TY - JOUR A1 - Trendelenburg, Michael F. A1 - Scheer, Ulrich A1 - Franke, W. W. T1 - Structural organization of the transcription of ribosomal DNA in oocytes of the house cricket N2 - No abstract available Y1 - 1973 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33113 ER - TY - JOUR A1 - Scheer, Ulrich T1 - Structure of lampbrush chromosome loops during different states of transcriptional activity as visualized in the presence of physiological salt concentrations N2 - Lampbrush chromosomes of amphibian oocytes were isolated in the presence of near-physiological salt concentrations, to preserve their native state, and studied by electron microscopy of ultrathin s~dions. The transcriptional state of the lampbrush chromosomes was experimentally modulated by incubating the oocytes for various time periods in medium containing actinomycin D. The observations show that the structure of the lateral loops changes rapidly in response to alterations in transcriptional activity. During decreasing transcriptional activity and reduced packing density of transcripts, the chromatin axis first condensed into nucleosomes and then into an approximately 30 nm thick higher order chromatin fiber. Packaging of the loop axis into supranucleosomal structures may contribute to the foreshortening and retraction of the loops observed during inhibition of transcription and in later stages of meiotic prophase. The increasing packing density of the DNA during the retraction process of the loops could also be visualized by immunofluorescence microscopy using antibodies to DNA. The dependence of the loop chromatin structure on transcriptional activity is discussed in relation to current views of mechanisms involved in gene activation. KW - lampbrush chromosomes KW - chromatin structure KW - electron microscopy KW - immunofluorescence microscopy KW - DNA antibodies Y1 - 1987 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-39304 ER - TY - JOUR A1 - Reinhard, Matthias A1 - Halbrügge, Maria A1 - Scheer, Ulrich A1 - Wiegand, Christiane A1 - Jockusch, Brigitte M. A1 - Walter, Ulrich T1 - The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts N2 - Vasoactive agents which elevate either cGMP or cAMP inhibit platelet activation by pathways sharing at least one component, the 46/50 kDa vasodilator-stimulated phosphoprotein (V ASP). V ASP is stoichiometrically phosphorylated by both cGMP-dependent and cAMPdependent protein kinases in intact human platelets, and its phosphorylation correlates very well with platelet inhibition caused by cGMP- and cAMP-elevating agents. Here we report that in human platelets spread on glass, V ASP is associated predominantly with the distal parts of radial micro filament bundles and with microfilaments outlining the periphery, whereas less V ASP is associated with a central microfilamentous ring. V ASP is also detectable in a variety of different cell types including fibroblasts and epithelial cells. In fibroblasts, V ASP is concentrated at focal contact areas, along microfilament bundles (stress fibres) in a punctate pattern, in the periphery of protruding lamellae, and is phosphorylated by cGMP- and cAMP-dependent protein kinases in response to appropriate stimuli. Evidence for the direct binding of V ASP to F -actin is also presented. The data demonstrate that V ASP is a novel phosphoprotein associated with actin filaments and focal contact areas, i.e. transmembrane junctions between microfilaments and the extracellular matrix. KW - cAMP / cGMP / cytoskeleton / phosphorylation / protein kinase Y1 - 1992 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-34246 ER - TY - JOUR A1 - Weisenberger, Dieter A1 - Scheer, Ulrich A1 - Benavente, Ricardo T1 - The DNA topoisomerase I inhibitor camptothecin blocks postmitotic reformation of nucleoli in mammmalian cells N2 - No abstract available KW - Cytologie KW - Nucleolus-DNA KW - opoisomerase I KW - camptothecin KW - mitosis Y1 - 1993 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-41434 ER - TY - JOUR A1 - Krohne, Georg A1 - Franke, Werner W. A1 - Scheer, Ulrich T1 - The major polypeptides of the nuclear pore complex N2 - Nuclear envelopes of maturing oocytes of various amphibia contain an unusually high number of pore complexes in very close packing. Consequently, nuclear envelopes , which can be manually isolated in great purity, provide a remarkable enrichment of nuclear pore complex material, relative to membranous and other interporous structures. When the polypeptides of nuclear envelopes isolated from oocytes of Xenopl/s la evis and Triturus alpestris are examined by gel electrophoresis, visualized either by staining with Coomassie blue or by radiotluorography after in vitro reaction with [3H]dansyl chloride , a characteristic pattern is obtained (10 major and 15 minor bands). This polypeptide pattern is radically different from that of the nuclear contents isolated from the same cell. Extraction of the nuclear envelope with high salt concentrations and moderateIy ac tive detergents such as Triton X- 100 results in the removal of membrane material but leaves most of the non-membranous structure of the pore complexes. The dry weight of the pore complex (about 0.2 femtograms) remains essentially unchanged during such extractions as measured by quantitative electron microscopy . The extracted preparations which are highly enriched in nuclear pore complex material contain only two major polypeptide components with apparent molecular weights of 150000 and 73000. Components of such an electrophoretic mobility are not present as major bands , if at all , in nuclear contents extracted in the same way. lt is concluded that these two polypeptides are the major constituent protein(s) of the oocyte nuclear pore complex and are specific for this structure. When nuclear envelopes are isolated from rat liver and extracted with high salt buffers and Triton X- 100 similar bands are predominant, but two additional major components of molecular weights of 78000 and 66000 are also recognized. When the rat liver nuclear membranes are further subfractionated material enriched in the 66000 molecular weight component can be separated from the membrane material, indicating that this is relatively loosely associated material , probably a part of the nuclear matrix . The results suggest that the nuclear pore complex is not only a characteristic ubiquitous structure but also contains similar, if not identical , skeletal proteins that are remarkably re sistant to drastic changes of ionic strength as weil as to treatments with detergents and thiol reagents. Y1 - 1978 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33078 ER - TY - JOUR A1 - Franke, Werner W. A1 - Scheer, Ulrich A1 - Krohne, Georg A1 - Jarasch, Ernst-Dieter T1 - The nuclear envelope and the architecture of the nuclear periphery N2 - No abstract available Y1 - 1981 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33108 ER - TY - JOUR A1 - Scheer, Ulrich A1 - Dabauvalle, Marie-Christine A1 - Merkert, Hilde A1 - Benavente, Ricardo T1 - The nuclear envelope and the organization of the pore complexes N2 - No abstract available Y1 - 1988 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-34275 ER - TY - JOUR A1 - Scheer, Ulrich A1 - Weisenberger, Dieter T1 - The nucleolus N2 - No abstract available Y1 - 1994 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-32037 ER - TY - JOUR A1 - Scheer, Ulrich T1 - The rifamycin derivative AF/013 is cytolytic N2 - No abstract available Y1 - 1975 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-32429 ER - TY - JOUR A1 - Scheer, Ulrich T1 - The ultrastructure of the nuclear envelope of amphibian ooctyes: IV. On the chemical nature of the nuclear pore complex material N2 - In order to investigate the chemical composition of the nuclear pore complexes isolated nuclei from mature Xenopus laevis oocytes were manually fractioned into nucleo· plasmic aggregates and the nuclear envelopes. The whole isolation procedure takes no more than 60- 90 sec, and the pore complexes of the isolated envelopes are well preserved as demonstrated by electron microscopy. Minor nucleoplasmic and cytoplasmic contaminations associated with the isolated nuclear envelopes were determined with electron microscopic morphometry and were found to be quantitatively negligible as far as their mass and nucleic acid content is concerned. The RNA content of the fractions was determined by direct phosphorus analysis after differential alkaline hydrolysis. Approximately 9% of the total nuclear RNA of the mature Xenopus egg was found to be attached to the nuclear envelope. The nonmembranous elements of one pore complex contain 0.41 X 10- 16 g RNA. This value agrees well with the content estimated from morphometric data. The RNA package density in the pore complexes (270 X 10- 15 g/fJ-3) is compared with the nucleolar, nucleoplasmic and cytoplasmic RNA concentration and is discussed in context with the importance of the pore complexes for the nucleo-cytoplasmic transport of RNA-containing macromolecules. Additionally, the results of the chemical analyses as well as of the 3H-actinomycin D autoradiography and of the nucleoprotein staining method of Bernhard (1969) speak against the occurence of considerable amounts of DNA in the nuclear pore complex structures. KW - Nuclear envelope KW - Amphibian oocytes KW - Nuclear pore complex KW - Chemical nature KW - Electron microscopy Y1 - 1972 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-39500 ER -