dc.contributor.author | Ding, Y | |
dc.contributor.author | Dale, T | |
dc.date.accessioned | 2018-09-17T15:16:57Z | |
dc.date.issued | 2002 | |
dc.identifier | 7 | |
dc.identifier.citation | Trends in Biochemical Sciences, 2002, 27 pp. 327 - 329 | |
dc.identifier.issn | 0968-0004 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/2740 | |
dc.identifier.doi | 10.1016/S0968-0004(02)02137-0 | |
dc.description.abstract | The control of β-catenin levels is vital to the cell. The primary means of regulation is through ubiquitin-mediated degradation. This process is regulated by Wnt signalling and is frequently disrupted in cancer. Three recent papers show that the initial step in marking β-catenin for degradation involves phosphorylation by casein kinase 1. This then allows phosphorylation by glycogen synthase kinase-3, and the recruitment of ubiquitin-ligase components. | |
dc.format.extent | 327 - 329 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.title | Wnt signal transduction: kinase cogs in a nano-machine? | |
dc.type | Journal Article | |
rioxxterms.versionofrecord | 10.1016/S0968-0004(02)02137-0 | |
rioxxterms.licenseref.startdate | 2002 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Trends in Biochemical Sciences | |
pubs.notes | keywords: Wnt signaling, B-catenin, kinases, in brief ribozymes, apolipoproein, blycobioloby | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR | |
pubs.volume | 27 | |
pubs.embargo.terms | Not known | |
dc.contributor.icrauthor | Dale, Trevor | en |