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  • 11
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 279 (1979), S. 260-262 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Competition radioimmunoassay. Poly(A) polymerase was purified from nuclei of Morris hepatoma 3924A as described previously19 and subjected to affinity chromatography on DNA-cellulose 4. Purified enzyme was iodinated with Na 125I and Chloramine T essentially as described by Greenwood et ...
    Type of Medium: Electronic Resource
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  • 12
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 104 (1991), S. 155-162 
    ISSN: 1573-4919
    Keywords: multiple functional motifs ; enhancer ; rat ribosomal gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Previous studies from this laboratory have characterized a 174 by enhancer element which is located 2kb upstream of the initiation site. Half of the enhancer action is controlled by a 37 by element at the 3′ end of the 174 by region. We now report that a 43 by adjacent domain which is located upstream of the 37 by element constitutes an additional motif of the rDNA enhancer. When the plasmid consisting of the 43 by DNA upstream of the rDNA core promoter was transcribed in a fractionated rat tumor cell extract (fraction DE-B), transcription of rDNA was augmented 4 fold. Electrophoretic mobility shift and DNAase I footprinting analyses showed that the purified 37 by enhancer (E1)-binding protein, (E1BF) not only interacted with the enhancer motif El but also interacted with the neighbouring 43 by enhancer domain E2. The specificity of the binding was demonstrated by competition with unlabeled 37 by and 43 by fragment and lack of competition with nonspecific DNAs in the mobility shift assay. These studies have shown that a single pol I transcription factor can bind to multiple enhancer domains with no significant sequence homologies and such multiple interactions may result in maximal transcription of ribosomal gene from the core promoter.
    Type of Medium: Electronic Resource
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  • 13
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 70 (1986), S. 11-20 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Remarkable advances have been made in the identification of the promoter regions for the ribosomal RNA genes from lower and higher eukaryotes. There has been some progress in the elucidation of the factors that control transcription of the ribosomal RNA gene. The characterization of the transcription factors are crucial for the understanding of the molecular mechanisms of ribosomal gene expression.
    Type of Medium: Electronic Resource
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  • 14
    Electronic Resource
    Electronic Resource
    Springer
    Journal of clinical immunology 7 (1987), S. 24-28 
    ISSN: 1573-2592
    Keywords: Poly(A) polymerase antibodies ; autoimmune diseases ; liver and hepatoma poly(A) polymerase ; nuclear antigens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Sera from 53 patients, 26 with systemic lupus erythematosus (SLE), 8 with rheumatoid arthritis (RA), 9 with Sjogren's syndrome (SS), and 10 with scleroderma (Scl), were screened for the presence of antibodies against liver-type poly(A) polymerase and tumor-type poly(A) polymerase. Sixty percent of the patients with the above four autoimmune diseases have antibodies directed against liver poly(A) polymerase, whereas sera from 74% of the patients contained anti-hepatoma poly(A) polymerase antibodies. About 25% of the patients produced antibodies exclusively against the tumor poly(A) polymerase. IgG containing anti-liver or anti-tumor poly(A) polymerase antibodies inhibited the activity of the respective enzyme. IgG containing antibodies against liver and tumor enzymes inhibited the activity of both enzymes, whereas IgG from sera that did not react with poly(A) polymerase had no effect on either enzyme. These data demonstrated the specificity of these autoantibodies and confirmed the results of the radioimmunoassay.
    Type of Medium: Electronic Resource
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  • 15
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 62 (1996), S. 506-515 
    ISSN: 0730-2312
    Keywords: heat shock ; pre-rRNA processing ; S-100 extract ; U3 snoRNA ; 3′ processing ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The effect of heat shock on pre-rRNA processing at the primary site within external transcribed spacer region 1 (ETS1) was studied in S-100 extract derived from mouse lymphosarcoma cells. In vivo labeling with [32P]orthophosphate showed that the synthesis of the rRNA precursor and its processing to 28S and 18S rRNAs were inhibited significantly due to heat shock. The processing activity was reduced by 50% at 1 h and was completely blocked following 2-h exposure of cells at 42°C. Mixing S-100 extracts from the control and heat-treated cells did not affect the processing activity in the control extract, which proves the absence of a nuclease or other inhibitor(s) of processing in the extract from the heat-shocked cells. Heat shock did not affect interaction between pre-rRNA and U3 snoRNA, a prerequisite for the processing at the primary site, but significantly altered RNA-protein interaction. Three polypeptides of 200, 110, 52 kDa that specifically cross-link to pre-rRNA spanning the primary processing site were inactivated after heat shock. Hyperthermia did not alter 3′ end processing of SV40L pre-mRNA. © 1996 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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