Search Results - (Author, Cooperation:M. Krause)
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1Schmidt, S., Linge, A., Zwanenburg, A., Leger, S., Lohaus, F., Krenn, C., Appold, S., Gudziol, V., Nowak, A., von Neubeck, C., Tinhofer, I., Budach, V., Sak, A., Stuschke, M., Balermpas, P., Rödel, C., Bunea, H., Grosu, A.-L., Abdollahi, A., Debus, J., Ganswindt, U., Belka, C., Pigorsch, S., Combs, S. E., Mönnich, D., Zips, D., Baretton, G. B., Buchholz, F., Baumann, M., Krause, M., Löck, S., for the DKTK-ROG
The American Association for Cancer Research (AACR)
Published 2018Staff ViewPublication Date: 2018-03-16Publisher: The American Association for Cancer Research (AACR)Print ISSN: 1078-0432Electronic ISSN: 1557-3265Topics: MedicinePublished by: -
2Sardi, M., Krause, M., Heilberger, J., Gasch, A. P.
Genetics Society of America (GSA)
Published 2018Staff ViewPublication Date: 2018-12-11Publisher: Genetics Society of America (GSA)Electronic ISSN: 2160-1836Topics: BiologyPublished by: -
3Lenczuk, D., Zinke-Cerwenka, W., Greinix, H., Wölfler, A., Prattes, J., Zollner-Schwetz, I., Valentin, T., Lin, T. C., Meinitzer, A., Hoenigl, M., Krause, R.
The American Society for Microbiology (ASM)
Published 2018Staff ViewPublication Date: 2018-05-26Publisher: The American Society for Microbiology (ASM)Print ISSN: 0066-4804Electronic ISSN: 1098-6596Topics: BiologyMedicinePublished by: -
4Bierbach, D., Landgraf, T., Romanczuk, P., Lukas, J., Nguyen, H., Wolf, M., Krause, J.
Royal Society
Published 2018Staff ViewPublication Date: 2018-08-09Publisher: Royal SocietyElectronic ISSN: 2054-5703Topics: Natural Sciences in GeneralKeywords: robotics, biomimetics, cognitionPublished by: -
5Andrea Kadović, Sebastian M. Krause, Guido Caldarelli, and Vinko Zlatic
American Physical Society (APS)
Published 2018Staff ViewPublication Date: 2018-12-11Publisher: American Physical Society (APS)Print ISSN: 1539-3755Electronic ISSN: 1550-2376Topics: PhysicsKeywords: Networks and Complex SystemsPublished by: -
6R. Diehl ; T. Siegert ; W. Hillebrandt ; S. A. Grebenev ; J. Greiner ; M. Krause ; M. Kromer ; K. Maeda ; F. Ropke ; S. Taubenberger
American Association for the Advancement of Science (AAAS)
Published 2014Staff ViewPublication Date: 2014-08-02Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
7S. Fan ; R. Baets ; A. Petrov ; Z. Yu ; J. D. Joannopoulos ; W. Freude ; A. Melloni ; M. Popovic ; M. Vanwolleghem ; D. Jalas ; M. Eich ; M. Krause ; H. Renner ; E. Brinkmeyer ; C. R. Doerr
American Association for the Advancement of Science (AAAS)
Published 2012Staff ViewPublication Date: 2012-01-10Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
8Staff View
Type of Medium: articlePublication Date: 2003Keywords: Pädagogik ; Diagnose ; Beruf ; Psychologe ; Qualität ; Standard ; Testen ; ArztIn: Frühförderung interdisziplinär, Bd. 22 (2003) H. 1, S. 2, 0721-9121Language: German -
9Staff View
Type of Medium: OnlinePublication Date: 2015Keywords: Multimedia ; Lernumgebung ; Chemie ; Reise ; Industrie ; NordwestdeutschlandIn: Bernholt, Sascha (Hrsg.), Heterogenität und Diversität-Vielfalt der Voraussetzungen im naturwissenschaftlichen Unterricht., Kiel: IPN (2015), S. 552-554, 978-3-89088-362-5Language: German -
10Krause, M. [Verfasser] ; Ostersehlt, D. [Verfasser] ; Mehrwald, T. [Verfasser] ; Runden, H.-J. [Verfasser] ; Mroske, S. [Verfasser] ; Eilks, I. [Verfasser]
Published 2014Staff ViewType of Medium: OnlinePublication Date: 2014Keywords: Lehrer ; Experiment ; Projekt ; Naturwissenschaftlicher Unterricht ; Modell ; BremenIn: Bernholt, Sascha (Hrsg.), Naturwissenschaftliche Bildung zwischen Science- und Fachunterricht., Kiel: IPN (2014), S. 354-356, 978-3-89088-361-8Language: German -
11Staff View
Type of Medium: OnlinePublication Date: 2015Keywords: Selbstkonzept ; Digitale Medien ; Lehrer ; Chemieunterricht ; NutzungIn: Bernholt, Sascha (Hrsg.), Heterogenität und Diversität-Vielfalt der Voraussetzungen im naturwissenschaftlichen Unterricht., Kiel: IPN (2015), S. 681-683, 978-3-89088-362-5Language: German -
12Kleint, C. A. ; Krause, M. K. ; Höhne, R. ; Walter, T. ; Semmelhack, H. C. ; Lorenz, M. ; Esquinazi, P.
[S.l.] : American Institute of Physics (AIP)
Published 1998Staff ViewISSN: 1089-7550Source: AIP Digital ArchiveTopics: PhysicsNotes: Magnetic exchange anisotropy has been studied in epitaxial Fe3O4 based bilayers grown by pulsed laser deposition on MgO substrates. Measurements of the exchange biasing of the Fe3O4 magnetization curves were performed on (100)- and (111)-oriented Fe3O4 (20 nm)/CoO (20 nm) bilayers and (100)-oriented Co0.16Fe2.84O4 (190 nm)/Fe3O4 (40–370 nm) bilayers. The effective exchange bias field Heb and coupling energy were found to be 10–102 kA/m and 1–2 mJ/m2, respectively. The dependence of Heb on the thickness d of the soft magnetic component (magnetite) of the cobalt ferrite/magnetite bilayer Heb∼1/d is found to be in agreement with the predictions of a Stoner–Wohlfarth-type model. The order of magnitude and the temperature dependence of Heb for the Fe3O4/CoO bilayers are similar to those of bilayers prepared by molecular beam epitaxy. © 1998 American Institute of Physics.Type of Medium: Electronic ResourceURL: -
13Krause, M. ; Weindler, J. ; Spang, S. ; Ruprecht, K. W.
Oxford : Blackwell Science Ltd
Published 1999Staff ViewISSN: 1365-2044Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineType of Medium: Electronic ResourceURL: -
14Krause, M. ; Hulman, M. ; Kuzmany, H.
College Park, Md. : American Institute of Physics (AIP)
Published 1999Staff ViewISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: Raman scattering and infrared absorption of the C84 and Sc2@C84 isomers 23:D2d were studied at room temperature and 95 K. The results are compared to the response of pristine and doped C60. According to the lower symmetry and the higher number of atoms C84 exhibits much more vibrational modes than C60, in particular at wave numbers above 500 cm−1. For lower energies the vibrational structure of C84 resembles a downshifted and split C60 spectrum. After the encapsulation of two scandium atoms the overall vibrational structure and the number of C84 modes was preserved as a result of the similar geometric structure. From the very good correlation of the C84 and Sc2@C84 cage modes metal to fullerene charge transfer induced shifts could be analyzed. The lines were found less shifted compared to the C60 modes in exohedral doped A6C60 (A=K,Rb,Cs). Increased line widths of low energy cage modes were attributed to an additional intramolecular relaxation channel related to the dynamics of the encapsulated scandium ions. A set of nine new lines with almost complementary Raman and infrared intensities was found for Sc2@C84 below 200, at 246 and at 259 cm−1, and attributed to Sc–C84 vibrations. These vibrations were further identified as Sc–C84 stretching and Sc–C84 deformation modes. The Sc–C84 valence force constant of 1.19 N/cm was derived with a linear three-mass oscillator model for Sc2@C84. Both, the charge transfer induced line shifts and the Sc–C84 valence force constant indicate an effective transfer of approximately two electrons per scandium to the carbon cage. This is in agreement with an electronic state (Sc2.2+)2@C84〈sup ARRANGE="STAGGER"〉4.4− previously proposed on the basis of x-ray powder diffraction, x-ray photoemission spectroscopy (XPS), and quantum chemical calculations. The unexpected high number of Sc–C84 vibrations is attributed to crystal field and factor group splitting. © 1999 American Institute of Physics.Type of Medium: Electronic ResourceURL: -
15Structure and stability of endohedral fullerene Sc3NC80: A Raman, infrared, and theoretical analysisStaff View
ISSN: 1089-7690Source: AIP Digital ArchiveTopics: PhysicsChemistry and PharmacologyNotes: Structure and stability of endohedral fullerene Sc3N@C80 were studied by temperature-dependent Raman and infrared spectroscopy as well as by quantum-chemical [density-functional-based tight-binding] calculations. The material showed a remarkable thermal stability up to 650 K. By both theory and experiment, translational and rotational Sc3N modes were found. These modes give a direct evidence for the formation of a Sc3N–C80 bond which induces a significant reduction of the ideal Ih–C80 symmetry. From their splitting pattern a crystal structure with more than one molecule in the unit cell is proposed. According to our results: (i) a significant charge transfer from the Sc3N cluster to the C80 cage; (ii) the strength of three Sc–N bonds; (iii) the chemical bond between triscandium nitride cluster and C80 cage; and (iv) a large HOMO–LUMO gap are responsible for the high stability and abundance of Sc3N@C80. © 2001 American Institute of Physics.Type of Medium: Electronic ResourceURL: -
16Staff View
ISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The entire nucleotide sequence of the Bacillus brevis grsB gene encoding the gramicidin S synthetase 2, which activates and condenses the four amino acids proline, valine, ornithine and leucine has been determined. The gene contains an open reading frame of 13359bp which encodes a protein of 4453 amino acids with a predicted Mr of 510287. The gene is located within the gramicidin S biosynthetic operon, also containing the genes grsT and grsA, whose nucleotide sequences have been determined previously. Within the GrsB amino acid sequence four conserved and repeated domains of about 600 amino acids (45–50% identity) have been identified. The four domains are separated by non-homologous sequences of about 500 amino acids. The domains also share a high degree of similarity (20–70%) with eight peptide synthetases of bacterial and fungal origin as well as with conserved sequences of nine other adenylate-forming enzymes of diverse origin. On the basis of sequence homology and functional similarities, we infer that those enzymes share a common evolutionary origin and present a phylogenetic tree for this superfamily of domain-bearing enzymes.Type of Medium: Electronic ResourceURL: -
17Staff View
ISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineType of Medium: Electronic ResourceURL: -
18Homologous DNA sequences on the virulence plasmids of pathogenic Yersinia and Salmonella dublin LaneStaff View
ISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: Yersinia and Salmonella harbour plasmids that encode traits important for virulence, enabling both pathogenic genera to survive and grow in cells of the reticulo-endothelial organs during systemic infections. We have detected DNA homology between the Salmonella dublin virulence plasmid pSDL2 and the plasmids of the pathogenic Yersinia species pestis, pseudotuberculosis, and enterocolitica. Three regions of pSDL2 were found to share homology with the virulence plasmid pIB1 of Yersinia pseudotuberculosis. Two separate hybridizing segments mapped within the previously characterized 6.4 kb vir region of pSDL2 in the Sal1 B fragment. The third homologous region involved the regions of plB1, which hybridized to the Sal1 C2 fragment of pSDL2. The virulence plasmid pCD1 from Y. pestis showed similar homology with the three regions of pSDL2. Homologies to the vir and Sal1 C2 regions of pSDL2 were also found on plasmids from Yersinia enterocolitica serotypes 0:9, 0:3 and 0:5, 27. The discovery of separate homologous regions on the virulence plasmids of Salmonella and Yersinia suggests a distant evolutionary relationship.Type of Medium: Electronic ResourceURL: -
19Krause, M. ; Roudier, C. ; Fierer, J. ; Harwood, J. ; Guiney, D.
Oxford, UK : Blackwell Publishing Ltd
Published 1991Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: The virulence properties of various non-typhoid Salmonella serotypes depend on the presence of large plasmids 60–100 kb in size. We have shown previously that the virulence region on the 80 kb plasmid pSDL2 of Salmonella dublinLane maps within a 14kb SalI fragment. In this report we show that an 8.2kb region within this fragment is sufficient to express lethal disease in BALB/c mice. Sequence analysis of this segment revealed six sequential open reading frames designated vsdA–F, which encode putative proteins of 13–65kDa. Deletion analysis and location of Tn5-oriT inserts which abolish virulence suggest that vsdA, vsdC, vsdD and vsdE are essential for virulence expression. Downstream of vsdF we discovered a locus involved in stable plasmid maintenance. Deletion of that region resulted in plasmid multimerization and instability.Type of Medium: Electronic ResourceURL: -
20Staff View
ISSN: 0020-1693Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Chemistry and PharmacologyType of Medium: Electronic ResourceURL: