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Silke Robatzek

Researcher at Ludwig Maximilian University of Munich

Publications -  121
Citations -  18286

Silke Robatzek is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Arabidopsis & Flagellin. The author has an hindex of 59, co-authored 116 publications receiving 16098 citations. Previous affiliations of Silke Robatzek include University of Basel & Max Planck Society.

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The WRKY superfamily of plant transcription factors

TL;DR: The WRKY proteins are a superfamily of transcription factors with up to 100 representatives in Arabidopsis that appear to be involved in the regulation of various physio-logical programs that are unique to plants, including pathogen defense, senescence and trichome development.
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A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence

TL;DR: BAK1 is shown to have a functional role in PRR-dependent signalling, which initiates innate immunity, and evidence is provided that FLS2 and BAK1 form a complex in vivo, in a specific ligand-dependent manner, within the first minutes of stimulation with flagellin.
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Bacterial disease resistance in Arabidopsis through flagellin perception.

TL;DR: It is shown that treatment of plants with flg22, a peptide representing the elicitor-active epitope of flagellin, induces the expression of numerous defence-related genes and triggers resistance to pathogenic bacteria in wild-type plants, but not in plants carrying mutations in the flageLLin receptor gene FLS2.
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The N Terminus of Bacterial Elongation Factor Tu Elicits Innate Immunity in Arabidopsis Plants

TL;DR: It is shown that elongation factor Tu, the most abundant bacterial protein, acts as a PAMP in Arabidopsis thaliana and other Brassicaceae, and an N-acetylated peptide comprising the first 18 amino acids, termed elf18, is fully active as inducer of defense responses.
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Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis

TL;DR: It is proposed that plant cells regulate pathogen-associated molecular pattern (PAMP)-mediated PRR activities by subcellular compartmentalization.