@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{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}
}