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Xuemin Wang
Researcher at University of Adelaide
Publications - 67
Citations - 6271
Xuemin Wang is an academic researcher from University of Adelaide. The author has contributed to research in topics: Phosphorylation & Eukaryotic initiation factor. The author has an hindex of 36, co-authored 67 publications receiving 5676 citations. Previous affiliations of Xuemin Wang include University of Dundee & University of British Columbia.
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Journal ArticleDOI
Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase
TL;DR: PDK1 is required for activation of members of the AGC kinase family; it is shown that two such kinases, p70 S6 kinase (regulated via mTOR) and p90RSK1 (activated by Erk) phosphorylate eEF2k at a conserved serine and inhibit its activity.
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The mTOR pathway in the control of protein synthesis.
Xuemin Wang,Christopher G. Proud +1 more
TL;DR: Signaling through mammalian target of rapamycin (mTOR) is activated by amino acids, insulin, and growth factors, and impaired by nutrient or energy deficiency.
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Amino acid availability regulates p70 S6 kinase and multiple translation factors.
TL;DR: The data show that amino acid supply regulates multiple translation factors in mammalian cells and indicates that protein kinase B may act upstream of p70 S6 kinase through a pathway independent of this enzyme.
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The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase.
Yvonne L. Woods,Philip Cohen,Walter Becker,Ross Jakes,Michel Goedert,Xuemin Wang,Christopher G. Proud +6 more
TL;DR: In this paper, the e-subunit of rat eukaryotic protein-synthesis initiation factor 2B (eIF2Be) was shown to be phosphorylated by two isoforms of dual-specificity tyrosine-phosphorylated and regulated kinase (DYRK2 and DYRK1A), but only weakly or not at all by other 'proline-directed' protein kinases tested.
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The Phosphorylation of Eukaryotic Initiation Factor eIF4E in Response to Phorbol Esters, Cell Stresses, and Cytokines Is Mediated by Distinct MAP Kinase Pathways
Xuemin Wang,Andrea Flynn,Andrew J. Waskiewicz,Benjamin L.J. Webb,Robert G.J. Vries,Ian A. Baines,Jonathan A. Cooper,Christopher G. Proud +7 more
TL;DR: It is shown, using specific inhibitors, that this involves both the p38 mitogen-activated protein (MAP) kinase and Erk signaling pathways, and that this blocks the phosphorylation of eIF4E by Mnk1 in vitro, which may explain the absence of an increase in eIF 4E phosphorylated under these conditions.