@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}
}
@incollection{ScheerDabauvalle1985,
  author    = {Scheer, Ulrich and Dabauvalle, Marie-Christine},
  title     = {Functional organization of the amphibian oocyte nucleus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41178},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1985},
  abstract  = {No abstract available},
  subject      = {Oogenese},
  language  = {en}
}