Please use this identifier to cite or link to this item:
https://doi.org/10.1038/367040a0
DC Field | Value | |
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dc.title | A brain serine/threonine protein kinase activated by Cdc42 and Rac1 | |
dc.contributor.author | Manser, E. | |
dc.contributor.author | Leung, T. | |
dc.contributor.author | Salihuddin, H. | |
dc.contributor.author | Zhao, Z.-S. | |
dc.contributor.author | Lim, L. | |
dc.date.accessioned | 2014-12-12T07:29:21Z | |
dc.date.available | 2014-12-12T07:29:21Z | |
dc.date.issued | 1994-01-06 | |
dc.identifier.citation | Manser, E., Leung, T., Salihuddin, H., Zhao, Z.-S., Lim, L. (1994-01-06). A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367 (6458) : 40-46. ScholarBank@NUS Repository. https://doi.org/10.1038/367040a0 | |
dc.identifier.issn | 00280836 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/115554 | |
dc.description.abstract | A new brain serine/threonine protein kinase may be a target for the p21(ras)-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. The kinase complexes specifically with activated (GTP-bound) p21, inhibiting p21 GTPase activity and leading to kinase autophosphorylation and activation. Autophosphorylated kinase has a decreased affinity for Cdc42/Rac, freeing the p21 for further stimulatory activities or downregulation by GTPase-activating proteins. This bimolecular interaction provides a model for studying p21 regulation of mammalian phosphorylation signalling pathways. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/367040a0 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1038/367040a0 | |
dc.description.sourcetitle | Nature | |
dc.description.volume | 367 | |
dc.description.issue | 6458 | |
dc.description.page | 40-46 | |
dc.description.coden | NATUA | |
dc.identifier.isiut | A1994MP86500051 | |
Appears in Collections: | Staff Publications |
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