@article{vonJagowSebald1980,
  author    = {von Jagow, Gerhard and Sebald, Walter},
  title     = {b-Type cytochromes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47383},
  year      = {1980},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldMachleidtWachter1980,
  author    = {Sebald, Walter and Machleidt, Werner and Wachter, Elmar},
  title     = {N,N'-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47394},
  year      = {1980},
  abstract  = {T~e N,N'-dicrclohexylcarbodiimide-binding proteolipid subumt of the mitochondrial adenosinetriphosphatases (ATP phosphohydrolase, EC 3.6.1.3) of Neurosporacrassa and Saccharomyces cerevisiae were purified from mitochondria incubated with the radioactively labeled inhibitor. The specifically labeled subunit was cleaved with cyanogen bromide and N-bromosuccinimide, and the resultant fragments were separated by gel chromatography in the presence of 80\% (vol/vol) formic acid. The N,N'-dicyclohexylcarbodiimide label was recovered in each organism exclusively in a 17-residue fragment. Further analysis by automated solid-phase Edman degrada.ti.on revealed tha~ the bound label was present at only one positIOn, correspondmg to a glutamyl residue. The NN'~ icyc~ohexyl~a~bodiiJ?1~de-'!l0dified glutamyl residue is the ~nly Id~ntIcal aCidic posItIon m both proteins and occurs in the middle of a hydrophobic sequence of about 25 residues.},
  subject      = {Dicyclohexylcarbodiimid},
  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}
}
@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{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{FrankeKleinschmidtSpringetal.1981,
  author    = {Franke, Werner W. and Kleinschmidt, J{\"u}rgen A. and Spring, Herbert and Krohne, Georg and Grund, Christine and Trendelenburg, Michael F. and St{\"o}hr, Michael and Scheer, Ulrich},
  title     = {A nucleolar skeleton of protein filaments demonstrated in amplified nucleoli of Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33130},
  year      = {1981},
  abstract  = {The amplified, extrachromosomal nucleoli of Xenopus oocytes contain a meshwork of -4-nm-thick filaments, which are densely coiled into higher-order fibrils of diameter 30-40 nm and are resistant to treatment with high- and low-salt concentrations, nucleases (DNase I, pancreatic RNase, micrococcal nuclease), sulfhydryl agents, and various nonionic detergents. This filamentous "skeleton" has been prepared from manually isolated nuclear contents and nucleoli as weil as from nucleoli isolated by fluorescence-activated particle sorting. The nucleolar skeletons are observed in light and electron microscopy and are characterized by ravels of filaments that are especially densely packed in the nucleolar cortex. DNA as weil as RNA are not constituents of this structure, and precursors to ribosomal RNAs are completely removed from the extraction-resistant filaments by treatment with high-salt buffer or RN ase. Fractions of isolated nucleolar skeletons show specific enrichment of an acidic major protein of 145,000 mol wt and an apparent pi value of -6.15, accompanied in some preparations by various amounts of minor proteins. The demonstration of this skeletal structure in "free" extrachromosomal nucleoli excludes the problem of contaminations by nonnucleolar material such as perinucleolar heterochromatin normally encountered in studies of nucleoli from somatic cells. It is suggested that this insoluble protein filament complex forms a skeleton specific to the nucleolus proper that is different from other extraction-resistant components of the nucleus such as matrix and lamina and is involved in the spatial organization of the nucleolar chromatin and its transcriptional products. In studies of the organization of the interphase nucleus, considerable progress has been made in the elucidation of the arrangement of chromatin components and transcriptional products. However, relatively little is known about the composition and function of another category of nuclear structures, the nonnucleoproteinaceous architectural components that are insoluble in solutions of low and high ionic strength, despite numerous studies dedicated to this problem. Such structures include (a) the nuclear envelope and its pore complexes (I, 15, 18, 23, 37, 41), (b) a peripheral layer of insoluble protein ("lamina"; I, 15, 22, 23, 59), (e) certain skeletal proteins related to the chromosome "scaffold" described by Laemmli and coworkers (see references 2 and 3), and (d) ill-defined tangles of fibrillar structures of the nuclear interior that are collectively described as residual "matrix" (6, 21 ; for reviews, see references THE JOURNAL OF CEll BrOlOGY . VOlUME 90 AUGUST 1981 289-299 © The RockefeIler University Press · 0021 -9525/ 81 / 08/ 0289/ 11 \$1 .00 4 and 12). The latter, preparatively},
  language  = {en}
}
@article{Scheer1981,
  author    = {Scheer, Ulrich},
  title     = {Identification of a novel class of tandemly repeated genes transcribed on lampbrush chromosomes of Pleurodeles waltlii},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33153},
  year      = {1981},
  abstract  = {Electron microscope preparations of lampbrush chromosomes from oocytes of Pleurodeles waltl;; have revealed a new class of tandemly repeated genes. These genes are highly active, as judged by the close spacing of nascent transcripts. They occur in clusters of >100 copies and are transcribed in units containing roughly 940 base pairs of DNA that are separated by nontranscribed spacers of an estimated DNA content of 2,410 base pairs. The size and the pattern of arrangement of these transcription units can not be correlated with any of the repetitious genes so far described.},
  language  = {en}
}
@article{WernerSebald1981,
  author    = {Werner, S. and Sebald, Werner},
  title     = {Immunological techniques for studies on the biogenesis of mitochondrial membrane proteins},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82044},
  year      = {1981},
  abstract  = {no abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SchairerHoppeSebaldetal.1982,
  author    = {Schairer, H. U. and Hoppe, J. and Sebald, Walter and Friedl, P.},
  title     = {Topological and functional aspects of the proton conductor, F\(_0\), of the Escherichia coli ATP-synthase},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62721},
  year      = {1982},
  abstract  = {The isolated H\(^+\) conductor, F\(_0\) , of the Escherichia co1i ATP-synthase consists of three subunits, a, b, and c. H\(^+\) -permeable liposomes can be reconstit~ted with F\(_0\) and lipids; addition of F\(_1\)-ATPase reconstitutes a functional ATP-synthase. Mutants with altered or misslng F\(_0\) subunits are defective in H\(^+\) conduction. Thus, all three subunits are necessary for the expression of H\(^+\) conduction. The subunits a and b contain binding sites for F\(_1\)• Computer calculations, cross-links, membrane-permeating photo-reactive labels, and proteases were used to develop tentative structural models for the individual F\(_0\) subunits.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldFriedlSchaireretal.1982,
  author    = {Sebald, Walter and Friedl, P. and Schairer, H. U. and Hoppe, J.},
  title     = {Structure and genetics of the H\(^+\)-conducting F\(_0\) portion of the ATP synthase},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62733},
  year      = {1982},
  abstract  = {The ATP synthase occurs in remarkably conserved form in procaryotic and eucaryotic cells. Thus, our present knowledge of ATP synthase is derived from sturlies of the enzyme from different organisms, each affering specific experimental possibilities. In recent tim es, research on the H\(^+\) -conducting F0 part of the ATP synthase has been greatly stimulated by two developments in the Escherichio coli system. Firstly, the purification and reconstitution of the whole ATP synthase as weil as the proton conductor Fa from E. coli have been achieved. These functionally active preparations are well defined in terms of subunit composition, similar to the thermophilic enzyme from PS-3 studied by Kagawa's group.u Secondly, the genetics and the molecular cloning of the genes of all the F\(_0\) subunits from E. coli yielded information on the function of subunit polypeptides and essential amino acid residues. Furthermore, the amino acid sequence of hydrophobic F\(_0\) subunits, which are difficult to analyze by protein-chemical techniques, could be derived from the nucleotide sequence of the genes. These achievements, which shall be briefly summarized in the next part of this communication, provide the framework to study specific aspects of the structure and function of the F\(_0\) subunits.},
  subject      = {Biochemie},
  language  = {en}
}
@article{ViebrockPerzSebald1982,
  author    = {Viebrock, A. and Perz, A. and Sebald, Walter},
  title     = {The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62742},
  year      = {1982},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SchartlBarnekowBaueretal.1982,
  author    = {Schartl, Manfred and Barnekow, A. and Bauer, H. and Anders, F.},
  title     = {Correlations of inheritance and expression between a tumor gene and the cellular homolog of the Rous sarcoma virus-transforming gene in Xiphophorus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61937},
  year      = {1982},
  abstract  = {No abstract available},
  subject      = {Physiologische Chemie},
  language  = {en}
}
@article{BarnekowSchartlAndersetal.1982,
  author    = {Barnekow, A. and Schartl, Manfred and Anders, F. and Bauer, H.},
  title     = {Identification of a fish protein associated with a kinase activity and related to the Rous sarcoma virus transforming protein},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61946},
  year      = {1982},
  abstract  = {No abstract available},
  subject      = {Physiologische Chemie},
  language  = {en}
}
@article{KreftHughes1982,
  author    = {Kreft, J{\"u}rgen and Hughes, Colin},
  title     = {Cloning vectors derived from plasmids and phage of Bacillus},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47014},
  year      = {1982},
  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{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}
}