@article{DerksenTrendelenburgScheeretal.1973, author = {Derksen, J. and Trendelenburg, Michael F. and Scheer, Ulrich and Franke, Werner W.}, title = {Spread chromosomal nucleoli of Chironomus salivary glands}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32209}, year = {1973}, abstract = {No abstract available}, language = {en} } @article{DabauvalleSchulzScheeretal.1988, author = {Dabauvalle, Marie-Christine and Schulz, Barbara and Scheer, Ulrich and Peters, Reiner}, title = {Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34288}, year = {1988}, abstract = {No abstract available}, language = {en} } @misc{DabauvalleScheer1991, author = {Dabauvalle, Marie-Christine and Scheer, Ulrich}, title = {Assembly of nuclear pore complexes in Xenopus egg extract}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41194}, year = {1991}, abstract = {No abstract available}, language = {en} } @article{DabauvalleLoosScheer1990, author = {Dabauvalle, Marie-Christine and Loos, Karin and Scheer, Ulrich}, title = {Identification of a soluble precursor complex essential for nuclear pore assembly in vitro}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32801}, year = {1990}, abstract = {No abstract available}, language = {en} } @article{DabauvalleLoosMerkertetal.1991, author = {Dabauvalle, Marie-Christine and Loos, Karin and Merkert, Hilde and Scheer, Ulrich}, title = {Spontaneous assembly of pore complex-containing membranes ("Annulate lamellae") in Xenopus egg extract in the absence of chromatin}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32797}, year = {1991}, abstract = {No abstract available}, language = {en} } @inproceedings{DabauvalleWilkenEwaldetal.1994, author = {Dabauvalle, M.-C. and Wilken, N. and Ewald, A. and Kuhbier, A. and Sen{\´e}cal, J.-L. and Scheer, Ulrich}, title = {Nuclear pore complex structure analyzed by immunogold EM with human autoantibodies}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39439}, year = {1994}, abstract = {No abstract available}, language = {en} } @article{BonaScheerBautz1981, author = {Bona, Marion and Scheer, Ulrich and Bautz, Ekkehard K. F.}, title = {Antibodies to RNA polymerase II (B) inhibit transcription in lampbrush chromosomes after microinjection into living amphibian oocytes}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33128}, year = {1981}, abstract = {Antibodies directed against RNA polymerase II (B) from Drosophila melanogaster were obtained from rabbit sera and, as monoclonal immunoglobulins, from mouse hybridomas and shown to cross-react with the amphibian enzyme protein. Localization by indirect immunofluorescence microscopy revealed the association of this enzyme with chromatin of interphase nuclei of amphibian cells and its absence in nucleoli. Purified immunoglobulins were microinjected in to nuclei ofliving vitellogenic oocytes of Ple1lrodeles waltlii and X enopus laevis and their effects on transcriptional processes were monitored by biochemical and light and electron microscopic stud ies. RNA polymerase II antibodies from rabbit sera caused a rapid and almost complete release of nascent transcripts from the chromatin axis of the loops of lampbrush chromosomes, followed by collapse of the loops and their retraction on the main chromosome axis. Monoclonal murine antibodies to the Iarge RNA polymerase II subunits also inhibited transcription in chromosome Ioops but appeared to inhibit initiation rather than elongation events. Activities of class land III RNA polymerases were not significantly affected by injection of antibodies to polymerase II, indicating immunological differences between the three RNA polymerases. The potential value of the in vitro test system described , as a very sensitive assay for detecting proteins involved in transcription in living cells, is discussed. 1}, language = {en} } @article{BenaventeSchmidtZachmannHuegleDoerretal.1988, author = {Benavente, Ricardo and Schmidt-Zachmann, Marion S. and H{\"u}gle-D{\"o}rr, B. and Reimer, G. and Rose, K. M. and Scheer, Ulrich}, title = {Identification and definition of nucleolus-related fibrillar bodies in micronucleated cells}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39423}, year = {1988}, abstract = {Small nucleolus-related bodies which occur in the nUcleoplasm of " micronuclei" lacking nucleolar organizers have been studied by immunofluorescence microscopy. These bodies stained specifically with three different antibodies directed against proteins that are normally associated with the dense fibrillar component of functional nucleoli, but not with antibodies specific for certain proteins of the granular component or the fibrillar centers. Our data show that, in the absence of rRNA genes, the various constituent proteins characteristic of the dense fibrillar component spontaneously assemble into spherical entities but that the subsequent fusion of these bodies into larger structures is prevented in these micronuclei. The similarity between these nucleolus-related bodies of micronuclei and the prenucleolar bodies characteristic of early stages of nucleologenesis during mitotic telophase is discussed.}, language = {en} } @article{BenaventeScheerChaly1989, author = {Benavente, Ricardo and Scheer, Ulrich and Chaly, Nathalie}, title = {Nucleocytoplasmic sorting of macromolecules following mitosis: fate of nuclear constituents after inhibition of pore complex function}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40777}, year = {1989}, abstract = {PtK2 cells in which pore complex-mediated transport is blocked by microinjection early in mitosis of a monoclonal antibody (specific for an Mr 68000 pore complex glycoprotein) or of wheat germ agglutinin (WGA) complete cytokinesis. However, their nuclei remain stably arrested in a telophase-like organization characterized by highly condensed chromatin and the absence of nucleoli, indicating a requirement for pore-mediated transport for the reassembly of interphase nuclei. We have now examined this requirement more closely by monitoring the behavior of individual nuclear macromolecules in microinjected cells using immunofluorescence microscopy and have investigated the effect of microinjecting the antibody or WGA on cellular ultrastructure. The absence of nuclear transport did not affect the sequestration into daughter nuclei of components such as DNA, DNA topoisomerase I and the nucleolar protein fibrillarin that are carried through mitosis on chromosomes. On the other hand, lamins, snRNAs and the p68 pore complex glycoprotein, all cytoplasmic during mitosis, remained largely cytoplasmic in the telophase-arrested cells. Electron microscopy showed the nuclei to be surrounded by a doublelayered membrane with some inserted pore complexes. In addition, however, a variety of membranous structures with associated pore complexes was regularly noted in the cytoplasm, suggesting that chromatin may not be essential for the postmitotic formation of pore complexes. We propose that cellular compartmentalization at telophase is a two-step process. First, a nuclear envelope tightly encloses the condensed chromosomes, excluding non-selectively all macromolecules not associated with the chromosomes. Interphase nuclear organization is then progressively restored by selective pore complex-mediated uptake of nuclear proteins from the cytoplasm.}, subject = {Cytologie}, language = {en} } @article{BenaventeRoseReimeretal.1987, author = {Benavente, Ricardo and Rose, Kathleen M. and Reimer, Georg and H{\"u}gle-D{\"o}rr, Barbara and Scheer, Ulrich}, title = {Inhibition of nucleolar reformation after microinjection of antibodies to RNA polymerase I into mitotic cells}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33247}, year = {1987}, abstract = {The formation of daughter nuclei and the reformation of nucleolar structures was studied after microinjection of antibodies to RNA polymerase I into dividing cultured cells (PtK2). The fate of several nucleolar proteins representing the three main structural subcomponents of the nucleolus was examined by immunofluorescence and electron microscopy. The results show that the RNA polymerase I antibodies do not interfere with normal mitotic progression or the early steps of nucleologenesis, i.e. , the aggregation of nucleolar material into prenucleolar bodies. However,they inhibit the telophasic coalescence of the prenucleolar bodies into the chromosomal nucleolar organizer regions, thus preventing the formation of new nucleoli. These prenucleolar bodies show a fibrillar organization that also compositionally resembles the dense fibrillar component of interphase nucleoli . We conclude that during normal nucleologenesis the dense fibrillar component forms from preformed entities around nucleolar organizer regions, and that this association seems to be dependent on the presence of an active form of RNA polymerase I.}, language = {en} }