@article{AckerHuckstorfSaueretal.2004, author = {Acker, Helmut and Huckstorf, Christine and Sauer, Heinrich and Streller, Tino and Wartenberg, Maria}, title = {Deciphering the oxygen sensing pathway by microscopy}, year = {2004}, language = {en} } @article{AlbrechtHaebelKochetal.2004, author = {Albrecht, Tanja and Haebel, Sophie and Koch, Anke and Krause, Ulrike and Eckermann, Nora and Steup, Martin}, title = {Yeast glycogenin (Glg2p) produced in Escherichia coli is simultaneously glucosylated at two vicinal tyrosin residues but results in a reduced bacterial glycogen accumulation}, year = {2004}, abstract = {Saccharomyces cerevisiae possesses two glycogenin isoforms (designated as Glg1p and Glg2p) that both contain a conserved tyrosine residue, Tyr232. However, Glg2p possesses an additional tyrosine residue, Tyr230 and therefore two potential autoglucosylation sites. Glucosylation of Glg2p was studied using both matrix-assisted laser desorption ionization and electrospray quadrupole time of flight mass spectrometry. Glg2p, carrying a C-terminal (His(6)) tag, was produced in Escherichia coli and purified. By tryptic digestion and reversed phase chromatography a peptide (residues 219-246 of the complete Glg2p sequence) was isolated that contained 4-25 glucosyl residues. Following incubation of Glg2p with UDPglucose, more than 36 glucosyl residues were covalently bound to this peptide. Using a combination of cyanogen bromide cleavage of the protein backbone, enzymatic hydrolysis of glycosidic bonds and reversed phase chromatography, mono- and diglucosylated peptides having the sequence PNYGYQSSPAM were generated. MS/MS spectra revealed that glucosyl residues were attached to both Tyr232 and Tyr230 within the same peptide. The formation of the highly glucosylated eukaryotic Glg2p did not favour the bacterial glycogen accumulation. Under various experimental conditions Glg2p-producing cells accumulated approximately 30\% less glycogen than a control transformed with a Glg2p lacking plasmid. The size distribution of the glycogen and extractable activities of several glycogen-related enzymes were essentially unchanged. As revealed by high performance anion exchange chromatography, the intracellular maltooligosaccharide pattern of the bacterial cells expressing the functional eukaryotic transgene was significantly altered. Thus, the eukaryotic glycogenin appears to be incompatible with the bacterial initiation of glycogen biosynthesis}, language = {en} } @article{AleAghaBolayBraunetal.2004, author = {Ale-Agha, Nosratollah and Bolay, Adrien and Braun, Uwe and Jage, Horst and Kummer, Volker and Lebeda, Ales and Piatek, Marcin and Shin, Hyeon-Dong and Zimmermannova-Pastircakova, Katarina}, title = {Erysiphe catalpae and E. elevata in Europe}, year = {2004}, language = {en} } @article{AndersBeierBrunketal.2004, author = {Anders, Kenneth and Beier, Wolfgang and Brunk, Ingo and Burkart, Bettina and Mrzljak, Anders and Oehlschl{\"a}ger, Susanne}, title = {Freie Sukzession und Offenlandmanagement}, isbn = {3-540-22449-1}, year = {2004}, language = {de} } @article{AndersMrzljakWallschlaegeretal.2004, author = {Anders, Kenneth and Mrzljak, Jadranka and Wallschl{\"a}ger, Hans-Dieter and Wiegleb, Gerhard}, title = {Handbuch Offenlandmanagement am Beispiel ehemaliger und in Nutzung befindlicher Truppen{\"u}bungspl{\"a}tze}, publisher = {Springer}, address = {Berlin}, isbn = {3-540-22449-1}, pages = {320 S.}, year = {2004}, language = {de} } @article{AndersProchnowSchlaudereretal.2004, author = {Anders, Kenneth and Prochnow, Annette and Schlauderer, Ralf and Wiegleb, Gerhard}, title = {Die Szenario-Methode als Instrument der Naturschutzplanung im Offenland}, isbn = {3-540-22449-1}, year = {2004}, language = {de} } @article{Baumann2004, author = {Baumann, Otto}, title = {Konventionelle Fluoreszenzmikroskopie : Theorie und Anwendungsm{\"o}glichkeiten}, year = {2004}, language = {de} } @article{Baumann2004, author = {Baumann, Otto}, title = {Spatial pattern of nonmuscle myosin-II distribution during the development of the Drosophila compound eye and implications for retinal morphogenesis}, year = {2004}, abstract = {Nonmuscle myosin-II is a motor protein that drives cell movement and changes in cell shape during tissue and organ development. This study has determined he dynamic changes in myosin-II distribution during Drosophila compound eye morphogenesis. In photoreceptor neurons, myosin-II is undetectable at the apical domain throughout the first half of pupal life, at which time this membrane domain is involuted into the epithelium and progresses toward the retinal floor. Myosin-II is deployed at the apical surface at about 60\% of pupal development, once the developing rhabdomeres reach the retinal floor. Subsequently, myosin-II becomes restricted to two stripes at the sides of the developing rhabdomere, adopting its final position within the visual cells R1-6; here, myosin-II is associated with a set of actin filaments that extend alongside the rhabdomeres. At the midpupal stage, myosin-II is also incorporated into stress-fiber-like arrays within the basal endfeet of the pigment cells that then change their shape. This spatiotemporal pattern of myosin- II localization and the morphological defects observed in the eyes of a myosin-II mutant suggest that the myosin-II/F- actin system is involved in the alignment of the rhabdomeres within the retina and in the flattening of the retinal floor. The observation that the myosin-II/F-actin arrays are incomplete or disorganized in R7/R8 and in rhodopsin-1-null R1-6 suggests further that the establishment and stability of this cytoskeletal system depend on rhodopsin-1 expression. (C) 2004 Elsevier Inc. All rights reserved}, language = {en} } @article{BaumannKuehnelDamesetal.2004, author = {Baumann, Otto and K{\"u}hnel, Dana and Dames, Petra and Walz, Bernd}, title = {Dopaminergic and serotonergic innervation of cockroach salivary glands : distribution and morphology of synapses and release sites}, year = {2004}, abstract = {The paired salivary glands in the cockroach are composed of acini with ion-transporting peripheral P-cells and protein-secreting central C-cells, and a duct system for the modification of the primary saliva. Secretory activity is controlled by serotonergic and dopaminergic neurons, whose axons form a dense plexus on the glands. The spatial relationship of release sites for serotonin and dopamine to the various cell types was determined by anti-synapsin immunofluorescence confocal microscopy and electron microscopy. Every C-cell apparently has only serotonergic synapses on its surface. Serotonergic and dopaminergic fibres on the acini have their release zones at a distance of similar to0.5 mum from the P-cells. Nerves between acinar lobules may serve as neurohaemal organs and contain abundant dopaminergic and few serotonergic release sites. Some dopaminergic and serotonergic release sites reside in the duct epithelium, the former throughout the duct system, the latter only in segments next to acini. These findings are consistent with the view that C-cells respond exclusively to serotonin, P-cells to serotonin and dopamine, and most duct cells only to dopamine. Moreover, the data suggest that C-cells are stimulated by serotonin released close to their surface, whereas P-cells and most duct cells are exposed to serotonin/dopamine liberated at some distance}, language = {en} } @article{BeathamMiddletonRomeroetal.2004, author = {Beatham, Jane L. and Middleton, A. and Romero, Rosario and VanderVen, Peter F. M. and Blanco, Gonzalo}, title = {Functional characterisation of the Ky protein}, issn = {0960-8966}, year = {2004}, language = {en} }