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1Latest Papers from Table of Contents or Articles in PressD. T. Jones ; N. Jager ; M. Kool ; T. Zichner ; B. Hutter ; M. Sultan ; Y. J. Cho ; T. J. Pugh ; V. Hovestadt ; A. M. Stutz ; T. Rausch ; H. J. Warnatz ; M. Ryzhova ; S. Bender ; D. Sturm ; S. Pleier ; H. Cin ; E. Pfaff ; L. Sieber ; A. Wittmann ; M. Remke ; H. Witt ; S. Hutter ; T. Tzaridis ; J. Weischenfeldt ; B. Raeder ; M. Avci ; V. Amstislavskiy ; M. Zapatka ; U. D. Weber ; Q. Wang ; B. Lasitschka ; C. C. Bartholomae ; M. Schmidt ; C. von Kalle ; V. Ast ; C. Lawerenz ; J. Eils ; R. Kabbe ; V. Benes ; P. van Sluis ; J. Koster ; R. Volckmann ; D. Shih ; M. J. Betts ; R. B. Russell ; S. Coco ; G. P. Tonini ; U. Schuller ; V. Hans ; N. Graf ; Y. J. Kim ; C. Monoranu ; W. Roggendorf ; A. Unterberg ; C. Herold-Mende ; T. Milde ; A. E. Kulozik ; A. von Deimling ; O. Witt ; E. Maass ; J. Rossler ; M. Ebinger ; M. U. Schuhmann ; M. C. Fruhwald ; M. Hasselblatt ; N. Jabado ; S. Rutkowski ; A. O. von Bueren ; D. Williamson ; S. C. Clifford ; M. G. McCabe ; V. P. Collins ; S. Wolf ; S. Wiemann ; H. Lehrach ; B. Brors ; W. Scheurlen ; J. Felsberg ; G. Reifenberger ; P. A. Northcott ; M. D. Taylor ; M. Meyerson ; S. L. Pomeroy ; M. L. Yaspo ; J. O. Korbel ; A. Korshunov ; R. Eils ; S. M. Pfister ; P. Lichter
Nature Publishing Group (NPG)
Published 2012Staff ViewPublication Date: 2012-07-27Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Aging/genetics ; Amino Acid Sequence ; Cell Transformation, Neoplastic ; Cerebellar Neoplasms/classification/diagnosis/*genetics/pathology ; Child ; Chromatin/metabolism ; Chromosomes, Human/genetics ; DEAD-box RNA Helicases/genetics ; DNA Helicases/genetics ; DNA-Binding Proteins/genetics ; Genome, Human/*genetics ; Genomics ; Hedgehog Proteins/metabolism ; High-Throughput Nucleotide Sequencing ; Histone Demethylases/genetics ; Humans ; Medulloblastoma/classification/diagnosis/*genetics/pathology ; Methylation ; Mutation/genetics ; Mutation Rate ; Neoplasm Proteins/genetics ; Nuclear Proteins/genetics ; Oncogene Proteins, Fusion/genetics ; Phosphoprotein Phosphatases/genetics ; Polyploidy ; Receptors, Cell Surface/genetics ; Sequence Analysis, RNA ; Signal Transduction ; T-Box Domain Proteins/genetics ; Transcription Factors/genetics ; Wnt Proteins/metabolism ; beta Catenin/geneticsPublished by: -
2Articles: DFG German National LicensesPochhammer, V. Hans 〈Fregattenkapitän z〉
Wiesbaden : Periodicals Archive Online (PAO)
Published 1944Staff ViewISSN: 0016-7479Topics: GeographyURL: -
3FIS Bildung LiteraturdatenbankStaff View
Type of Medium: bookPublication Date: 2008Keywords: Sekundarbereich ; Unterricht ; Internationaler Vergleich ; AufsatzsammlungLanguage: English -
4FIS Bildung LiteraturdatenbankStaff View
Type of Medium: bookPublication Date: 1988Keywords: SportLanguage: GermanNote: Literaturangaben 13 -
5Articles: DFG German National LicensesSaunders, Neil F. W. ; Houben, Edith N. G. ; Koefoed, Sarah ; De Weert, Sandra ; Reijnders, Willem N. M. ; Westerhoff, Hans V. ; De Boer, Anthonius P. N. ; Van Spanning, Rob J. M.
Oxford BSL : Blackwell Science Ltd
Published 1999Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The nirIX gene cluster of Paracoccus denitrificans is located between the nir and nor gene clusters encoding nitrite and nitric oxide reductases respectively. The NirI sequence corresponds to that of a membrane-bound protein with six transmembrane helices, a large periplasmic domain and cysteine-rich cytoplasmic domains that resemble the binding sites of [4Fe-4S] clusters in many ferredoxin-like proteins. NirX is soluble and apparently located in the periplasm, as judged by the predicted signal sequence. NirI and NirX are homologues of NosR and NosX, proteins involved in regulation of the expression of the nos gene cluster encoding nitrous oxide reductase in Pseudomonas stutzeri and Sinorhizobium meliloti. Analysis of a NirI-deficient mutant strain revealed that NirI is involved in transcription activation of the nir gene cluster in response to oxygen limitation and the presence of N-oxides. The NirX-deficient mutant transiently accumulated nitrite in the growth medium, but it had a final growth yield similar to that of the wild type. Transcription of the nirIX gene cluster itself was controlled by NNR, a member of the family of FNR-like transcriptional activators. An NNR binding sequence is located in the middle of the intergenic region between the nirI and nirS genes with its centre located at position −41.5 relative to the transcription start sites of both genes. Attempts to complement the NirI mutation via cloning of the nirIX gene cluster on a broad-host-range vector were unsuccessful, the ability to express nitrite reductase being restored only when the nirIX gene cluster was reintegrated into the chromosome of the NirI-deficient mutant via homologous recombination in such a way that the wild-type nirI gene was present directly upstream of the nir operon.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesVan Spanning, Rob J. M. ; De Boer, Anthonius P. N. ; Reijnders, Willem N. M. ; Westerhoff, Hans V. ; Stouthamer, Adriaan H. ; Van Der Oost, John
Oxford BSL : Blackwell Science Ltd
Published 1997Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The Paracoccus denitrificansfnrP gene encoding a homologue of the Escherichia coli FNR protein was localized upstream of the gene cluster that encodes the high-affinity cbb3-type oxidase. FnrP harbours the invariant cysteine residues that are supposed to be the ligands of the redox-sensitive [4Fe–4S] cluster in FNR. NNR, another FNR-like transcriptional regulator in P. denitrificans, does not. Analysis of FnrP and NNR single and double mutants revealed that the two regulators each exert exclusive control on the expression of a discrete set of target genes. In FnrP mutants, the expression of cytochrome c peroxidase was blocked, that of membrane-bound nitrate reductase and the cbb3-type oxidase was significantly reduced, whilst the activity of the bb3-type quinol oxidase was increased. The amounts of the nitrite and nitric oxide reductases in these FnrP mutants were the same as in the wild type. NNR mutants, on the other hand, were disturbed exclusively in the concentrations of nitrite reductase and nitric oxide reductase. An FnrP.NNR double mutant combined the phenotypes of the single mutant strains. In all three mutants, the concentrations and/or activities of the aa3-type oxidase, cytochrome c550, cytochrome c552, and nitrous oxide reductase equalled those in the wild type. As the FNR boxes in front of the FnrP- and NNR-regulated genes are highly similar to or even identical to each other, the absence of cross-talk between the regulation by FnrP and NNR implies that as yet unidentified factors are important in the control. It is proposed that the redox state of an intracellular redox couple other than the oxygen/water couple is one of the factors that modulates the activity of FnrP.Type of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesWorkum, Marielle ; Dooren, Silvy J. M. ; Oldenburg, Nienke ; Molenaar, Douwe ; Jensen, Peter R. ; Snoep, Jacky L. ; Westerhoff', Hans V.
Oxford, UK : Blackwell Publishing Ltd
Published 1996Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: ATP/ADP ratios were varied in different ways and the degree of negative supercoiling was determined in Escherichia coli. Independent of whether the ATP/ADP ratio was reduced by a shift to anaerobic conditions, by addition of a protonophore (dinitrophenol) or by potassium cyanide addition, DNA supercoiling decreased similarly with the ATP/ADP ratio. The experiments were performed under well-defined conditions, where oxidative phosphorylation was the dominant route for ATP synthesis, i.e. using a minimal salts medium with succinate as the sole free-energy and carbon source, and in the presence or absence of ammonia as the nitrogen source. The results of the different experiments were consistent with a single linear relationship between the log(ATP/ADP) and the change in linking number. The dependence of DNA supercoiling on the ATP/ADP ratio was not influenced by inhibitors of transcription or translation. Because the ATP/ADP ratio was modulated in different ways, the unique relationship suggests coupling between the phosphorylation potential and DNA supercoiling. This was most probably mediated by the DNA gyrase, independent of topoisomerase I or transcription.Type of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesRohwer, Johann M. ; Bader, Rechien ; Westerhoff, Hans V. ; Postma, Pieter W.
Oxford BSL : Blackwell Science Ltd, UK
Published 1998Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The uptake of methyl α-D-glucopyranoside by the phosphoenolpyruvate-dependent phosphotransferase system of Salmonella typhimurium could be inhibited by prior incubation of the cells with glycerol. Inhibition was only observed for glycerol preincubation times longer than 45 s and required the preinduction of both the glucose and the glycerol-catabolizing systems. Larger extents of inhibition by glycerol correlated with higher intracellular levels of glycerol kinase when the glp regulon had been induced to different extents. Preincubation with lactate did not inhibit methyl α-D-glucopyranoside uptake significantly, although both lactate and glycerol were oxidized by the cells. The cellular free-energy state of the cells (intracellular [ATP]/[ADP] ratio) was virtually identical for lactate and glycerol preincubation, suggesting that the inhibition of phosphotransferase-mediated uptake was not a metabolic effect. In vitro, phosphotransferase activity was inhibited to a maximal extent of 32% upon titrating cell-free extracts with high concentrations of commercial glycerol kinase. The results show that uptake systems that have hitherto been regarded merely as targets of the phosphotransferase system component IIAGlc also have the capacity themselves to retroinhibit the phosphotransferase system flux, presumably by sequestration of the available IIAGlc, provided that these systems are induced to appropriate levels.Type of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesHeeswijk, Wally C. ; Rabenberg, Maarten ; Westerhoff, Hans V. ; Kahn, Daniel
Oxford, UK : Blackwell Publishing Ltd
Published 1993Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: Regulation of glutamine-synthetase (GS) activity in enteric bacteria involves a complex cascade of events. In response to nitrogen limitation, a transferase catalyses the uridylylation of the PII protein, which in turn stimulates deadenylylation of GS. Deadenylylated GS is the more active form of the enzyme. Here we characterize in detail the genes from Escherichia coli encoding uridylyl-transferase (gInD), the PII protein (glnB), and adenylyl-transferase (glnE). glnD is transcribed from its own promoter, glnE is cotranscribed with another gene, orfXE, whereas glnB is partly cotranscribed with a gene encoding a homologue of the transcription activator NtrC. All three gln regulatory genes were constitutively expressed at a tow level, i.e. their expression was independent of the nitrogen status and the RNA polymerase sigma factor σ;54. We conclude that the functioning of the GS adenylylation cascade is regulated by modulation of the activities of uridylyl-transferase and adenylyl-transferase, rather than by changes in the expression of their genes.Type of Medium: Electronic ResourceURL: -
10Articles: DFG German National LicensesVan Heeswijk, Wally C. ; Hoving, Sjouke ; Molenaar, Douwe ; Stegeman, Brenda ; Kahn, Daniel ; Westerhoff, Hans V.
Oxford BSL : Blackwell Science Ltd
Published 1996Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The PII protein has been considered pivotal to the dual cascade regulating ammonia assimilation through glutamine synthetase activity. Here we show that PII, encoded by the glnB gene, is not always essential; for instance upon ammonia deprivation of a glnB deletion strain, glutamine synthetase can be deadenylylated as effectively as in the wild-type strain. We describe a new operon, glnK amtB, which encodes a homologue of PII and a putative ammonia transporter. We cloned and overexpressed glnK and found that the expressed protein had almost the same molecular weight as PII, reacted with polyclonal PII antibody, and was 67% identical in terms of amino acid sequence with Escherichia coli PII. Like PII, purified GlnK can activate the adenylylation of glutamine synthetase in vitro, and, in vivo, the GlnK protein is uridylylated in a glnD-dependent fashion. Unlike PII, however, the expression of glnK depends on the presence of UTase, nitrogen regulator I (NRI), and absence of ammonia. Because of a NRI and a σN (σ54) RNA polymerase-binding consensus sequence upstream from the glnK gene, this suggests that glnK is regulated through the NRI/NRII two-component regulatory system. Indeed, in cells grown in the presence of ammonia, glutamine synthetase deadenylylation upon ammonia depletion depended on PII. Possible regulatory implications of this conditional redundancy of PII are discussed.Type of Medium: Electronic ResourceURL: -
11Articles: DFG German National LicensesDerOost, John ; Nederkoom, Paul H. J. ; Stouthamer, Adriaan H. ; Westerhoff, Hans V. ; Spanning, Rob J. M.
Oxford, UK : Blackwell Publishing Ltd
Published 1996Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineType of Medium: Electronic ResourceURL: -
12Articles: DFG German National LicensesBeaumont, Hubertus J. E. ; Lens, Sylvia I. ; Reijnders, Willem N. M. ; Westerhoff, Hans V. ; Van Spanning, Rob J. M.
Oxford, UK : Blackwell Science Ltd
Published 2004Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: Production of nitric oxide (NO) and nitrous oxide (N2O) by ammonia (NH3)-oxidizing bacteria in natural and man-made habitats is thought to contribute to the undesirable emission of NO and N2O into the earth's atmosphere. The NH3-oxidizing bacterium Nitrosomonas europaea expresses nitrite reductase (NirK), an enzyme that has so far been studied predominantly in heterotrophic denitrifying bacteria where it is involved in the production of these nitrogenous gases. The finding of nirK homologues in other NH3-oxidizing bacteria suggests that NirK is widespread among this group; however, its role in these nitrifying bacteria remains unresolved. We identified a gene, nsrR, which encodes a novel nitrite (NO2–)-sensitive transcription repressor that plays a pivotal role in the regulation of NirK expression in N. europaea. NsrR is a member of the Rrf2 family of putative transcription regulators. NirK was expressed aerobically in response to increasing concentrations of NO2– and decreasing pH. Disruption of nsrR resulted in the constitutive expression of NirK. NsrR repressed transcription from the nirK gene cluster promoter (Pnir), the activity of which correlated with NirK expression. Reconstruction of the NsrR-Pnir system in Escherichia coli revealed that repression by NsrR was reversed by NO2– in a pH-dependent manner. The findings are consistent with the hypothesis that N. europaea expresses NirK as a defence against the toxic NO2– that is produced during nitrification.Type of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesA functional genomics strategy that uses metabolome data to reveal the phenotype of silent mutationsRaamsdonk, Léonie M. ; Teusink, Bas ; Broadhurst, David ; Zhang, Nianshu ; Hayes, Andrew ; Walsh, Michael C. ; Berden, Jan A. ; Brindle, Kevin M. ; Kell, Douglas B. ; Rowland, Jem J. ; Westerhoff, Hans V. ; van Dam, Karel ; Oliver, Stephen G.
[s.l.] : Nature America Inc.
Published 2001Staff ViewISSN: 1546-1696Source: Nature Archives 1869 - 2009Topics: BiologyProcess Engineering, Biotechnology, Nutrition TechnologyNotes: [Auszug] A large proportion of the 6,000 genes present in the genome of Saccharomyces cerevisiae, and of those sequenced in other organisms, encode proteins of unknown function. Many of these genes are “silent,” that is, they show no overt phenotype, in terms of growth rate or other fluxes, ...Type of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesStaff View
ISSN: 0044-3301Topics: PhilosophyNotes: BERICHTEURL: -
15Articles: DFG German National LicensesStaff View
ISSN: 1546-1696Source: Nature Archives 1869 - 2009Topics: BiologyProcess Engineering, Biotechnology, Nutrition TechnologyNotes: [Auszug] Systems analysis has historically been performed in many areas of biology, including ecology, developmental biology and immunology. More recently, the genomics revolution has catapulted molecular biology into the realm of systems biology. In unicellular organisms and well-defined cell lines of ...Type of Medium: Electronic ResourceURL: -
16Articles: DFG German National LicensesStaff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] RECENT progress in cooling methods have made it possible to obtain temperatures where kT becomes comparable with the energy separation, due to space quantization of nuclear spins in high magnetic fields.1 The nuclei will, under such conditions, occupy the lower levels of space ...Type of Medium: Electronic ResourceURL: -
17Articles: DFG German National LicensesStaff View
ISSN: 0268-1080Topics: MedicineURL: -
18Articles: DFG German National LicensesHellingwerf, Klaas J. ; Postma, Pieter W. ; Tommassen, Jan ; Westerhoff, Hans V.
Oxford, UK : Blackwell Publishing Ltd
Published 1995Staff ViewISSN: 1574-6976Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Abstract: The molecular basis of many forms of signal transfer in living organisms is provided via the transient phosphorylation of regulatory proteins by transfer of phosphoryl groups between these proteins. The dominant form of signal transduction in prokaryotic microorganisms proceeds via so-called two-component regulatory systems. These systems constitute phosphoryl transfer pathways, consisting of two or more components. Most of these pathways are linear, but some converge and some are divergent. The molecular properties of some of the well-characterised representatives of two-component systems comply with the requirements to be put upon the elements of a neural network: they function as logical operators and show the phenomenon of autoamplification. Because there are many phosphoryl transfer pathways in parallel and because there also appears to be cross-talk between these pathways, the total of all two-component regulatory systems in a single prokaryotic cell may show the typical characteristics fo a ‘phospho-neural network’. This may wel lead to signal amplification, associative responses and memory effects, characteristics which are typical for neural networks. One of the main challenges in molecular microbial physiology is to determine the extent of the connectivity of the constituting elements of this presumed ‘phospho-neural network’, and to outline the extent of intelligence-like behaviour this network can generate. Escherichia coli is the organism of choice for this characterization.Type of Medium: Electronic ResourceURL: -
19Articles: DFG German National LicensesKäufer, Norbert ; Altmann, Michael ; Döhren, Hans v.
Oxford, UK : Blackwell Publishing Ltd
Published 1981Staff ViewISSN: 1574-6968Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyType of Medium: Electronic ResourceURL: -
20Articles: DFG German National LicensesStaff View
ISSN: 1574-6968Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Abstract Many areas of microbiology and biotechnology are directly concerned with the isolation, study or engineering of cells capable of (over)producing metabolites of commercial significance. Yet the study, production or improvement of such strains has often been at best semi-empirical. The metabolic control theory developed by Kacser, Burns, Heinrich and Rapoport can provide a rational and quantitative basis for the description and improvement of such processes.Type of Medium: Electronic ResourceURL: