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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    British journal of dermatology 150 (2004), S. 0 
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK; Malden , USA : Blackwell Science Ltd
    Scandinavian journal of immunology 59 (2004), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Anti-Golgi autoantibodies (AGAs) and their targets have been reported from several diseases. However, the association of AGAs, selective autoantigens and related clinical diseases is still obscure. In this study, the presence of AGAs in the sera of 5983 patients was screened to explore the association of AGAs and clinical diseases. By means of indirect immunofluorescence using HEp-2 cells, sera of 12 patients bearing AGAs were identified. The location of recognized Golgi autoantigen(s) was confirmed by the treatment of monensin and double immunostaining using β-COP. Using the immunoelectron microscopy, AGA immunoreactivity was clearly demonstrated at a stack structure, characteristic of the Golgi complex. Furthermore, analysis of the 12 AGA-positive sera by Western blot revealed at least 15 components of Golgi antigens with relative molecular weights ranging from 54 to 350 kDa, and several Golgi autoantigens identified may be novel. Notably, over half of the AGA-positive cases found belong to non-autoimmune diseases, particularly hepatic disorder. This study presents the association of AGAs, components of the Golgi complex and clinical diseases.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 261 (1999), S. 374-380 
    ISSN: 1617-4623
    Keywords: Key wordsEscherichia coli ; ribA ; GTP cyclohydrolase II ; SoxS binding ; RNA polymerase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ribA gene, encoding GTP cyclohydrolase II in Escherichia coli, is a member of the soxRS regulon, which is induced by superoxide-generating agents. By evaluating lacZ expression driven by the ribA promoter carrying different lengths of upstream region in a monolysogen, we found that the superoxide-responsive element resides between 56 and 94 nucleotides upstream of the transcriptional start site. Purified SoxS protein bound to this region and protected nucleotides between positions −80 and −58 from degradation by DNase I. This region contains a putative SoxS-binding sequence (soxbox) in reverse orientation. The SoxS protein interacted specifically with four guanine residues within the soxbox sequence, as demonstrated by methylation interference analysis. These results clearly indicate that SoxS binds to the reversed soxbox sequence in the ribA gene, while in other known genes of the soxRS regulon it binds to the normally oriented soxbox. Possible modes of interaction between SoxS and RNA polymerase are discussed.
    Type of Medium: Electronic Resource
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