SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex

Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association

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26066-73

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P31

scholarly article

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4804656

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10.1074/JBC.M001831200

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P407

P433

34

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P478

275

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P577

2000-08-25T00:00:00Z

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P698

10862613

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