@article{TrendelenburgScheerFranke1973,
  author    = {Trendelenburg, Michael F. and Scheer, Ulrich and Franke, W. W.},
  title     = {Structural organization of the transcription of ribosomal DNA in oocytes of the house cricket},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33113},
  year      = {1973},
  abstract  = {No abstract available},
  language  = {en}
}
@article{Scheer1987,
  author    = {Scheer, Ulrich},
  title     = {Structure of lampbrush chromosome loops during different states of transcriptional activity as visualized in the presence of physiological salt concentrations},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39304},
  year      = {1987},
  abstract  = {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.},
  language  = {en}
}
@misc{ScheerThiryGoessens1993,
  author    = {Scheer, Ulrich and Thiry, Marc and Goessens, Guy},
  title     = {Structure, function and assembly of the nucleolus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32057},
  year      = {1993},
  abstract  = {No abstract available},
  language  = {en}
}
@incollection{ScheerFranke1974,
  author    = {Scheer, Ulrich and Franke, Werner W.},
  title     = {Structures and functions of the nuclear envelope},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39777},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1974},
  abstract  = {No abstract available},
  subject      = {Zellkern},
  language  = {en}
}
@inproceedings{FrankeZentgrafScheer1978,
  author    = {Franke, Werner W. and Zentgraf, Hanswalter and Scheer, Ulrich},
  title     = {Supranucleosomal and non-nucleosomal chromatin configurations},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39447},
  year      = {1978},
  abstract  = {A significant contribution to the understanding of chromatin organization was the d iscovery of the nucleosome as a globular repeating unit of the package of DNA (Hewish and Burgoyne, 1973; Woodcock, 1973; Kornberg, 1974; Olins and Olins, 1974; for review see Oudet et al., 1978 a) . In accord with the original definition and in ag reement with most workers in this field of research we identify a nucleosome as a spheric alor slightly oblate gr anular particle 10-13 nm in diameter, containing about 200 base pairs of DNA and two of each of the four his tones H2a, H2b, H3 and H4. It is this structure in which the bulk of the nuclear chroma tin is organized in most eukaryotic cells, with the exception of the dinofl age llates (Rae and Steele, 1977; dinofl agellate DNA, however, c an be packed into nucleosoma l structures in vitro by addition of the appropriate amounts of histones;the same reference). Although it seems clear from the work reported that condensed and transcriptiona lly inactive chroma tin is contained in nucleosomes as the principle for first order p acking of DNA there are two important questions onto which we are focusing in the present study: ( i ) What is the higher order of p a cking present in - and perhaps typical-of - the condensed sta te of chromatin, and (ii) what is the specific form of arrangement of transcriptionally a ctive chromatin?},
  language  = {en}
}
@article{WeisenbergerScheerBenavente1993,
  author    = {Weisenberger, Dieter and Scheer, Ulrich and Benavente, Ricardo},
  title     = {The DNA topoisomerase I inhibitor camptothecin blocks postmitotic reformation of nucleoli in mammmalian cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41434},
  year      = {1993},
  abstract  = {No abstract available},
  subject      = {Cytologie},
  language  = {en}
}
@article{KrohneFrankeScheer1978,
  author    = {Krohne, Georg and Franke, Werner W. and Scheer, Ulrich},
  title     = {The major polypeptides of the nuclear pore complex},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33078},
  year      = {1978},
  abstract  = {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.},
  language  = {en}
}
@article{FrankeScheerKrohneetal.1981,
  author    = {Franke, Werner W. and Scheer, Ulrich and Krohne, Georg and Jarasch, Ernst-Dieter},
  title     = {The nuclear envelope and the architecture of the nuclear periphery},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33108},
  year      = {1981},
  abstract  = {No abstract available},
  language  = {en}
}
@article{ScheerDabauvalleMerkertetal.1988,
  author    = {Scheer, Ulrich and Dabauvalle, Marie-Christine and Merkert, Hilde and Benavente, Ricardo},
  title     = {The nuclear envelope and the organization of the pore complexes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34275},
  year      = {1988},
  abstract  = {No abstract available},
  language  = {en}
}
@book{KartenbeckZentgrafScheeretal.1971,
  author    = {Kartenbeck, J. and Zentgraf, H. and Scheer, Ulrich and Franke, Werner W.},
  title     = {The nuclear envelope in freeze-etching},
  isbn      = {3-540-05538-X},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40534},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1971},
  abstract  = {No abstract available},
  subject      = {Anatomie},
  language  = {en}
}