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Ireen Köllmer

Researcher at Free University of Berlin

Publications -  7
Citations -  1725

Ireen Köllmer is an academic researcher from Free University of Berlin. The author has contributed to research in topics: Cytokinin & Arabidopsis. The author has an hindex of 7, co-authored 7 publications receiving 1517 citations.

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Root-Specific Reduction of Cytokinin Causes Enhanced Root Growth, Drought Tolerance, and Leaf Mineral Enrichment in Arabidopsis and Tobacco

TL;DR: It is demonstrated that a single dominant gene could regulate a complex trait, root growth, and cytokinin regulates root growth in a largely organ-autonomous fashion that is consistent with its dual role as a hormone with both paracrine and long-distance activities.
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Immediate-early and delayed cytokinin response genes of Arabidopsis thaliana identified by genome-wide expression profiling reveal novel cytokinin-sensitive processes and suggest cytokinin action through transcriptional cascades.

TL;DR: A genome-wide view of changes in cytokinin-responsive transcript abundance of genes that might be functionally relevant for the many biological processes that are governed by cytokinins is presented.
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Acoustic communication in noise: regulation of call characteristics in a New World monkey.

TL;DR: This study on common marmosets Callithrix jacchus is the first to examine noise-dependent mechanisms of vocal plasticity in a New World monkey, finding the first evidence of such mechanism of vocal Plasticity in an animal communication system.
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New Insights into the Biology of Cytokinin Degradation

TL;DR: The results corroborate the relevance of metabolic control in determining cytokinin activity and show using reporter gene and semiquantitative RT-PCR analyses regulation of individual CKX genes by cytokinIn, auxin, ABA, and phosphate starvation.
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Biochemical Characterization of Cytokinin Oxidases/Dehydrogenases from Arabidopsis thaliana Expressed in Nicotiana tabacum L.

TL;DR: Cytokinin nucleotides, considered as resistant to CKX attack until now, were found to be potent substrates for some of the CKX isoforms and biochemical characterization of the AtCKX1, AtCkX2, At cKX4 and AtcKX7 enzymes showed pH-dependent activity profiles.