@article{Scheer2018,
  author    = {Scheer, Ulrich},
  title     = {Boveri's research at the Zoological Station Naples: Rediscovery of his original microscope slides at the University of W{\"u}rzburg},
  series = {Marine Genomics},
  volume    = {40},
  journal   = {Marine Genomics},
  doi       = {10.1016/j.margen.2018.01.003},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-228453},
  pages     = {1-8},
  year      = {2018},
  abstract  = {Eric Davidson once wrote about Theodor Boveri: "From his own researches, and perhaps most important, his generalized interpretations, derive the paradigms that underlie modern inquiries into the genomic basis of embryogenesis" (Davidson, 1985). As luck would have it, the "primary data" of Boveri's experimental work, namely the microscope slides prepared by him and his wife Marcella during several stays at the Zoological Station in Naples (1901/02, 1911/12 and 1914), have survived at the University of Wurzburg. More than 600 slides exist and despite their age they are in a surprisingly good condition. The slides are labelled and dated in Boveri's handwriting and thus can be assigned to his published experimental work on sea urchin development. The results allowed Boveri to unravel the role of the cell nucleus and its chromosomes in development and inheritance. Here, I present an overview of the slides in the context of Boveri's work along with photographic images of selected specimens taken from the original slides. It is planned to examine the slides in more detail, take high-resolution focal image series of significant specimens and make them online available.},
  language  = {en}
}
@article{ScheerWeisenberger1994,
  author    = {Scheer, Ulrich and Weisenberger, Dieter},
  title     = {The nucleolus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32037},
  year      = {1994},
  abstract  = {No abstract available},
  language  = {en}
}
@article{Scheer1994,
  author    = {Scheer, Ulrich},
  title     = {Harold Garnet Callan 1917-1993},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-80789},
  year      = {1994},
  abstract  = {Professor Harold Gamet Callan, honorary member of the German Society for Cell Biology, died on the 3rd November 1993, at the age of 76. His name is inseparably connected with lampbrush chromosomes, the most spectacular and aesthetically ailuring form of chromosomes, which occupied the major part of his scientific career. " Mick" Callan's pioneering studies led to fruitful new concepts, served as a building block for many subsequent studies by others, and contributed enormously to our current understanding of chromosome organization and activity ...},
  subject      = {Harold Garnet Callan},
  language  = {en}
}
@article{WilkenKossnerSenecaletal.1993,
  author    = {Wilken, Norbert and Kossner, Ursula and Sen{\´e}cal, Jean-Luc and Scheer, Ulrich and Dabauvalle, Marie-Christine},
  title     = {Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32049},
  year      = {1993},
  abstract  = {No abstract available},
  language  = {en}
}
@article{FischerHockScheer1993,
  author    = {Fischer, Dagmar and Hock, Robert and Scheer, Ulrich},
  title     = {DNA Topoisomerase II is not detectable on lampbrush chromosomes but enriched in the amplified nucleoli of xenopus oocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-32654},
  year      = {1993},
  abstract  = {In somatic cells DNA topoisomerase II (topo II) is thought to be involved in the domain Organization of the genome by anchoring the basis of chromatin loops to a chromosomal scafFold. Lampbrush chromosomes of am-phibian oocytes directly display this radial loop Organization in cytological preparations. In order to find out whether topo II may play a role in the Organization of these meiotic chromosomes, we performed immunofluorescence studies using antibodies against Xenopus topo II. Our results indicate that topo II is apparently absent from lampbrush chromosomes and is hence unlikely to act as a "fastener" of the numerous lateral chromosomal loops. Topo II was, however, enriched in the amplified nucleoli of Xenopus oocytes.},
  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{HockMoormannFischeretal.1993,
  author    = {Hock, Robert and Moormann, Antoon and Fischer, Dagmar and Scheer, Ulrich},
  title     = {Absence of somatic histone H1 in oocytes and preblastula embryos of Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41350},
  year      = {1993},
  abstract  = {Available data on the occurrence and expression of somatic histone HI during oogenesis and early embryogenesis of Xenopus laevis are contradictory. In particular the reported presence of a large storage pool of histone HIA in oocytes is difficult to reconcile with the high transcriptional activity of all gene classes in this specific cell type. In the present study we have used polyclonal antibodies raised against somatic Xenopus histone HI (HIA and HIA/B) for combined immunoblotting experiments to quantitate HI pools and immunolocalization studies to visualize chromosome- bound HI. Both approaches failed to detect soluble or chromosomal histone HI in vitellogenic oocytes, eggs, and cleavage-stage embryos up to early blastula. In addition, chromatin assembled in Xenopus egg extract was also negative for histone HI as revealed by immunofluorescence microscopy. Lampbrush chromosomes not only lacked histone HI but also the previously identified histone HI-like B4 protein (Smith et al., 1988, Genes Dev. 2,1284-1295). In contrast, chromosomes of eggs and early embryos fluoresced brightly with anti-B4 antibodies. Our results lend further support to the view that histone HI expression is developmentally regulated during Xenopus oogenesis and embryogenesis similar to what is known from other species.},
  language  = {en}
}
@article{BellDabauvalleScheer1992,
  author    = {Bell, Peter and Dabauvalle, Marie-Christine and Scheer, Ulrich},
  title     = {In vitro assembly of prenucleolar bodies in Xenopus egg extract},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34233},
  year      = {1992},
  abstract  = {Nuclei assembled in Xenopus egg extract from purified DNA or chromatin resemble their natural counterparts in a number of structural and functional features. However, the most obvious structural element of normal interphase nuclei, the nucleolus, is absent from the in vitro reconstituted nuclei. By EM, cytological silver staining, and immunofluorescence microscopy employing antibodies directed against various nucleolar components we show that nuclei assembled in vitro contain numerous distinct aggregates that resemble prenucleolar bodies (PNBs) by several criteria. Formation of these PNB-like structures requires pore complex-mediated nuclear transport of proteins but is independent of the genetic content of the in vitro nuclei as well as transcriptional and translational events. Our data indicate that nuclei assembled in vitro are capable of initiating early steps of nucleologenesis but that the resulting PNBs are unable to fuse with each other, probably due to the absence of a functional nucleolus organizer. With appropriate modifications, this experimental system should be useful to define and analyze conditions promoting the site-specific assembly of PNBs into a coherent nucleolar body.},
  language  = {en}
}
@article{ReinhardHalbrueggeScheeretal.1992,
  author    = {Reinhard, Matthias and Halbr{\"u}gge, Maria and Scheer, Ulrich and Wiegand, Christiane and Jockusch, Brigitte M. and Walter, Ulrich},
  title     = {The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34246},
  year      = {1992},
  abstract  = {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.},
  language  = {de}
}
@article{FischerWeisenbergerScheer1992,
  author    = {Fischer, D. and Weisenberger, D. and Scheer, Ulrich},
  title     = {In situ hybridization of DIG-labeled rRNA probes to mouse liver ultrathin sections},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-69458},
  year      = {1992},
  abstract  = {No abstract available.},
  subject      = {Hybridisierung <Biologie>},
  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}
}
@article{ThiryScheerGoessens1991,
  author    = {Thiry, Marc and Scheer, Ulrich and Goessens, Guy},
  title     = {Localization of nucleolar chromatin by immunocytochemistry and in situ hybridization at the electron microscopic level},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39289},
  year      = {1991},
  abstract  = {Nucleoli are the morphological expression of the activity of a defined set of chromosomal segments bearing rRNA genes. The topological distribution and composition of the intranucleolar chromatin as well as the definition of nucleolar structures in which enzymes of the rDNA transcription machinery reside have been investigated in mammalian cells by various immunogold labelling approaches at the ultrastructural level. The precise intranucleolar location of rRNA genes has been further specified by electron microscopic in situ hybridization with a non-autoradiographic procedure. Our results indicate that the fibrillar centers are the sole nucleolar structures where rDNA, core histones, RNA polymerase I and DNA to po isomerase I are located together. Taking into account the potential value and limitations of immunoelectron microscopic techniques, we propose that transcription of the rRNA genes takes place within the confines of the fibrillar centers, probably close to the boundary regions to the surrounding dense fibrillar component.},
  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{BenaventeDabauvalleScheeretal.1989,
  author    = {Benavente, Ricardo and Dabauvalle, Marie-Christine and Scheer, Ulrich and Chaly, Nathalie},
  title     = {Functional role of newly formed pore complexes in postmitotic nuclear reorganization},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40754},
  year      = {1989},
  abstract  = {Many nuclear proteins are released into the cytoplasm at prometaphase and are transported back into the daughter nuclei at the end of mitosis. To determine the role of this reentry in nuclear remodelling during early interphase, we experimentally manipulated nuclear protein uptake in dividing cells. Recently we and others have shown that signal-dependent, pore complex-mediated uptake of nuclear protein is blocked in living cells on microinjection of the lectin wheat germ agglutinin (WGA), or of antibodies such as PI1 that are directed against WGA-binding pore complex glycoproteins. In the present study, we microinjected mitotic PtKz cells with WGA or antibody PIt and followed nuclear reorganization of the daughter cells by immunofluorescence and electron microscopy. The inhibitory effect on nuclear protein uptake was monitored by co-injection of the karyophilic protein nucleoplasmin. When injected by itself early in mitosis, nucleoplasmin became sequestered into the daughter nuclei as they entered telophase. In contrast, nucleoplasmin was excluded from the daughter nuclei in the presence of WGA or antibody PI1 . Although PtKz cells with blocked nuclear protein uptake completed cytokinesis, their nuclei showed a telophaselike organization characterized by highly condensed chromatin surrounded by a nuclear envelope containing a few pore complexes. These findings suggest that pore complexes become functional as early as telophase, in close coincidence with nuclear envelope reformation. They further indicate that the extensive structural rearrangement of the nucleus during the telophase-G1 transition is dependent on the influx of karyophilic proteins from the cytoplasm through the pore complexes, and is not due solely to chromosome- associated components.},
  language  = {en}
}
@article{WeberSchmidtScheer1989,
  author    = {Weber, Thomas and Schmidt, Erwin and Scheer, Ulrich},
  title     = {Mapping of transcription units on Xenopus laevis lampbrush chromosomes by in situ hybridization with biotin-labeled cDNA probes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40763},
  year      = {1989},
  abstract  = {A non-radioactive in situ hybridization method is described for the localization of transcription units of defined genes to lateral loops of Xenopus laevis lampbrush chromosomes. Two Xenopus cONA probes were used encoding the nucleolar protein N038/ B23 and cytokeratin 1(8). Both proteins are known to be synthesized in Xenopus oocytes, and Northern blot analysis revealed the presence of the corresponding mRNAs in different oogenic stages. The probes were enzymatically labeled with biotin-dCTP and hybridized to lampbrush chromosomes. The sites of hybridization were detected either by indirect immunofluorescence microscopy using rabbit antibodies against biotin and fluorescein-conjugated antirabbit IgG or enzymatically using peroxidase-conjugated streptavi din. The probe encoding the nucleolar protein hybridized to two sets of lateral loops on different bivalents, the cytokeratin probe to at least four. Our finding that each probe hybridized to more than one chromosomal locus may reflect the tetraploid nature of the Xenopus laevis genome or results from cross-hybridization to other transcriptionally active members of the N038/ B23-nucleoplasmin or the cytokeratin-Iamin gene families. The method described should facilitate further in situ hybridization studies with appropriate genomic clones in order to map specific DNA sequences to defined loop regions and to come to a better understanding of the relationship between loop organization and gene transcription unit.},
  subject      = {Cytologie},
  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{ThiryScheerGoessens1988,
  author    = {Thiry, Marc and Scheer, Ulrich and Goessens, Guy},
  title     = {Immunoelectron microscopic study of nucleolar DNA during mitosis in Ehrlich tumour cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40745},
  year      = {1988},
  abstract  = {In order to investigate the DNA localization within Ehrlich tumor cell nucleoli during mitosis, two recent immunocytochemical methods using either an anti-DNA or an anti-bromodeoxyuridine (BrdU) monoclonal antibody have been applied. In both cases, the immunogold labeling has been performed on ultrathin sections of cells embedded either in Lowicryl K4M or in Epon, respectively. Identical results are observed with both immunocytochemical approaches. In the interphase nucleolus, besides the labeling of the perinucleolar chromatin shell and of its intranucleolar invaginations which penetrate into the nucleolar body and often terminate at the fibrillar centers, a few gold particles are also preferentially found towards the peripheral region of the fibrillar centers. In contrast, the dense fibrillar component and the granular component are never labeled. During mitosis, the fibrillar centers persist at the chromosomal nucleolus organizing regions (NOR's) and can be selectively stained by the silver method. However, these metaphase fibrillar centers are no longer decorated by the DNA- or BrdU antibodies. These results indicate that until the end of prophase, rRNA genes are present inside the fibrillar center material, disappear during metaphase and reappear in reconstituting nucleoli during telophase. Thus, fibrillar centers appear to represent structures sui generis, which are populated by rRNA genes only when the nucleolus is functionally active. In segregated nucleoli after actinomycin D treatment, the DNA labeling is exclusively restricted to the perinucleolar chromatin blocks. These findings also suggest that the DNA content of the fibrillar center material varies according to the rRNA transcription level of the cells. The results are discussed in the light of the present knowledge of the functional organization of the nucleolus.},
  subject      = {Cytologie},
  language  = {en}
}
@article{RoseSzopaHanetal.1988,
  author    = {Rose, Kathleen M. and Szopa, Jan and Han, Fu-Sheng and Cheng, Yung-Chi and Richter, Arndt and Scheer, Ulrich},
  title     = {Association of DNA topoisomerase I and RNA polymerase I: A possible role for topoisomerase I in ribosomal gene transcription},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33901},
  year      = {1988},
  abstract  = {RNA polymerase I preparations purified from a rat hepatoma contained DNA topoisomerase activity. The DNA topoisomerase associated with the polymerase had an Mr of 110000, required Mg2+ but not ATP, and was recognized by anti-topoisomerase I antibodies. When added to RNA polymerase I preparations containing topoisomerase activity, anti-topoisomerase I antibodies were able to inhibit the DNA relaxing activity of the preparation as well as RNA synthesis in vitro. RNA polymerase II prepared by analogous procedures did not contain topoisomerase activity and was not recognized by the antibodies. The topoisomerase I: polymerase I complex was reversibly dissociated by column chromatography on Sephacryl S200 in the presence of 0.25 M (NH4hS04. Topoisomerase I was immunolocalized in the transcriptionally active ribosomal gene complex containing RNA polymerase I in situ. These data indicate that topoisomerase I and RNA polymerase I are tightly complexed both in vivo and in vitro, and suggest a role for DNA topoisomerase I in the transcription of ribosomal genes.},
  language  = {en}
}
@article{ReimerRaskaScheeretal.1988,
  author    = {Reimer, Georg and Raska, Ivan and Scheer, Ulrich and Tan, Eng M.},
  title     = {Immunolocalization of 7-2-ribonucleoprotein in the granular component of the nucleolus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33890},
  year      = {1988},
  abstract  = {Certain autoimmune sera contain antibodies against a nucleolar ribonucleoprotein particle associated with 7-2-RNA (R. Reddy et al. (1983) J. Bioi. Chem . 258, 1383; C. Hashimoto and J. A. Steitz (1983) J. Bioi. Chem. 258, 1379). In this study, we showed by immunofluorescence microscopy that antibodies reactive with 7-2-ribonucleoprotein immunolocalized in the granular regions of actinomycin D and 5,6-dichloro-I-j3-D-ribofuranosylbenzimidazole (DRB)-segregated nucleoli from Vero cells. By electron microscopic immunocytochemistry, antigen-antibody complexes were located in the granular component of transcriptionally active nucleoli from rat liver hepatocytes and HeLa cells. Anti-7- 2-RNP antibodies from two autoimmune sera immunoprecipitated a major protein of Mr 40,000 from e5S] methionine-Iabeled HeLa cell extract. The immunolocalization data suggest that 7-2-ribonucleoprotein may be involved in stages of ribosome biogenesis which take place in the granular component of the nucleolus, i.e., assembly, maturation, and/or transport of preribosomes},
  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{ThiryScheerGoessens1988,
  author    = {Thiry, Marc and Scheer, Ulrich and Goessens, Guy},
  title     = {Localization of DNA within Ehrlich tumour cells nucleoli by immunoelectron microscopy},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39327},
  year      = {1988},
  abstract  = {The distribution of DNA in Ehrlich tumour cell nucleoli was investigated by means of an immunocytochemical approach , involving a monoclonal antibody directed against double- and single-stranded DNA. Immunolabelling was performed . either before or after the embedding process. The postembedding labelling method allows better ultrastructural preservation than the preembedding labelling method. In particular, the various nucleolar components are well preserved and identifiable. In the nucleolus, labelling is particularly concentrated over the perinucleolar chromatin and over its intranucleolar invaginations, which penetrate the nucleolar body and often terminate at the fibrillar centres. In addition, aggregates of gold particles are found in the fibrillar centres, preferentially towards the peripheral regions. By contrast, the dense fibrillar component is completely devoid of labelling. The results seem to indicate that DNA containing the rDNA genes is located in the fibrillar centres, with a preference for the peripheral regions. This finding suggests that transcription of the rDNA genes should occur within the confines of the fibrillar centre, probably close to the boundary region of the surrounding dense fibrillar component. The results are discussed in the light of present knowledge of the functional organization of the nucleolus.},
  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}
}
@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}
}
@article{BenaventeReimerRoseetal.1988,
  author    = {Benavente, Ricardo and Reimer, Georg and Rose, Kathleen M. and H{\"u}gle-D{\"o}rr, Barbara and Scheer, Ulrich},
  title     = {Nucleolar changes after microinjection of antibodies to RNA polymerase I into the nucleus of mammalian cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40666},
  year      = {1988},
  abstract  = {After microinjection of antibodies against RNA polymerase I into the nuclei of cultured rat kangaroo (PtKz) and rat (RVF-SMC) cells alterations in nucleolar structure and composition were observed. These were detected by electron microscopy and double-label immunofluorescence microscopy using antibodies to proteins representative of the three major components of the nucleolus. The microinjected antibodies produced a progressive loss of the material of the dense fibrillar component (DFC) from the nucleoli which, at 4 h after injection, were transformed into bodies with purely granular component (GC) structure with attached fibrillar centers (FCs). Concomitantly, numerous extranucleolar aggregates appeared in the nucleoplasm which morphologically resembled fragments of the DFC and contained a protein (fibrillarin) diagnostic for this nucleolar structure. These observations indicate that the topological distribution of the material constituting the DFC can be experimentally influenced in interphase cells, apparently by modulating the transcriptional activity of the rRNA genes. These effects are different from nucleolar lesions induced by inhibitory drugs such as actinomycin D-dependent "nucleolar segregation". The structural alterations induced by antibodies to RNA polymerase I resemble, however, the initial events of nucleolar disintegration during mitotic prophase.},
  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}
}
@article{ScheerRaska1987,
  author    = {Scheer, Ulrich and Raska, I.},
  title     = {Immunocytochemical localization of RNA polymerase I in the fibrillar centers of nucleoli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39618},
  year      = {1987},
  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}
}
@article{ReimerRoseScheeretal.1987,
  author    = {Reimer, Georg and Rose, Kathleen M. and Scheer, Ulrich and Tan, Eng M.},
  title     = {Autoantibody to RNA polymerase I in scleroderma sera},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34294},
  year      = {1987},
  abstract  = {Autoantibodies to components of the nucleolus are a unique serological feature of patients with scleroderma. There are autoantibodies of several specificities; one type produces a speckled pattern of nucleolar staining in immunofluorescence. In actinomycin D and 5,6-dichloro-{j-D-ribofuranosylbenzimidazoletreated Vero cells, staining was restricted to the fibrillar and not the granular regions. By double immunofluorescence, specific rabbit anti-RNA polymerase I antibodies stained the same fibrillar structures in drug-segregated nucleoli as scleroderma sera. Scleroderma sera immunoprecipitated 13 polypeptides from (35S)methionine-labeled HeLa cell extract with molecular weights ranging from 210,000 to 14,000. Similar polypeptides were precipitated by rabbit anti-RNA polymerase I antibodies, and their common identities were confirmed in immunoabsorption experiments. Microinjection of purified IgG from a patient with speckled nucleolar staining effectively inhibited ribosomal RNA transcription. Autoantibodies to RNA polymerase I were restricted to certain patients with scleroderma and were not found in other autoimmune diseases.},
  language  = {en}
}
@article{ScheerMessnerHazanetal.1987,
  author    = {Scheer, Ulrich and Messner, Karin and Hazan, Rachel and Raska, Ivan and Hansmann, Paul and Falk, Heinz and Spiess, Eberhard and Franke, Werner W.},
  title     = {High sensitivity immunolocalization of double and single-stranded DNA by a monoclonal antibody},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41063},
  year      = {1987},
  abstract  = {A monoclonal antibody (AK 30-10) is described which specifically reacts with DNA both in double and single-stranded forms but not with other molecules and structures, including deoxyribonucleotides and RNAs. When used in immunocytochemical experiments on tissue sections and permeabilized cultured cells, this antibody detects DNA-containing structures, even when the DNA is present in very small amounts. Examples of high resolution detection include the DNA present in amplified extrachromosomal nucleoli, chromomeres of lampbrush chromosomes, mitochondria, chloroplasts and mycoplasmal particles. In immunoelectron microscopy using the immunogold technique, the DNA was localized in distinct substructures such as the "fibrillar centers" of nucleoli and certain stromal centers in chloroplasts. The antibody also reacts with DNA of chromatin of living cells, as shown by microinjection into cultured mitotic cells and into nuclei of amphibian oocytes. The potential value and the limitations of immunocytochemical DNA detection are discussed.},
  subject      = {Cytologie},
  language  = {en}
}
@article{ScheerHansmannFalketal.1986,
  author    = {Scheer, Ulrich and Hansmann, Paul and Falk, Heinz and Sitte, Peter},
  title     = {Ultrastructural localization of DNA in two Cryptomonas species by use of a monoclonal DNA-antibody},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39746},
  year      = {1986},
  abstract  = {Immunogold cytochemistry - DNA localization - Cryptomonas nucleomorph The distribution and subcellular localization of DNA in the unicellular alga Cryptomonas has been investigated electron-microscopically by indirect immunocytochemistry, using a monoclonal DNA antibody and a gold-Iabeled secondary antibody. This technique proved to be very sensitive and entirely specific. DNA could be demonstrated in four different compartments (nucleus, nucleomorph, plastid, and mitochondrion). Within the plastid, DNA is concentrated in stroma regions that are localized preferentially around the center of the organelle. The mitochondrion contains several isolated DNA-containing regions (nucleoids). Within the nucleus, most of the DNA is localized in the 'condensed' chromatin. DNA was also detectable in small areas of the nucleolus, whereas the interchromatin space of the nucleus appeared almost devoid of DNA. Within the nucleomorph, DNA is distributed inhomogeneously in the matrix. DNA could furthermore be detected in restricted areas of the 'fibrillogranular body' of the nucleomorph, resembling the situation encountered in the nucleol us. The presence of DNA and its characteristic distribution in the nucleomorph provide additional, strong evidence in favour of the interpretation of that organelle as the residual nucleus of a eukaryotic endosymbiont in Cryptomonas.},
  subject      = {Cytologie},
  language  = {en}
}
@article{HadjiolovaRoseScheer1986,
  author    = {Hadjiolova, Krassimira and Rose, Kathleen M. and Scheer, Ulrich},
  title     = {Immunolocalization of nucleolar proteins after D-galactosamine-induced inhibition of transcription in rat hepatocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33205},
  year      = {1986},
  abstract  = {No abstract available},
  language  = {en}
}
@article{ReimerScheerPetersetal.1986,
  author    = {Reimer, Georg and Scheer, Ulrich and Peters, Jan-Michael and Tan, Eng M.},
  title     = {Immunolocalization and partial characterization of a nucleolar autoantigen (PM-Scl) associated with polymyositis / scleroderma overlap syndromes.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33191},
  year      = {1986},
  abstract  = {Precipitating anti-PM-Sel antibodies are present in sera from patients with polymyositis. scleroderma. and polymyositis/scleroderma overlap syndromes. By indirect immunofluorescence microscopy. anti-PM-Scl antibodies stained the nucleolus in cells of different tissues and species. suggesting that the antigen is highly conserved. By electron microscopy, anti-PM-Scl antibodies reacted primarily with the granular component of the nuc1eolus. Drugs that inhibit rRNA synthesis had a marked effect on the expression of PM-Scl antigen. In actinomycin D-treated cells, immunofluorescence staining by anti-PM-Scl was sign{\"u}icantly reduced with residual staining restricted to the granular regions of nuc1eoli. Treatment with 5,6-dichloro-beta-D- ribofuranosylbenzimidazole (DRB) also selectively reduced nuc1eolar staining. On a molecular level, anti-PM-Sel antibodies precipitated 11 polypeptides with molecular weights (Mr) ranging from 110,000 to 20,000. The Mr 80,000 and 20.000 polypeptides were phosphorylated. Evidence suggests that the PM-Scl antigen complex may be related to a prerlbosomal particle.},
  language  = {en}
}
@article{Scheer1986,
  author    = {Scheer, Ulrich},
  title     = {Das Chromatin : seine Struktur und Funktion},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-80790},
  year      = {1986},
  abstract  = {no abstract available},
  subject      = {Chromatin},
  language  = {de}
}
@article{Scheer1986,
  author    = {Scheer, Ulrich},
  title     = {Injection of antibodies into the nucleus of amphibian oocytes: an experimental means of interfering with gene expression in the living cell},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41182},
  year      = {1986},
  abstract  = {No abstract available},
  language  = {en}
}
@article{HuegleScheerFranke1985,
  author    = {H{\"u}gle, Barbara and Scheer, Ulrich and Franke, Werner W.},
  title     = {Ribocharin: a nuclear M\(_r\) 40,000 protein specific to precursor particles of the large ribosomal subunit},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41169},
  year      = {1985},
  abstract  = {Using a monoclonal antibody (No-194) we have identified, in Xenopus laevis and other amphibia, an acidic protein of M, 40,000 (ribocharin) which is specifically associated with the granular component of the nucleolus and nucleoplasmic 65S particles. These particles contain the nuclear 28S rRNA and apparently represent the precursor to the large ribosomal subunit in nucleocytoplasmic transit. By immunoelectron microscopy ribocharin has been localized in the granular component of the nucleolus and in interchromatin granules. During mitosis ribocharin-containing particles are associated with surfaces of chromosomes and are recollected in the reconstituting nucleoli in late telophase. We suggest that ribocharin is a specific component of precursor particles of the large ribosomal subunit, which dissociates from the 65S particle before passage through the nuclear envelope, and is reutilized in ribosome biogenesis.},
  language  = {en}
}
@article{HuegleHazanScheeretal.1985,
  author    = {H{\"u}gle, Barbara and Hazan, Rachel and Scheer, Ulrich and Franke, Werner W.},
  title     = {Localization of ribosomal protein S1 in the granular component of the interphase nucleolus and its distribution during mitosis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39695},
  year      = {1985},
  abstract  = {Using antibodies to various nucleolar and ribosomal proteins, we define, by immunolocalization in situ, the distribution of nucleolar proteins in the different morphological nucleolar subcompartments. In the present study we describe the nucleolar localization of a specific ribosomal protein (51) by immunofluorescence and immunoelectron microscopy using a monoclonal antibody (R5 1-105). In immunoblotting experiments, this antibody reacts specifically with the largest and most acidic protein of the small ribosomal subunit (51) and shows wide interspecies cross-reactivity from amphibia to man. Beside its localization in cytoplasmic ribosomes, this protein is found to be specifically localized in the granular component of the nucleolus and in distinct granular aggregates scattered over the nucleoplasm. This indicates that ribosomal protein 51, in contrast to reports on other ribosomal proteins, is not bound to nascent pre-rRNA transcripts but attaches to preribosomes at later stages of rRNA processing and maturation. This protein is not detected in the residual nucleolar structures of cells inactive in rRNA synthesis such as amphibian and avian erythrocytes. During mitosis, the nucleolar material containing ribosomal protein 51 undergoes a remarkable transition and shows a distribution distinct from that of several other nucleolar proteins. In prophase, the nucleolus disintegrates and protein 51 appears in numerous small granules scattered throughout the prophase nucleus. During metaphase and anaphase, a considerable amount of this protein is found in association with the surfaces of all chromosomes and finely dispersed in the cell plasm. In telophase, protein 51-containing material reaccumulates in granular particles in the nucleoplasm of the newly formed nuclei and, finally, in the re-forming nucleoli. These observations indicate that the nucleolus-derived particles containing ribosomal protein 51 are different from cytoplasmic ribosomes and, in the living cell, are selectively recollected after mitosis into the newly formed nuclei and translocated into a specific nucleolar subcompartment, i.e ., the granular component. The nucleolar location of ribosomal protein 51 and its rearrangement du'ring mitosis is discussed in relation to the distribution of other nucleolar proteins.},
  subject      = {Cytologie},
  language  = {en}
}
@article{ScheerSchmidtZachmannHuegleetal.1984,
  author    = {Scheer, Ulrich and Schmidt-Zachmann, Marion S. and H{\"u}gle, Barbara and Franke, Werner W.},
  title     = {Identification and localization of a novel nucleolar protein of a high molecular weight by a monoclonal antibody},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39786},
  year      = {1984},
  abstract  = {A monoclonal murine antibody (No-I 14) is described which reacts specifically with a polypeptide of molecular weight (M,) 180000 present in low-speed nuclear pellets from oocytes and somatic cells of Xenopus laevis and X. borealis and in isolated amplified nucleoli. Two-dimensional gel electrophoresis has revealed the acidic nature of this polypeptide (isoelectric at pH of ca 4.2 in the presence of 9.5 M urea). A relatively large proportion of the protein is extracted at elevated ionic strength( i.e., at 0.4-0.5 M alkali salt) in a form sedimenting at approx. 7-8S , compatible with a monomeric state. It is also extracted by digestion with RNase but not with DNase. In immunofluorescence microscopy, antibody No-114 stains intensely nucleoli of oocytes and all somatic cells examined , including the residual nucleolar structure of Xenopus erythrocytes which are transcriptionally inactive. During mitosis the antigen does not remain associated with the nucleolar organizer regions (NOR) of chromosomes but is released and dispersed over the cytoplasm until telophase when it re-associates with the reforming interphase nucleoli. At higher resolution the immunofluorescent region is often resolved into a number of distinct subnucleolar components of varied size and shape. Immunoelectron microscopy using colloidal gold-coupled secondary antibodies reveals that the M, 180000 protein is confined to the dense fibrillar component of the nucleolus. This conclusion is also supported by its localization in the fibrillar part of segregated nucleoli of cells treated with actinomycin D. We conclude that nucleoli contain a prominent protein of M, 180000 which contributes to the general structure of the dense fibrillar component of the interphase nucleolus , independent of its specific transcriptional activity.},
  language  = {en}
}
@article{ScheerHinssenFrankeetal.1984,
  author    = {Scheer, Ulrich and Hinssen, Horst and Franke, Werner W. and Jockusch, Brigitte M.},
  title     = {Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39706},
  year      = {1984},
  abstract  = {Nuclei of amphibian oocytes contain large amounts of actin, mostly in unpolymerized or short-polymer form. When antibodies to actin or actin-binding proteins (fragmin and the actin modulator from mammalian smooth muscle) are injected into nuclei of living oocytes of Pleurodeles waltlii, transcription of the lampbrush chromosomes, but not of the rRNA genes, is inhibited. When transcription is repressed by drugs or RNA is digested by microinjection of RNAase into oocyte nuclei, an extensive meshwork of actin filament bundles is seen in association with the isolated lampbrush chromosomes. These observations indicate a close relationship between the state of nuclear actin and transcriptional activity and suggest that nuclear actin may be involved in transcriptional events concerning protein-coding genes.},
  language  = {en}
}
@article{ScheerHuegleHazanetal.1984,
  author    = {Scheer, Ulrich and H{\"u}gle, Barbara and Hazan, Rachel and Rose, Kathleen M.},
  title     = {Drug-induced dispersal of transcribed rRNA genes and transcriptional products: Immunolocalization and silver staining of different nucleolar components in rat cells treated with 5,6-dichloro-1-Beta-D-ribofuranosylbenzimidazole},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33216},
  year      = {1984},
  abstract  = {Upon incubation of cultured rat cells with the adenosine analogue 5,6-dichloro-l-\&\#946;- D-ribofuranosylbenzimidazole (DRB), nucleoli reversibly dissociate into their substructures, disperse throughout the nuclear interior, and form nucleolar "necklaces". We have used this experimental system, which does not inhibit transcription of the rRNA genes, to study by immunocytochemistry the distribution of active rRNA genes and their transcriptional products during nucleolar dispersal and recovery to normal morphology. Antibodies to RNA polymerase I allow detection of template-engaged polymerase, and monoclonal antibodies to a ribosomal protein (S 1) of the small ribosomal subunit permit localization of nucleolar preribosomal particles. The results show that, under the action of DRB transcribed rRNA, genes spread throughout the nucleoplasm and finally appear in the form of several rows, each containing several (up to 30) granules positive for RNA polymerase land argyrophilic proteins. Nucleolar material containing preribosomal particles also appears in granular structures spread over the nucleoplasm but its distribution is distinct from that of rRNA gene-containing granules. We conclude that, although transcriptional units and preribosomal particles are both redistributed in response to DRB, these entities retain their individuality as functionally defined subunits. We further propose that each RNA polymerase-positive granular unit represents a single transcription unit and that each continuous array of granules ("string of nucleolar beads") reflects the linear distribution of rRNA genes along a nucleolar organizer region. Based on the total number of polymerase I-positive granules we estimate that a minimum of 60 rRNA genes are active during interphase of DRB-treated rat cells.},
  language  = {en}
}
@article{FrankeScheerZentgraf1984,
  author    = {Franke, Werner W. and Scheer, Ulrich and Zentgraf, Hanswalter},
  title     = {Organization of transcriptionally active and inactive chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40588},
  year      = {1984},
  abstract  = {No abstract available},
  subject      = {Deutschland},
  language  = {en}
}
@article{ScheerLanfranchiRoseetal.1983,
  author    = {Scheer, Ulrich and Lanfranchi, Gerolamo and Rose, Kathleen M. and Franke, Werner W. and Ringertz, Nils R.},
  title     = {Migration of rat RNA polymerase I into chick erythrocyte nuclei undergoing reactivation in chick-rat heterokaryons},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33232},
  year      = {1983},
  abstract  = {Transcriptionally inactive chick erythrocyte nudei were reactivated by Sendai virusinduced fusion of erythrocytes with rat L6j1 myoblasts. We used antibodies to trace the appearance of a specific protein engaged in transcription of a defined dass of genes, those coding for rRNA, during reactivation. Using immunofluorescence microscopy, we found increasing amounts of rat RNA polymerase I to appear, during a certain period of time after fusion, in the reforming nudeoli of the chick nudei. Amounts of rat RNA polymerase I sufficient to be detected by immunofluorescence microscopy had accumulated in the newly developed chick nudeoli 72- 190 h after fusion was initiated. This time interval coincides with the time when chick rRNA synthesis can first be detected. The results raise the possibility that during these stages of the reactivation process chick rRNA genes are transcribed by heterologous RNA polymerase I moleeules of rat origin.},
  language  = {en}
}
@article{KleinschmidtScheerDabauvalleetal.1983,
  author    = {Kleinschmidt, J{\"u}rgen A. and Scheer, Ulrich and Dabauvalle, Marie-Christine and Bustin, Michael and Franke, Werner W.},
  title     = {High mobility group proteins of amphibian oocytes: a large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33250},
  year      = {1983},
  abstract  = {No abstract available},
  language  = {en}
}
@article{Scheer1982,
  author    = {Scheer, Ulrich},
  title     = {A novel type of chromatin organization in lampbrush chromosomes of Pleurodeles waltlii: visualization of clusters of tandemly repeated, very short transcriptional units},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41087},
  year      = {1982},
  abstract  = {A novel chromatin configuration is described in lampbrush chromosomes of Pleurodeles waltlii oocytes which is different from transcriptionally inactive chromatin as weil as from the various forms of transcribed chromatin hitherto described. This novel type of chromatin is not arranged in Christmas tree-Iike configurations of densely packed lateral ribonucleoprotein (RNP) fibriIs but is characterized by a periodic alternating pattern of thick and thin regions which occur in clusters 01 some 10,000 repeats. Each thickened unit with an average length of 45 nm contains two c10sely spaced particles, the putative RNA polymerases, and each thickened unit is separated from the next one by a beaded chromatin spacer with a length of about 80 nm. This chromatin spacer contains on average two particles of approximately 14 nm in diameter, assumed to be nucleosomes. The thickened regions are interpreted to represent short transcriptional units containing approximately 130 base pairs of DNA which are separated from each other by nontranscribed spacers of 240-400 base pairs of DNA. The possibility is discussed that these transcriptional units represent 5S rRNA or tRNA genes.},
  language  = {en}
}
@article{SommervilleScheer1982,
  author    = {Sommerville, John and Scheer, Ulrich},
  title     = {Transcription of complementary repeat sequences in amphibian oocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33915},
  year      = {1982},
  abstract  = {Repeat sequences are transcribed in the germinal vesicles of amphibian oocytes. In the hnRNA population both complements of the repeats are found and can be readily detected because they form intermolecular duplex structures. The structure and formation of duplex regions have been studied in the hnRNA of Xenopus laevis, Triturus cristatus, Amphiuma means and Necturus maculosus, a series of amphibians of increasing genome size (C-value). In T. cristatus, the duplex structures are mostly 600- 1200 bp in length, whereas in X. laevis they are shorter and in N. maculosus they tend to be longer. Although the proportion of RNA sequence capable of rapidly forming duplex structures is different in different organisms, this property bears no relationship to C-value. However the sequence complexity of complementary repeats, as estimated from the rate of duplex formation, does show an increasing trend with C-value. The complementary repeats found in oocyte hnRNA are transcribed from families of DNA sequence that are each represented in the genome by thousands of copies. The extent of cross-species hybridization is low, indicating that the repeat sequences transcribed in different amphibian genera are not the same. In situ hybridization experiments indicate that the repeat sequences are spread throughout the genome. The evolution and possible function of complementary repeats are considered.},
  language  = {en}
}
@article{Scheer1982,
  author    = {Scheer, Ulrich},
  title     = {Biologische Objekte im Transmissions-Elektronenmikroskop (Teil 4): Spreitungstechniken},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39652},
  year      = {1982},
  abstract  = {Visualizing nucleic acids (DNA, RNA), nucleoprotein complexes and chromatin requires the use of special electron microscopicspreading techniques. In part 4 (27 refs.), methods are outlined for spreading DNA and RNA molecules for electron microscopic observation, these methods using modifications of the basic protein film method developed by A. Kleinschmidt and R. K. Zahn (1959). Hybridization techniques that allow the observation of heteroduplexes formed between two DNA molecules or between DNA and RNA molecules are reviewed, with special emphasis being placed on the DNA-RNA hybrids as a tool for elucidating RNA splicing. Techniques for studying DNA-protein interactions without the use of a protein monolayer film are mentioned. Finally, the "Miller spreading technique" for visualizing the nucleosomal organization of eukaryotic chromatin as well as the transcription of genes is discribed and illustrated.},
  language  = {de}
}
@article{ScheerSommerville1982,
  author    = {Scheer, Ulrich and Sommerville, John},
  title     = {Sizes of chromosome loops and hnRNA molecules in oocytes of amphibia of different genome sizes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33094},
  year      = {1982},
  abstract  = {The lengths of lampbrush chromosome loops and their tran scription units show a positive correlation with genome size in oocytes of amphibia with different C values. However, there is no such correlation with contour lengths of hnRNA molecu les isolated from these oocytes. These results indi cate th at more ON A sequences are transcribed in amphibia of higher C value , but that processing of RNA transc ripts occurs while they are still attached to the chromosomes as nascent ribonucleoprotein fibrils.},
  language  = {en}
}
@article{MorenoDiazdelaEspinaFrankeKrohneetal.1982,
  author    = {Moreno-Diaz de la Espina, Susana and Franke, Werner W. and Krohne, Georg and Trendelenburg, Michael F. and Grund, Christine and Scheer, Ulrich},
  title     = {Medusoid fibril bodies: a novel type of nuclear filament of diameter 8 to 12 nm with periodic ultrastructure demonstrated in oocytes of Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34116},
  year      = {1982},
  abstract  = {No abstract available},
  language  = {en}
}
@article{ScheerZentgrafSauer1981,
  author    = {Scheer, Ulrich and Zentgraf, Hanswalter and Sauer, Helmut W.},
  title     = {Different chromatin structures in Physarum polycephalum: a special form of transcriptionally active chromatin devoid of nucleosomal particles},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33148},
  year      = {1981},
  abstract  = {Nonnucleolar chromatin from interphase nuclei of Physarum polycephalum plasmodia occurs in two different structural configurations as seen in electron microscopic spread preparations. While the majority of the chromatin is devoid of nascent ribonucleoprotein (RNP) fibrils and compacted into nucleosomal particles, a minor proportion (10- 20\%) is organized differently and reveals a smooth contour. It is this form of smooth chromatin which is rich in transcription units (mean length: 1.36±0.21 11m). Only occasionally are solitary nascent RNP fibrils observed which are associated with beaded strands of chromatin. In transcribed smooth chromatin nucleosomal particles are not only absent from the transcription units but also from their nontranscribed flan king regions, indicating that this special structural aspect is not merely a direct consequence of the transcriptional process. The existence of ca. 10- 20\% of Physarum chromatin in the smoothly contoured form is discussed in relation to reports of a preferential digestibility of a similar proportion of Physarum chromatin by DNAse I (Jalouzot et al. , 1980) and to the altered configuration of "peak A" chromatin subunits after micrococcal nuclease digestion (Johnson et al., 1978a, b).},
  language  = {en}
}
@article{ScheerSommerville1981,
  author    = {Scheer, Ulrich and Sommerville, J.},
  title     = {Structural organization of nascent transcripts and hnRNA molecules in amphibian oocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39765},
  year      = {1981},
  abstract  = {Comparisons ofrelative lengths oflampbrush loops, nascent RNP transcripts and hnRNA molecules from oocytes of amphibia with different C-values show that there is an increasing trend in loop, and transcriptional unit, length with increase in genome size but no increasing trend with respect to RN A contour length.The formation of duplex regions and circles in RNP fibrils indicates that RNA processing may occur within the nascent fibrils. The hnRNA molecules from oocytes of the various amphibia readily form intermolecular duplex structures. These complementary sequences have a low kinetic complexity and are transcribed from highly repetitive sequences distributed throughout the genome. Their possible function is considered.},
  language  = {en}
}
@article{ZentgrafMuellerScheeretal.1981,
  author    = {Zentgraf, H. and M{\"u}ller, U. and Scheer, Ulrich and Franke, W. W.},
  title     = {Evidence for the existence of globular units in the supranucleosomal organization of chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34123},
  year      = {1981},
  abstract  = {No abstract available},
  language  = {en}
}