Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/18960
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dc.contributor.authorGupta, A-
dc.contributor.authorAnjomani-Virmouni, S-
dc.contributor.authorKoundouros, N-
dc.contributor.authorPoulogiannis, G-
dc.date.accessioned2019-08-15T14:09:58Z-
dc.date.available2017-05-19-
dc.date.available2019-08-15T14:09:58Z-
dc.date.issued2017-05-19-
dc.identifier.citationMolecular and Cellular Oncology, 2017, 4 (6), pp. 1 - 2en_US
dc.identifier.issn2372-3556-
dc.identifier.issnhttp://dx.doi.org/10.1080/23723556.2017.1329692-
dc.identifier.urihttp://bura.brunel.ac.uk/handle/2438/18960-
dc.description.abstractCancer and Parkinson disease (PD) derive from distinct alterations in cellular processes, yet there are pathogenic mutations that are unequivocally linked to both diseases. Here we expand on our recent findings that loss of parkin RBR E3 ubiquitin protein ligase (PRKN, best known as PARK2)—which is genetically linked to PD—promotes cancer progression via redox-mediated inactivation of phosphatase and tensin homolog (PTEN) by S-nitrosylation.en_US
dc.description.sponsorshipInstitute of Cancer Research, Londonen_US
dc.format.extent1 - 2-
dc.language.isoenen_US
dc.publisherTaylor & Francisen_US
dc.subjectCanceren_US
dc.subjectNitrosative stressen_US
dc.subjectPARK2en_US
dc.subjectPTENen_US
dc.subjectS-nitrosylationen_US
dc.titlePARK2 loss promotes cancer progression via redox-mediated inactivation of PTENen_US
dc.typeArticleen_US
dc.identifier.doihttp://dx.doi.org/10.1080/23723556.2017.1329692-
dc.relation.isPartOfMolecular and Cellular Oncology-
pubs.issue6-
pubs.publication-statusPublished-
pubs.volume4-
Appears in Collections:Dept of Life Sciences Research Papers

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