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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of environmental contamination and toxicology 62 (1999), S. 179-186 
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 72 (1998), S. 924-926 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A large blue shift of electroluminescence (EL) was achieved from oxidized n-type porous silicon (PS) in a persulphate solution under cathodic polarization. The two-peak phenomenon observed in the EL spectrum suggests that there are two types of luminescent centers located in the nanoscale silicon particles and at the surface of the oxidized PS layer, respectively. It is found that only the low-energy peak having luminescent centers in nanoscale silicon particles can be tuned by voltage, supporting the quantum confinement model. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 19 (1984), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid P component (AP/SAP), a glycoprotein, precipitated with purified snail galactans from Helix pomatia and Ariania arbustorum in a dose-dependent manner. Radiolabelled AP hinds to human peripheral blood mononuclear cells (PBMC), erythrocytes, and cells derived from human non-T, non-B acute lymphocytic leukaemia. The AP cell binding is specific in that it is dose-dependent and can be blocked both by excess cold AP and by Helix promatia galactan. although it cannot be blocked by an equal amount of the monosaccharide galactose. In vitro studies of human PBMC immune responses demonstrated that AP inhibits PBMC proliferation responses to mycobacterial purified protein derivative and to phytohaemagglutinin and the humoral, antibody response to pokeweed mitogen. The AP-induced suppression of non-specific antibody production by human PBMC was dependent on the time at which AP was added to the culture. AP was suppressive if added in the first 48 h of the 7-day culture, and the suppression could not be reversed by washing the cells after the exposure to AP. The mechanism of AP-induced immunosuppression is still unclear, but human SAP circulates as a pair of pentameric rings, having ten identical subunits that bind to galactose polymers, and our present data suggest that AP affects the immune response through its properties as a lectin.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Surface & Coatings Technology 37 (1989), S. 31-36 
    ISSN: 0257-8972
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Chromatography A 586 (1991), S. 1-9 
    ISSN: 0021-9673
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 20 (1984), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid deposits almost invariably contain a pentagonal-shaped protein (a so-called pentraxin), termed amyloid P component (AP), in close apposition to the amyloid fibrils. AP is also detected alongside normal dust elastin fibres in skin and basement membrane. In the present studies, purified human AP was shown to inhibit the activity of porcine pancreatic elastase. The inhibition of elastolytic activity was not abolished by heating AP to 70°C. Furthermore, two other human serum proteins used as controls did not inhibit elastase activity: albumin, which has a similarly acidic pI, and C-reactive protein, which is a pentraxin, sharing 55% sequence homology with AP. Enzyme kinetic studies showed that elastase treated with AP had a slower elastolytic rate than untreated elastase. The inhibitory effect of AP was reversed by high substrate (fivefold) concentration. These observations suggest that AP may function in vivo to protect elastin and amyloid fibrils from proteolytic cleavage, Indeed, this may in part account for the relative resistance of amyloid deposits to resorption and proteolysis.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 389 (1982), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1435-1463
    Keywords: Keywords: Oxidative stress ; diabetes ; aging ; advanced glycation endproducts ; lipid peroxidation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary. Many approaches have been undertaken to understand Alzheimer's disease (AD) but the heterogeneity of the etiologic factors makes it difficult to define the clincally most important factor determining the onset and progression of the disease. However, there is increasing evidence that the previously so-called "secondary factors" such as a disturbed glucose metabolism, oxidative stress and formation of "advanced glycation endproducts" (AGEs) and their interaction in a vicious cycle are also important for the onset and progression of AD. AGEs are protein modifications that contribute to the formation of the histopathological and biochemical hallmarks of AD: amyloid plaques, neurofibrillary tangles and activated microglia. Oxidative modifications are formed by a complex cascade of dehydration, oxidation and cyclisation reactions, subsequent to a non-enzymatic reaction of sugars with amino groups of proteins. Accumulation of AGE-crosslinked proteins throughout life is a general phenomenon of ageing. However, AGEs are more than just markers of ageing since they can also exert adverse biologic effects on tissues and cells, including the activation of intracellular signal transduction pathways, leading to the upregulation of cytokine and free radical production (oxidative stress). Oxidative stress is involved in various divergent events leading to cell damage, including an increase in membrane rigidity, DNA strand breaks and an impairment in glucose uptake. In addition, other age-related metabolic changes such as depletion of antioxidants or decreased energy production by a disturbed glucose metabolism diminish the ability of the cell to cope with the effects of radical-induced membrane, protein and DNA damage. With our improving understanding of the molecular basis for the clinical symptoms of dementia, it is hoped that the elucidation of the etiologic causes, particularly the positive feedback loops involving radical damage and a reduced glucose metabolism, will help to develop novel "neuroprotective" treatment strategies able to interrupt this vicious cycle of oxidative stress and energy shortage in AD.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-1335
    Keywords: Key words FGF3 ; Tumor ; Nude mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Recently, the expression of fibroblast growth factor 3 (FGF3) was found in 55% of human Kaposi's sarcoma (KS) tumor tissues examined, while almost no expression of FGF3 was found in normal skin. To further these studies, human FGF3 cDNA were constructed by the overlap-extension method. The proteins translated from two FGF3 cDNA, which differ only in the sequences preceding the AUG presumed to be the initiation codon, were shown to have the same molecular mass. This result suggests that translation of human FGF3, which is different from mouse FGF3, begins only at the AUG site. The human FGF cDNA was transfected into NIH3T3 cells. The NIH 3T3 cells transformed by FGF3 were then injected subcutaneously into athymic nude mice. Nodular lesions developed at the injection sites in all seven mice injected with the F3-1 cell clone, which showed high expression of FGF3, and in two out of six mice injected with the F3-2 cell clone, which expressed a low level of FGF3. Histopathological features of these tumors contained fascicles of spindle-shaped cells surrounding irregular endothelial lined vascular clefts, similar to those observed in human KS lesions. Immunohistochemical staining for factor V111 antigen revealed reactivity in multiple areas, especially in abundant vascular structures of the tumor sections examined. The expression of FGF3 together with the FGF receptors FGFR1, FGFR2, and FGFR3, was detected in the mouse tumors by Northern blot analysis. Our results indicate that tumors induced by FGF3-transformed NIH3T3 cells show some similarities to human KS tumors. In conclusion, our results demonstrate the potential tumorigenic and angiogenic role of human FGF3.
    Type of Medium: Electronic Resource
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