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Wolfgang P. Schröder

Researcher at Grünenthal GmbH

Publications -  151
Citations -  6794

Wolfgang P. Schröder is an academic researcher from Grünenthal GmbH. The author has contributed to research in topics: Thylakoid & Photosystem II. The author has an hindex of 47, co-authored 149 publications receiving 6287 citations. Previous affiliations of Wolfgang P. Schröder include Umeå University & Stockholm University.

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Proteome Map of the Chloroplast Lumen of Arabidopsis thaliana

TL;DR: A systematic characterization of the luminal thylakoid proteins from the model organism Arabidopsis thaliana showed that 19 of 36 luminal precursors were marked by a twin-arginine motif for import via the Tat pathway, and it was estimated that the thylAKoid lumen of the chloroplast contains ∼80 proteins.
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Astrocytes in the hippocampus of patients with temporal lobe epilepsy display changes in potassium conductances

TL;DR: Functional properties of astrocytes were investigated with the patch‐clamp technique in acute hippocampal brain slices obtained from surgical specimens of patients suffering from pharmaco‐resistant temporal lobe epilepsy (TLE) in patients with significant neuronal cell loss.
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The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature

TL;DR: A proteomic approach is taken to identify 43 differentially displayed proteins that participate in photosynthesis, other plastid metabolic functions, hormone biosynthesis and stress sensing and signal transduction in Arabidopsis.
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Identification of the phosphorylation sites of the murine small heat shock protein hsp25.

TL;DR: Native phosphorylated mouse small heat shock protein hsp25 from Ehrlich ascites tumor cells was isolated and the in vivo phosphorylation sites of the protein were determined.
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The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.

TL;DR: Deletion mutations of the low molecular mass subunits from both prokaryotic and eukaryotic model systems are compared in an attempt to understand the function of these proteins, and it seems that the majority of them are involved in stabilization, assembly or dimerization of the PSII complex.