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dc.contributor.authorLabib, Karim
dc.date.accessioned2009-04-23T16:59:40Z
dc.date.available2009-04-23T16:59:40Z
dc.date.issued2008-10-24
dc.identifier.citationMaking connections at DNA replication forks: Mrc1 takes the lead. 2008, 32 (2):166-8 Mol. Cellen
dc.identifier.issn1097-4164
dc.identifier.pmid18951084
dc.identifier.doi10.1016/j.molcel.2008.10.005
dc.identifier.urihttp://hdl.handle.net/10541/66077
dc.description.abstractIn a recent issue of Molecular Cell, Lou et al. (2008) demonstrate that the Mrc1 protein associates with the DNA polymerase that acts on the leading strand at replication forks, suggesting a potential mechanism that could help to preserve genome stability.
dc.language.isoenen
dc.subject.meshCell Cycle Proteins
dc.subject.meshDNA Helicases
dc.subject.meshDNA Polymerase II
dc.subject.meshDNA Replication
dc.subject.meshDNA, Fungal
dc.subject.meshPhosphorylation
dc.subject.meshSaccharomyces Cerevisiae
dc.subject.meshSaccharomyces Cerevisiae Proteins
dc.titleMaking connections at DNA replication forks: Mrc1 takes the lead.en
dc.typeArticleen
dc.contributor.departmentCancer Research UK, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalMolecular Cellen
html.description.abstractIn a recent issue of Molecular Cell, Lou et al. (2008) demonstrate that the Mrc1 protein associates with the DNA polymerase that acts on the leading strand at replication forks, suggesting a potential mechanism that could help to preserve genome stability.


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