A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
about
Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolutionInteractions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID FamiliesHuman SMC5/6 complex promotes sister chromatid homologous recombination by recruiting the SMC1/3 cohesin complex to double-strand breaksIdentification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complexThe SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteinsHuman MMS21/NSE2 is a SUMO ligase required for DNA repairHistone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modificationsSUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair.Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modificationsStructure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNASUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiaeReplication-Associated Recombinational Repair: Lessons from Budding YeastFunctions of Ubiquitin and SUMO in DNA Replication and Replication StressStructural Insights into Ring Formation of Cohesin and Related Smc ComplexesCooperativity of the SUMO and Ubiquitin Pathways in Genome StabilityCrosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repairSUMOylation in control of accurate chromosome segregation during mitosisSmc5/6 coordinates formation and resolution of joint molecules with chromosome morphology to ensure meiotic divisionsStructural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 ComplexMechanisms, regulation and consequences of protein SUMOylationRequirement of Nse1, a subunit of the Smc5-Smc6 complex, for Rad52-dependent postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae.SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase IISUMOylation regulates the SNF1 protein kinase.Interplay between the Smc5/6 complex and the Mph1 helicase in recombinational repairSumoylation and the structural maintenance of chromosomes (Smc) 5/6 complex slow senescence through recombination intermediate resolution.PolySUMOylation by Siz2 and Mms21 triggers relocation of DNA breaks to nuclear pores through the Slx5/Slx8 STUbL.Sumoylation regulates Kap114-mediated nuclear transportDeficient sumoylation of yeast 2-micron plasmid proteins Rep1 and Rep2 associated with their loss from the plasmid-partitioning locus and impaired plasmid inheritance.Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles.End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1.Regulation of repair choice: Cdk1 suppresses recruitment of end joining factors at DNA breaks.Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangementsNucleoporins prevent DNA damage accumulation by modulating Ulp1-dependent sumoylation processesThe SUMO E3 ligase Siz2 exerts a locus-dependent effect on gene silencing in Saccharomyces cerevisiaeScc1 sumoylation by Mms21 promotes sister chromatid recombination through counteracting WaplYeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory domainsCooperation of sumoylated chromosomal proteins in rDNA maintenanceCharacterisation of the SUMO-like domains of Schizosaccharomyces pombe Rad60The SUMO isopeptidase Ulp2p is required to prevent recombination-induced chromosome segregation lethality following DNA replication stressA Chemical and Enzymatic Approach to Study Site-Specific Sumoylation
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P248
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P2860
A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
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2005 թվականի մարտին հրատարակված գիտական հոդված
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2005年の論文
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2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
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name
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@ast
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@en
A SUMO ligase is part of a nuc ...... and chromosomal organization.
@nl
type
label
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@ast
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@en
A SUMO ligase is part of a nuc ...... and chromosomal organization.
@nl
altLabel
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@en
prefLabel
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@ast
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@en
A SUMO ligase is part of a nuc ...... and chromosomal organization.
@nl
P2860
P3181
P356
P1476
A SUMO ligase is part of a nuc ...... r and chromosomal organization
@en
P2093
Xiaolan Zhao
P2860
P304
P3181
P356
10.1073/PNAS.0500537102
P407
P577
2005-03-29T00:00:00Z