Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jprot.2012.05.047
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dc.titleMolecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis
dc.contributor.authorMatsunaga, S.
dc.contributor.authorSawasaki, T.
dc.contributor.authorOde, H.
dc.contributor.authorMorishita, R.
dc.contributor.authorFurukawa, A.
dc.contributor.authorSakuma, R.
dc.contributor.authorSugiura, W.
dc.contributor.authorSato, H.
dc.contributor.authorKatahira, M.
dc.contributor.authorTakaori-Kondo, A.
dc.contributor.authorYamamoto, N.
dc.contributor.authorRyo, A.
dc.date.accessioned2016-09-06T08:19:14Z
dc.date.available2016-09-06T08:19:14Z
dc.date.issued2012-08-03
dc.identifier.citationMatsunaga, S., Sawasaki, T., Ode, H., Morishita, R., Furukawa, A., Sakuma, R., Sugiura, W., Sato, H., Katahira, M., Takaori-Kondo, A., Yamamoto, N., Ryo, A. (2012-08-03). Molecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis. Journal of Proteomics 75 (15) : 4863-4873. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jprot.2012.05.047
dc.identifier.issn18743919
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/126737
dc.description.abstractXenotropic murine leukemia virus-related virus (XMRV) is a virus generated under artificial conditions by the recombination of 2 murine leukemia virus (MLV) proviruses, PreXMRV-1 and PreXMRV-2, during the in vivo passage of human prostate cancer cells in athymic nude mice. The molecular etiology of XMRV infection has not been characterized and its implication in human prostate cancer progression remains equivocal. As a step toward resolving this issue we developed an in vitro enzymatic assay system to characterize XMRV protease (PR)-mediated cleavage of host-cell proteins. Enzymatically-active XMRV PR protein was synthesized using a wheat-germ cell-free system. By monitoring cleavage activity of XMRV PR by AlphaScreen and 2-color immunoblot analyses, we revealed that the catalytic activity of XMRV PR is selectively blocked by the HIV PR inhibitor, Amprenavir, and identified several human tumor suppressor proteins, including PTEN and BAX, to be substrates of XMRV PR. This system may provide an attractive means for analyzing the function of retrovirus proteases and provide a technology platform for drug screening. © 2012 Elsevier B.V.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jprot.2012.05.047
dc.sourceScopus
dc.subjectAlphaSceen
dc.subjectCell-free protein synthesis
dc.subjectProtease
dc.subjectXMRV
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/j.jprot.2012.05.047
dc.description.sourcetitleJournal of Proteomics
dc.description.volume75
dc.description.issue15
dc.description.page4863-4873
dc.identifier.isiut000307609500027
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