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  • 1
    Electronic Resource
    Electronic Resource
    The archaeal halophilic virus-encoded Dam-like methyltransferase M.φCh1-I methylates adenine residues and complements dam mutants in the low salt environment of Escherichia coli (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 35 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The genome of the archaeal virus φCh1, infecting Natrialba magadii (formerly Natronobacterium magadii), is composed of 58.5 kbp linear ds DNA. Virus particles contain several RNA species in sizes of 100–800 nucleotides. A fraction of φCh1 genomes is modified within 5′-GATC-3′ and related sequences, as determined by various restriction enzyme digestion analyses. High performance liquid chromatography revealed a fifth base, in addition to the four nucleosides, which was identified as N6-methyladenosine. Genetic analyses and subsequent sequencing led to the identification of a DNA (N6-adenine) methyltransferase (mtase) gene. The protein product was designated M.φCh1-I. By the localization of the most conserved motifs (a DPPY motif occurring before FxGxG), the enzyme was placed within the β-subgroup of the (N6-adenine) methyltransferase class. The mtase gene of φCh1 was classified as a ‘late’ gene, as determined by measuring the kinetics of mRNA and protein expression in N. magadii during the lytic cycle of φCh1. After infection of cells, M.φCh1-I mRNA and protein could be detected in lower amounts than in the situation of virus induction from lysogenic cells. Consequently, only about 5% of the φCh1 progeny genomes after infection of N. magadii carry the M.φCh1-I methylation in contrast to 50% of virus genomes generated by induction of φCh1-lysogenic N. magadii cells. Heterologous expression of the mtase from a halophile with 3 M cytoplasmic salt concentration showed an unexpected feature: the protein was active in the low environment of Escherichia coli and was able to methylate DNA in vivo. Interestingly, it seemed to exhibit a higher sequence specificity in E. coli that resulted in adenine methylation exclusively in the sequence 5′-GATC-3′. Additionally, expression of M.φCh1-I in dam–E. coli cells led to a complete substitution of the function of M.Dam in DNA mismatch repair.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01786.x
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  • 2
    Electronic Resource
    Electronic Resource
    A longitudinal study of autoantibodies against central nervous system tissue and gangliosides in connective tissue diseases (2000)
    Springer
    Rheumatology international 19 (2000), S. 83-88 
    Details
    ISSN: 1437-160X
    Keywords: Key words Connective tissue diseases ; Longitudinal ; Neuropsychiatric ; Antibodies against central nervous tissue ; Gangliosides antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Our objective was to investigate longitudinally, antibodies against central nervous tissue (anti-CNS) derived from bovine brain and gangliosides GM1, GD1a, GD1b, and GT1b in 91 patients with connective tissue diseases (systemic lupus erythematosus, n=38; mixed connective tissue disease, n=16; primary Sjögren's syndrome, n=7; progressive systemic sclerosis, n=13; polymyositis/dermatomyositis, n=4; overlap syndrome, n=5; undifferentiated connective tissue disease, n=8). Anti-CNS and anti-ganglioside antibodies, measured by enzyme-linked immunosorbent assay, were found in 73% and 63% of patients, respectively. Anti-CNS positive sera were also reactive in Western blotting in 74% of cases and recognized up to 14 different polypeptides from 29 to 130 kDa. Anti-CNS and anti-ganglioside antibodies reflected only in a limited extent the disease activity. In 27 of 58 patients, anti-CNS antibodies remained positive independently of disease activity and antibody levels did not correlate with the phases of exacerbations. A total of 36 of 60 anti-CNS-positive patients, in contrast to two of 22 anti-CNS-negative patients, had major neuropsychiatric manifestations (P 〈 0.001). Anti-ganglioside antibodies were not significantly associated with neuropsychiatric manifestations. In conclusion, our longitudinal data suggest that anti-CNS antibodies may be an important marker for the diagnosis of cerebral involvement in connective tissue diseases, but the pathogenic role of these autoantibodies remains to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002960050108
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  • 3
    Electronic Resource
    Electronic Resource
    Detection of Elastase from Pseudomonas aeruginosa in Sputum and its Potential Role in Epithelial Cell Permeability (2000)
    Springer
    Lung 178 (2000), S. 181-189 
    Details
    ISSN: 1432-1750
    Keywords: Key words:Pseudomonas elastase—Monoclonal antibody—ELISA—Epithelial cells—Paracellular permeability.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Most clinical strains of Pseudomonas aeruginosa produce elastase, a zinc metalloprotease that is implicated in the pathogenesis of infections related to these organisms. To better understand the physiologic role of this protease in the regulation of airway permeability, we developed a panel of specific monoclonal antibodies (mAb) against purified Pseudomonas elastase (PE) that do not react with either neutrophil elastase or porcine pancreatic elastase. These mAbs were used in a competitive enzyme-linked immunosorbent assay to determine the concentrations of PE in sputum samples from patients with pulmonary infections. Sputum from patients infected with P. aeruginosa showed a varying amount of PE, whereas others indicated no signals. We also found that the mAbs blocked the effect of PE on epithelial barrier function in vitro on the basis of measurement of transmonolayer electrical resistance of polarized epithelial cells as an index of paracellular permeability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004080000021
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