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Els Van Der Schueren

Researcher at Ghent University

Publications -  7
Citations -  2108

Els Van Der Schueren is an academic researcher from Ghent University. The author has contributed to research in topics: Endoreduplication & Arabidopsis. The author has an hindex of 7, co-authored 7 publications receiving 1987 citations. Previous affiliations of Els Van Der Schueren include Flanders Institute for Biotechnology.

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Functional Analysis of Cyclin-Dependent Kinase Inhibitors of Arabidopsis

TL;DR: It is concluded that KRP2 exerts a plant growth inhibitory activity by reducing cell proliferation in leaves, but, in contrast to its mammalian counterparts, it may not control the timing of cell cycle exit and differentiation.
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Arabidopsis WEE1 kinase controls cell cycle arrest in response to activation of the DNA integrity checkpoint.

TL;DR: It is concluded that the plant WEE1 gene is not rate-limiting for cycle progression under normal growth conditions but is a critical target of the ATR-ATM signaling cascades that inhibit the cell cycle upon activation of the DNA integrity checkpoints, coupling mitosis to DNA repair in cells that suffer DNA damage.
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The plant-specific cyclin-dependent kinase CDKB1;1 and transcription factor E2Fa-DPa control the balance of mitotically dividing and endoreduplicating cells in Arabidopsis

TL;DR: Surprisingly, CDKB1;1 transcription was controlled by the E2F pathway, as shown by its upregulation in E2Fa-DPa–overproducing plants and mutational analysis of the E1-S and G2-M binding site in the CDKB 1;1 promoter.
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The Cyclin-Dependent Kinase Inhibitor KRP2 Controls the Onset of the Endoreduplication Cycle during Arabidopsis Leaf Development through Inhibition of Mitotic CDKA;1 Kinase Complexes

TL;DR: It is shown that the A-type cyclin-dependent kinase CDKA;1 and its specific inhibitor, the Kip-related protein, KRP2 regulate the mitosis-to-endocycle transition during Arabidopsis thaliana leaf development and illustrated that K RP2 protein abundance is regulated posttranscriptionally through CDK phosphorylation and proteasomal degradation.