rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2009-4-3
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pubmed:abstractText |
Maintaining genomic stability is critical for the prevention of disease. Numerous DNA repair pathways help to maintain genomic stability by correcting potentially lethal or disease-causing lesions to our genomes. Mounting evidence suggests that the post-translational modification sumoylation plays an important regulatory role in several aspects of DNA repair. The E3 SUMO ligase MMS21/NSE2 has gained increasing attention for its function in homologous recombination (HR), an error-free DNA repair pathway that mediates repair of double-strand breaks (DSBs) using the sister chromatid as a repair template. MMS21/NSE2 is part of the SMC5/6 complex, which has been shown to facilitate DSB repair, collapsed replication fork restart, and telomere elongation by HR. Here, I review the function of the SMC5/6 complex and its associated MMS21/NSE2 SUMO ligase activity in homologous recombination.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/NSMCE2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMC5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMC6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1568-7864
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-506
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pubmed:meshHeading |
pubmed-meshheading:19217832-Cell Cycle Proteins,
pubmed-meshheading:19217832-Chromatin,
pubmed-meshheading:19217832-DNA,
pubmed-meshheading:19217832-DNA Breaks, Double-Stranded,
pubmed-meshheading:19217832-DNA Repair,
pubmed-meshheading:19217832-Genomic Instability,
pubmed-meshheading:19217832-Humans,
pubmed-meshheading:19217832-Ligases,
pubmed-meshheading:19217832-Protein Processing, Post-Translational,
pubmed-meshheading:19217832-Recombination, Genetic,
pubmed-meshheading:19217832-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:19217832-Telomere,
pubmed-meshheading:19217832-Ubiquitin-Protein Ligase Complexes
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pubmed:year |
2009
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pubmed:articleTitle |
The Yin and Yang of the MMS21-SMC5/6 SUMO ligase complex in homologous recombination.
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pubmed:affiliation |
Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX 75390-9038, United States. Ryan.Potts@UTSouthwestern.edu
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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