@article{BaumannEckermann1994,
  author    = {Baumann, Ingrid and Eckermann, Nora},
  title     = {Ploidy level and chlorophyll content of single plastids and cells from callus cultures during conversion to autotrophic growth},
  year      = {1994},
  language  = {en}
}
@article{BaumannEckermannKrauseetal.1994,
  author    = {Baumann, Ingrid and Eckermann, Nora and Krause, Udo and Baumann, Guido},
  title     = {Effects of sucrose in the culture medium on cytological characteristics, pigments and photosynthetic activity of green callus cultures of sugar beet},
  year      = {1994},
  language  = {en}
}
@article{EckermannBaumann1995,
  author    = {Eckermann, Nora and Baumann, Guido},
  title     = {Enzymatic changes in callus cultures of sugar beet during the transition from photoheterotrophic to photoautotrophic growth},
  year      = {1995},
  language  = {en}
}
@article{RitteEckermannHaebeletal.2000,
  author    = {Ritte, Gerhard and Eckermann, Nora and Haebel, Sophie and Lorberth, Ruth and Steup, Martin},
  title     = {Compartmentation of the starch-related R1 protein in higher plants},
  year      = {2000},
  language  = {en}
}
@article{RitteLloydEckermannetal.2002,
  author    = {Ritte, Gerhard and Lloyd, James R. and Eckermann, Nora and Rottmann, Antje and Kossmann, Jens and Steup, Martin},
  title     = {The starch-related R1 protein is an a-glucan, water dikinase},
  issn      = {0027-8424},
  year      = {2002},
  language  = {en}
}
@article{EckermannFettkeSteup2002,
  author    = {Eckermann, Nora and Fettke, J{\"o}rg and Steup, Martin},
  title     = {Identification of polysaccharide binding proteins by affinity electrophoresis in inhomogeneous polyacrylamide gels and subsequent SDS-PAGE/MALDI-TOF analysis},
  year      = {2002},
  language  = {en}
}
@article{UsadelKuschinskyRossoetal.2004,
  author    = {Usadel, Bj{\"o}rn and Kuschinsky, Anja M. and Rosso, Mario G. and Eckermann, Nora and Pauly, Markus},
  title     = {RHM2 is involved in mucilage pectin synthesis and is required for the development of the seed coat in Arabidopsis},
  year      = {2004},
  abstract  = {Pectins are major components of primary plant cell walls and the seed mucilage of Arabidopsis. Despite progress in the structural elucidation of pectins, only very few enzymes participating in or regulating their synthesis have been identified. A first candidate gene involved-in the synthesis of pectinaceous rhamnogalacturonan I is RHM2, a putative plant ortholog to NDP-rhamnose biosynthetic enzymes in bacteria. Expression studies with a promoter beta-glucuronidase construct and reverse transcription PCR data show that RHM2 is expressed ubiquitously. Rhm2 T-DNA insertion mutant lines were identified using a reverse genetics approach. Analysis of the rhm2 seeds by various staining methods and chemical analysis of the mucilage revealed a strong reduction of rhamnogalacturonan I in the mucilage and a decrease of its molecular weight. In addition, scanning electron microscopy of the seed surface indicated a distorted testa morphology, illustrating not only a structural but also a developmental role for RGI or rhamnose metabolism in proper testa formation},
  language  = {en}
}
@article{FettkeEckermannPoesteetal.2004,
  author    = {Fettke, J{\"o}rg and Eckermann, Nora and Poeste, Simon and Steup, Martin},
  title     = {The glycan substrate of the cytosolic (Pho 2) phosphorylase isozyme from Pisum sativum L. : identification, linkage analysis and subcellular localization},
  issn      = {0960-7412},
  year      = {2004},
  abstract  = {The subcellular distribution of starch-related enzymes and the phenotype of Arabidopsis mutants defective in starch degradation suggest that the plastidial starch turnover is linked to a cytosolic glycan metabolism. In this communication, a soluble heteroglycan (SHG) from leaves of Pisum sativum L. has been studied. Major constituents of the SHG are galactose, arabinose and glucose. For subcellular location, the SHG was prepared from isolated protoplasts and chloroplasts. On a chlorophyll basis, protoplasts and chloroplasts yielded approximately 70\% and less than 5\%, respectively, of the amount of the leaf-derived SHG preparation. Thus, most of SHG resides inside the cell but outside the chloroplast. SHG is soluble and not membrane-associated. Using membrane filtration, the SHG was separated into a <10 kDa and a >10 kDa fraction. The latter was resolved into two subfractions (I and II) by field-flow fractionation. In the protoplast-derived >10 kDa SHG preparation the subfraction I was by far the most dominant compound. beta-Glucosyl Yariv reagent was reactive with subfraction II, but not with subfraction I. In in vitro assays the latter acted as glucosyl acceptor for the cytosolic (Pho 2) phosphorylase but not for rabbit muscle phosphorylase. Glycosidic linkage analyses of subfractions I and II and of the Yariv reagent reactive glycans revealed that all three glycans contain a high percentage of arabinogalactan-like linkages. However, SHG possesses a higher content of minor compounds, namely glucosyl, mannosyl, rhamnosyl and fucosyl residues. Based on glycosyl residues and glycosidic linkages, subfraction I possesses a more complex structure than subfraction II},
  language  = {en}
}
@article{RitteScharfEckermannetal.2004,
  author    = {Ritte, Gerhard and Scharf, Anke and Eckermann, Nora and Haebel, Sophie and Steup, Martin},
  title     = {Phosphorylation of transitory starch is increased during degradation},
  year      = {2004},
  abstract  = {The starch excess phenotype of Arabidopsis mutants defective in the starch phosphorylating enzyme glucan, water dikinase (EC 2.7.9.4) indicates that phosphorylation of starch is required for its degradation. However, the underlying mechanism has not yet been elucidated. In this study, two in vivo systems have been established that allow the analysis of phosphorylation of transitory starch during both biosynthesis in the light and degradation in darkness. First, a photoautotrophic culture of the unicellular green alga Chlamydomonas reinhardtii was used to monitor the incorporation of exogenously supplied P-32 orthophosphate into starch. Illuminated cells incorporated P-32 into starch with a constant rate during 2 h. By contrast, starch phosphorylation in darkened cells exceeded that in illuminated cells within the first 30 min, but subsequently phosphate incorporation declined. Pulse-chase experiments performed with P-32/P-31 orthophosphate revealed a high turnover of the starch-bound phosphate esters in darkened cells but no detectable turnover in illuminated cells. Secondly, leaf starch granules were isolated from potato (Solanum tuberosum) plants grown under controlled conditions and glucan chains from the outer granule layer were released by isoamylase. Phosphorylated chains were purified and analyzed using high performance anion-exchange chromatography and matrix-assisted laser desorption/ionization mass spectrometry. Glucans released from the surface of starch granules that had been isolated from darkened leaves possessed a considerably higher degree of phosphorylation than those prepared from leaves harvested during the light period. Thus, in the unicellular alga as well as in potato leaves, net starch degradation is accompanied with an increased phosphorylation of starch},
  language  = {en}
}
@article{EckermannFettkePaulyetal.2004,
  author    = {Eckermann, Nora and Fettke, J{\"o}rg and Pauly, Markus and Bazant, Esther and Steup, Martin},
  title     = {Starch-metabolism related isozymes in higher plants},
  year      = {2004},
  language  = {en}
}