@article{BalakrishnanAndreiSelmerSelmeretal.2010, author = {Balakrishnan, Karthikeyan and Andrei-Selmer, Luminita-Cornelia and Selmer, Thorsten and Bacher, Michael and Dodel, Richard}, title = {Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β}, series = {Journal of Alzheimer's Disease}, volume = {20}, journal = {Journal of Alzheimer's Disease}, number = {1}, isbn = {1387-2877}, pages = {135 -- 143}, year = {2010}, language = {en} } @article{BarbazanHagenbachPaulssenetal.2010, author = {Barbaz{\´a}n, Paula and Hagenbach, Adelheid and Paulßen, Elisabeth and Abram, Ulrich and Carballo, Rosa and Rodriguez-Hermida, Sabina and V{\´a}zquez-L{\´o}pez, Ezequiel M.}, title = {Tricarbonyl Rhenium(I) and Technetium(I) Complexes with Hydrazones Derived from 4,5-Diazafluoren-9-one and 1,10-Phenanthroline-5,6-dione}, series = {European Journal of Inorganic Chemistry}, journal = {European Journal of Inorganic Chemistry}, number = {29}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1099-0682}, doi = {10.1002/ejic.201000522}, pages = {4622 -- 4630}, year = {2010}, abstract = {Tricarbonylrhenium(I) and -technetium(I) halide (halide = Cl and Br) complexes of ligands derived from 4,5-diazafluoren-9-one (df) and 1,10-phenanthroline-5,6-dione (phen) derivatives of benzoic and 2-hydroxybenzoic acid hydrazides have been prepared. The complexes have been characterized by elemental analysis, MS, IR, 1H NMR and absorption and emission UV/Vis spectroscopic methods. The metal centres (ReI and TcI) are coordinated through the nitrogen imine atoms and establish five-membered chelate rings, whereas the hydrazone groups stand uncoordinated. The 1H NMR spectra suggest the same behaviour in solution on the basis of only marginal variations in the chemical shifts of the hydrazine protons.}, language = {en} } @article{BiselliBaeckerPoghossianetal.2010, author = {Biselli, Manfred and B{\"a}cker, Matthias and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Schnitzler, Thomas and Zang, Werner and Wagner, P.}, title = {Entwicklung eines modularen festk{\"o}rperbasierten Sensorsystems f{\"u}r die {\"U}berwachung von Zellkulturfermenationen}, series = {Sensoren und Messsysteme 2010 [Elektronische Ressource] : Vortr{\"a}ge der 15. ITG/GMA-Fachtagung vom 18. bis 19. Mai 2010 in N{\"u}rnberg / Informationstechnische Gesellschaft im VDE (ITG); VDI/VDE-Gesellschaft Mess- und Automatisierungstechnik (GMA)}, journal = {Sensoren und Messsysteme 2010 [Elektronische Ressource] : Vortr{\"a}ge der 15. ITG/GMA-Fachtagung vom 18. bis 19. Mai 2010 in N{\"u}rnberg / Informationstechnische Gesellschaft im VDE (ITG); VDI/VDE-Gesellschaft Mess- und Automatisierungstechnik (GMA)}, publisher = {VDE Verlag}, address = {Berlin}, isbn = {978-3-8007-3260-9}, pages = {688 -- 691}, year = {2010}, language = {de} } @article{ClaessenGrefenMangetal.2010, author = {Claessen, O. and Grefen, Dana and Mang, Thomas and Dikland, H. G. and Dikland, H. G. and Duin, M. van}, title = {Helle Fensterprofilmaterialien : Alterungsverhalten auf Basis von peroxidisch vernetztem EPDM}, series = {Kautschuk, Gummi, Kunststoffe : KGK}, volume = {63}, journal = {Kautschuk, Gummi, Kunststoffe : KGK}, number = {9}, isbn = {0948-3276}, pages = {350 -- 360}, year = {2010}, language = {de} } @article{DegeringEggertPulsetal.2010, author = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich}, title = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides}, series = {Applied and environmental microbiology}, volume = {76}, journal = {Applied and environmental microbiology}, number = {19}, publisher = {American Society for Microbiology}, address = {Washington, DC}, issn = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)}, doi = {10.1128/AEM.01146-10}, pages = {6370 -- 6378}, year = {2010}, abstract = {Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.}, language = {en} } @article{KowollikSchnitzlerBisellietal.2010, author = {Kowollik, S. and Schnitzler, Thomas and Biselli, Manfred and Krueger, R. and Zang, Werner and Peuscher, A. and Schillberg, S. and Fischer, R.}, title = {Die Rolle des Respirationsquotienten in der Zellkulturfermentation}, series = {Chemie Ingenieur Technik}, volume = {82}, journal = {Chemie Ingenieur Technik}, number = {9}, isbn = {Chemie Ingenieur Tec}, pages = {1505 -- 1506}, year = {2010}, language = {de} } @article{PaulssenAlbertoAbram2010, author = {Paulßen, Elisabeth and Alberto, Roger and Abram, Ulrich}, title = {Synthesis, Characterization, and Structures of R3EOTcO3 Complexes (E = C, Si, Ge, Sn, Pb) and Related Compounds}, series = {Inorganic Chemistry}, volume = {49}, journal = {Inorganic Chemistry}, number = {7}, publisher = {American Chemical Society}, address = {Washington}, issn = {1520-510X}, doi = {10.1021/ic1001094}, pages = {3525 -- 3530}, year = {2010}, abstract = {AgTcO4 reacts with R3ECl compounds (E = C, Si, Ge, Sn, Pb; R = Me, iPr, tBu, Ph), tBu2SnCl2, or PhMgCl under formation of novel trioxotechnetium(VII) derivatives. The carbon and silicon derivatives readily undergo decomposition, which was proven by 99Tc NMR spectroscopy and the isolation of decomposition products such as [TcOCl3(THF)(OH2)]. Compounds [Ph3GeOTcO3], [(THF)Ph3SnOTcO3], [(O3TcO)SntBu2(OH)]2, and [(THF)4Mg(OTcO3)2] are more stable and were isolated in crystalline form and characterized by X-ray diffraction.}, language = {en} } @article{PaulssenSchweighoeferAbram2010, author = {Paulßen, Elisabeth and Schweigh{\"o}fer, Philip V. and Abram, Ulrich}, title = {Reactions of [ReOX3(PPh3)2] Complexes (X = Cl, Br) with Phenylacetylene and the Structures of the Products}, series = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry}, volume = {636}, journal = {Zeitschrift f{\"u}r anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1521-3749}, doi = {10.1002/zaac.200900478}, pages = {779 -- 783}, year = {2010}, abstract = {Oxorhenium(V) complexes [ReOX3(PPh3)2] (X = Cl, Br) react with phenylacetylene under formation of complexes with ylide-type ligands. Compounds of the compositions [ReOCl3(PPh3){C(Ph)C(H)(PPh3)}] (1), [ReOBr3(OPPh3){C(Ph)C(H)(PPh3)}] (2), and [ReOBr3(OPPh3){C(H)C(Ph)(PPh3)}] (3) were isolated and characterized by X-ray diffraction. They contain a ligand, which was formed by a nucleophilic attack of released PPh3 at coordinated phenylacetylene. The structures of the products show that there is no preferable position for this attack. Cleavage of the Re-C bond in 3 and dimerization of the organic ligand resulted in the formation of the [{(PPh3)(H)CC(Ph)}2]2+ cation, which crystallized as its [(ReOBr4)(OReO3)]2- salt.}, language = {en} } @article{RibitschKarlBirnerGruenbergeretal.2010, author = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.}, title = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli}, series = {Journal of biotechnology}, volume = {150}, journal = {Journal of biotechnology}, number = {3}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1873-4863 (E-Journal); 0168-1656 (Print)}, doi = {10.1016/j.jbiotec.2010.09.947}, pages = {408 -- 416}, year = {2010}, abstract = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.}, language = {en} } @article{RossPlummerRodeetal.2010, author = {Ross, Jillian and Plummer, Simon M. and Rode, Anja and Scheer, Nico and Bower, Conrad C. and Vogel, Ortwin and Henderson, Colin J. and Wolf, C. Roland and Elcombe, Clifford R.}, title = {Human constitutive androstane receptor (CAR) and pregnane X receptor (PXR) support the hypertrophic but not the hyperplastic response to the murine nongenotoxic hepatocarcinogens phenobarbital and chlordane in vivo}, series = {Toxicological Sciences}, volume = {116}, journal = {Toxicological Sciences}, number = {2}, publisher = {Oxford University Press}, address = {Oxford}, issn = {1096-0929}, doi = {10.1093/toxsci/kfq118}, pages = {452 -- 466}, year = {2010}, abstract = {Mouse nongenotoxic hepatocarcinogens phenobarbital (PB) and chlordane induce hepatomegaly characterized by hypertrophy and hyperplasia. Increased cell proliferation is implicated in the mechanism of tumor induction. The relevance of these tumors to human health is unclear. The xenoreceptors, constitutive androstane receptors (CARs), and pregnane X receptor (PXR) play key roles in these processes. Novel "humanized" and knockout models for both receptors were developed to investigate potential species differences in hepatomegaly. The effects of PB (80 mg/kg/4 days) and chlordane (10 mg/kg/4 days) were investigated in double humanized PXR and CAR (huPXR/huCAR), double knockout PXR and CAR (PXRKO/CARKO), and wild-type (WT) C57BL/6J mice. In WT mice, both compounds caused increased liver weight, hepatocellular hypertrophy, and cell proliferation. Both compounds caused alterations to a number of cell cycle genes consistent with induction of cell proliferation in WT mice. However, these gene expression changes did not occur in PXRKO/CARKO or huPXR/huCAR mice. Liver hypertrophy without hyperplasia was demonstrated in the huPXR/huCAR animals in response to both compounds. Induction of the CAR and PXR target genes, Cyp2b10 and Cyp3a11, was observed in both WT and huPXR/huCAR mouse lines following treatment with PB or chlordane. In the PXRKO/CARKO mice, neither liver growth nor induction of Cyp2b10 and Cyp3a11 was seen following PB or chlordane treatment, indicating that these effects are CAR/PXR dependent. These data suggest that the human receptors are able to support the chemically induced hypertrophic responses but not the hyperplastic (cell proliferation) responses. At this time, we cannot be certain that hCAR and hPXR when expressed in the mouse can function exactly as the genes do when they are expressed in human cells. However, all parameters investigated to date suggest that much of their functionality is maintained.}, language = {en} }