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Analysis of the functional interaction of Arabidopsis starch synthase and branching enzyme isoforms reveals that the cooperative action of SSI and BEs results in glucans with polymodal chain length distribution similar to amylopectin.Reduction of the cytosolic phosphoglucomutase in Arabidopsis reveals impact on plant growth, seed and root development, and carbohydrate partitioningModification of the endogenous NO level influences apple embryos dormancy by alterations of nitrated and biotinylated protein patterns.Proteomic analysis of S-nitrosylated and S-glutathionylated proteins in wheat seedlings with different dehydration tolerances.Eukaryotic starch degradation: integration of plastidial and cytosolic pathways.Cytosolic heteroglycans in photoautotrophic and in heterotrophic plant cells.Starch phosphorylation: insights and perspectives.Starch-related carbon fluxes in roots and leaves of Arabidopsis thaliana.The glucan phosphorylation mediated by α-glucan, water dikinase (GWD) is also essential in the light phase for a functional transitory starch turn-over.Two carbon fluxes to reserve starch in potato (Solanum tuberosum L.) tuber cells are closely interconnected but differently modulated by temperature.Loss of cytosolic phosphoglucose isomerase affects carbohydrate metabolism in leaves and is essential for fertility of Arabidopsis.Glucose 1-phosphate is efficiently taken up by potato (Solanum tuberosum) tuber parenchyma cells and converted to reserve starch granules.Expression of human c-reactive protein in different systems and its purification from Leishmania tarentolae.Reduced starch granule number per chloroplast in the dpe2/phs1 mutant is dependent on initiation of starch degradation.The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the A- and B-type allomorphs of crystallized maltodextrins but the mode of action differs.Reduction of the plastidial phosphorylase in potato (Solanum tuberosum L.) reveals impact on storage starch structure during growth at low temperature.Identification, subcellular localization and biochemical characterization of water-soluble heteroglycans (SHG) in leaves of Arabidopsis thaliana L.: distinct SHG reside in the cytosol and in the apoplast.Starch Synthase 4 and Plastidal Phosphorylase Differentially Affect Starch Granule Number and Morphology.Feedback inhibition of starch degradation in Arabidopsis leaves mediated by trehalose 6-phosphate.The plastidial glucan, water dikinase (GWD) catalyses multiple phosphotransfer reactions.Phosphorylation of transitory starch by α-glucan, water dikinase during starch turnover affects the surface properties and morphology of starch granules.Novel starch-related enzymes and carbohydratesIdentification of a novel heteroglycan-interacting protein, HIP 1.3, from Arabidopsis thalianaGlucose-1-phosphate transport into protoplasts and chloroplasts from leaves of ArabidopsisA transglucosidase necessary for starch degradation and maltose metabolism in leaves at night acts on cytosolic heteroglycans (SHG)Starch-related cytosolic heteroglycans in roots from Arabidopsis thalianaSecretory leukocyte protease inhibitor (SLPI) might contaminate murine monoclonal antibodies after purification on protein GHeterologous expression of AtPAP2 in transgenic potato influences carbon metabolism and tuber developmentCarbon transitions from either Calvin cycle or transitory starch to heteroglycans as revealed by (14) C-labeling experiments using protoplasts from ArabidopsisArabidopsis cytosolic alpha-glycan phosphorylase, PHS2, is important during carbohydrate imbalanced conditionsEARLY STARVATION1 specifically affects the phosphorylation action of starch-related dikinases
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P50
description
researcher ORCID ID = 0000-0003-0137-7611
@en
wetenschapper
@nl
name
Joerg Fettke
@ast
Joerg Fettke
@en
Joerg Fettke
@es
Joerg Fettke
@nl
type
label
Joerg Fettke
@ast
Joerg Fettke
@en
Joerg Fettke
@es
Joerg Fettke
@nl
prefLabel
Joerg Fettke
@ast
Joerg Fettke
@en
Joerg Fettke
@es
Joerg Fettke
@nl
P214
P106
P1153
6506341479
P214
P31
P496
0000-0003-0137-7611
P7859
viaf-18398190