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Christa Verplancke

Researcher at Ghent University

Publications -  8
Citations -  391

Christa Verplancke is an academic researcher from Ghent University. The author has contributed to research in topics: Sesbania rostrata & Azorhizobium caulinodans. The author has an hindex of 5, co-authored 8 publications receiving 363 citations. Previous affiliations of Christa Verplancke include Flanders Institute for Biotechnology.

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Reactive oxygen species and ethylene play a positive role in lateral root base nodulation of a semiaquatic legume

TL;DR: Pharmacological experiments showed that ethylene and reactive oxygen species mediate Nod factor responses and are required for nodule initiation, whereby induction of division and infection could not be uncoupled.
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Calcium spiking patterns and the role of the calcium/calmodulin-dependent kinase CCaMK in lateral root base nodulation of Sesbania rostrata.

TL;DR: In parallel experiments, knockdown of the calcium/calmodulin-dependent protein kinase gene of S. rostrata abolished nodule development but not the formation of infection pockets by intercellular invasion at lateral root bases, suggesting that the colonization of the outer cortex is independent of Ca2+ spiking decoding.
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Seven in Absentia Proteins Affect Plant Growth and Nodulation in Medicago truncatula

TL;DR: A function for SINA E3 ligases in a broad spectrum of plant developmental processes, including nodulation, is illustrated by extensive microscopic analysis of 35S:SINAT5DN transgenic plants.
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Role of nodl and nodj in lipo‐chitooligosaccharide secretion in Azorhizobium caulinodans and Escherichia coli

TL;DR: In E. coli as well as in Azorhizobium, the nod/J‐encoded transporter showed a specificity for more hydrophilic LCOs, and was strongly reduced in the nodJ mutant, and restored to wild‐type levels after complementation.
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Srchi24, a chitinase homolog lacking an essential glutamic acid residue for hydrolytic activity, is induced during nodule development on Sesbania rostrata.

TL;DR: Sequence analyses revealed that Srchi24 is similar to class III chitinases, but lacks an important catalytic glutamate residue, and a function in nodulation is proposed for the Srchi 24 protein.