@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{BaumannEckermannMeinel1994,
  author    = {Baumann, Guido and Eckermann, Nora and Meinel, Thomas},
  title     = {Zur Kohlenstoffassimilation in gr{\"u}nen Zuckerr{\"u}ben-Kalluskulturen},
  year      = {1994},
  language  = {de}
}
@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{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{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{FettkeEckermannTiessenetal.2005,
  author    = {Fettke, J{\"o}rg and Eckermann, Nora and Tiessen, Axel and Geigenberger, Peter Ludwig and Steup, Martin},
  title     = {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},
  issn      = {0960-7412},
  year      = {2005},
  abstract  = {Water-soluble heteroglycans (SHG) were isolated from leaves of wild-type Arabidopsis thaliana L. and from two starch-deficient mutants. Major constituents of the SHG are arabinose, galactose, rhamnose, and glucose. SHG was separated into low (< 10 kDa; SHG(S)) and high (> 10 kDa; SHG(L)) molecular weight compounds. SHG(S) was resolved into approximately 25 distinct oligoglycans by ion exchange chromatography. SHG(L) was further separated into two subfractions, designated as subfraction I and II, by field flow fractionation. For the intracellular localization of the various SHG compounds several approaches were chosen: first, leaf material was subjected to non-aqueous fractionation. The apolar gradient fractions were characterized by monitoring markers and were used as starting material for the SHG isolation. Subfraction I and SHG(S) exhibited a distribution similar to that of cytosolic markers whereas subfraction II cofractionated with crystalline cellulose. Secondly, intact organelles were isolated and used for SHG isolation. Preparations of intact organelles (mitochondria plus peroxisomes) contained no significant amount of any heteroglycan. In isolated intact microsomes a series of oligoglycans was recovered but neither subfraction I nor II. In in vitro assays using glucose 1-phosphate and recombinant cytosolic (Pho 2) phosphorylase both SHG(S) and subfraction I acted as glucosyl acceptor whereas subfraction II was essentially inactive. Rabbit muscle phosphorylase a did not utilize any of the plant glycans indicating a specific Pho 2-glycan interaction. As revealed by in vivo labeling experiments using (CO2)-C-14 carbon fluxes into subfraction I and II differed. Furthermore, in leaves the pool size of subfraction I varied during the light-dark regime},
  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{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{DauvilleeChochoisSteupetal.2006,
  author    = {Dauvillee, David and Chochois, Vincent and Steup, Martin and Haebel, Sophie and Eckermann, Nora and Ritte, Gerhard and Ral, Jean-Philippe and Colleoni, Christophe and Hicks, Glenn and Wattebled, Fabrice and Deschamps, Philippe and Lienard, Luc and Cournac, Laurent and Putaux, Jean-Luc and Dupeyre, Danielle and Ball, Steven G.},
  title     = {Plastidial phosphorylase is required for normal starch synthesis in Chlamydomonas reinhardtii},
  series = {The plant journal},
  volume    = {48},
  journal   = {The plant journal},
  number    = {2},
  publisher = {Blackwell},
  address   = {Oxford},
  issn      = {0960-7412},
  doi       = {10.1111/j.1365-313X.2006.02870.x},
  pages     = {274 -- 285},
  year      = {2006},
  abstract  = {Among the three distinct starch phosphorylase activities detected in Chlamydomonas reinhardtii, two distinct plastidial enzymes (PhoA and PhoB) are documented while a single extraplastidial form (PhoC) displays a higher affinity for glycogen as in vascular plants. The two plastidial phosphorylases are shown to function as homodimers containing two 91-kDa (PhoA) subunits and two 110-kDa (PhoB) subunits. Both lack the typical 80-amino-acid insertion found in the higher plant plastidial forms. PhoB is exquisitely sensitive to inhibition by ADP-glucose and has a low affinity for malto-oligosaccharides. PhoA is more similar to the higher plant plastidial phosphorylases: it is moderately sensitive to ADP-glucose inhibition and has a high affinity for unbranched malto-oligosaccharides. Molecular analysis establishes that STA4 encodes PhoB. Chlamydomonas reinhardtii strains carrying mutations at the STA4 locus display a significant decrease in amounts of starch during storage that correlates with the accumulation of abnormally shaped granules containing a modified amylopectin structure and a high amylose content. The wild-type phenotype could be rescued by reintroduction of the cloned wild-type genomic DNA, thereby demonstrating the involvement of phosphorylase in storage starch synthesis.},
  language  = {en}
}