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Proteomic dissection of DNA polymerization

dc.contributor.authorBeck, Jennifer
dc.contributor.authorUrathamakul, Thitima
dc.contributor.authorWatt, Stephen J
dc.contributor.authorSheil, Margaret
dc.contributor.authorSchaeffer, Patrick
dc.contributor.authorDixon, Nicholas
dc.date.accessioned2015-12-13T22:57:57Z
dc.date.issued2006
dc.date.updated2015-12-12T07:19:54Z
dc.description.abstractDNA polymerases replicate the genome by associating with a range of other proteins that enable rapid, high-fidelity copying of DNA. This complex of proteins and nucleic acids is termed the replisome. Proteins of the replisome must interact with other networks of proteins, such as those involved in DNA repair. Many of the proteins involved in DNA polymerization and the accessory proteins are known, but the array of proteins they interact with, and the spatial and temporal arrangement of these interactions, are current research topics. Mass spectrometry is a technique that can be used to identify the sites of these interactions and to determine the precise stoichiometries of binding partners in a functional complex. A complete understanding of the macromolecular interactions involved in DNA replication and repair may lead to discovery of new targets for antibiotics against bacteria and biomarkers for diagnosis of diseases, such as cancer, in humans.
dc.identifier.issn1478-9450
dc.identifier.urihttp://hdl.handle.net/1885/83210
dc.publisherFuture Drugs Ltd
dc.sourceFuture Drugs: Expert Review Proteomics
dc.subjectKeywords: DNA; recombinant DNA; chromosome replication; DNA damage; DNA repair; electrospray mass spectrometry; macromolecule; mass spectrometry; polymerization; protein binding; protein cross linking; protein microarray; protein protein interaction; proteomics; re DNA polymerase; DNA repair; DNA replication; Electrospray ionization; Mass spectrometry; Molecular machine; Protein-protein complex; Replisome; TAP tag
dc.titleProteomic dissection of DNA polymerization
dc.typeJournal article
local.bibliographicCitation.issue2
local.bibliographicCitation.lastpage211
local.bibliographicCitation.startpage197
local.contributor.affiliationBeck, Jennifer, University of Wollongong
local.contributor.affiliationUrathamakul, Thitima, University of Wollongong
local.contributor.affiliationWatt, Stephen J, University of Wollongong
local.contributor.affiliationSheil, Margaret, University of Wollongong
local.contributor.affiliationSchaeffer, Patrick, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationDixon, Nicholas, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidSchaeffer, Patrick, u4047597
local.contributor.authoruidDixon, Nicholas, u8102891
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.ariespublicationMigratedxPub11434
local.identifier.citationvolume3
local.identifier.doi10.1586/14789450.3.2.197
local.identifier.scopusID2-s2.0-33745590415
local.type.statusPublished Version

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