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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1440
    Keywords: Key words Antibody ; Capsid antigens ; HHV-8 ; Kaposi’s sarcoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Sequences of a new herpesvirus with homology to gammaherpesvirinae were recently identified in AIDS-associated Kaposi’s sarcoma (KS). Subsequently this novel virus, called KS-associated virus (KSHV) or human herpesvirus (HHV) 8 was detected in classical KS and AIDS-associated body cavity based lymphomas by polymerase chain reaction. In this report major and minor capsid proteins of HHV-8 were molecularly cloned and produced as recombinant proteins in Escherichia coli. Sera from 69 HIV-1 infected patients with KS, 30 HIV-1 infected patients without KS and 106 control individuals were tested by enzyme-linked immunosorbent assay for anti-HHV-8 capsid IgM and IgG antibodies. Sera from four patients were tested over periods ranging from 18 months to 6 years. IgG antibodies directed against HHV-8 capsid antigens were detected in patients with AIDS-associated KS and in some AIDS patients without KS. Seroconversion with IgM and IgG antibodies directed against HHV-8 capsid proteins occurred more than 1 year prior to diagnosis of KS. In a considerable portion of KS patients no IgM or IgG antibodies against HHV-8 capsid proteins were detected. In these patients there was an inverse relationship between antibodies against HHV-8orf26 and the CD4/CD8 ratio, suggesting that the inconsistency of anti-HHV-8orf26 antibodies is due at least partly to an impaired immune response. No reactivity against HHV-8 capsid antigens was detected in the vast majority of sera from HIV-negative control individuals. Our findings indicate that a specific humoral immune response against capsid proteins is raised in HHV-8 infected individuals, and that anti-capsid antibodies can be used to diagnose HHV-8 infection. The correlation between occurrence of anti-HHV-8 antibodies and KS supports the hypothesis of a causative role of HHV-8.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 26 (1987), S. 347-357 
    ISSN: 1432-1432
    Keywords: Ribosome structure ; Electron microscopy ; Image analysis ; Evolutionary lineages
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Multivariate statistical analysis and classification techniques are powerful tools in sorting noisy electron micrographs of single particles according to their principal features, enabling one to form average images with an enhanced signal-to-noise ratio and a better reproducible resolution. We apply this methodology here to determining the characteristic views of the large (50S) ribosomal subunits from the eubacteriumEscherichia coli and the archaebacteriaMethanococcus vannielii, Sulfolobus solfataricus, andHalobacterium marismortui. Average images were obtained of the subunit in the common crown and kidney projections, but views of the particle in orientations intermediate between these two extremes were also elucidated for all species. These averages show reproducible detail of up to 2.0 nm resolution, thus enabling the visualization and interspecies comparison of many structural features as a first step toward comparing the actual three-dimensional structures. Our results disprove evolutionary lineages recently postulated on the basis of electron microscopical images of ribosomal subunits.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1173
    Keywords: Schlüsselwörter Hepatitis-C-Virus ; Dermatologische Assoziationen ; Key words Hepatitis C-virus ; Dermatologic manifestations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Acute infection with hepatitis C virus (HCV) is often clinically inapparent, but may affect several organ systems in its chronic course. In dermatology, common diseases such as lichen planus, cryoglobulinemic vasculitis and porphyria cutanea tarda have been described in association with HCV infection. A number of other dermatologic disorders, e.g., psoriasis, chronic urticaria, chronic pruritus, pseudo-kaposi sarcoma, necrolytic migratory erythema and Behçet disease, have been associated in case reports with HCV-induced liver disease. In this study we summarize the recent literature reports, present three patients observed by our group and update the topic.
    Notes: Zusammenfassung Die Infektion mit dem Hepatitis-C-Virus (HCV) verläuft im akuten Stadium meist asymptomatisch. Häufig entwickelt sich jedoch in der Folge eine klinisch stumme Hepatitis, die anschließend in eine Leberzirrhose münden kann. In den letzten Jahren wurden zahlreiche Erkrankungen verschiedener Organsysteme (z.B. Endokrinium, Knochenmark, Niere) in Assoziation mit der HCV-Infektion beschrieben, darunter auch diverse Dermatosen. Bei den HCV-assoziierten Dermatosen handelt es sich v.a. um Lichen ruber, kryoglobulinassoziierte Vaskulitiden oder Porphyria cutanea tarda. Auch für das Vorkommen anderer häufiger Dermatosen wie Psoriasis, chronisch-rezidivierende Urtikaria oder kasuistisch für chronischen Pruritus, Pseudokaposi, nekrolytische Erytheme, Morbus Behçet u.v.a. wurde die Assoziation mit einer Hepatitis-C-Infektion berichtet. In der vorliegenden Übersicht werden die derzeitigen Kenntnisse zusammengefaßt, drei Fälle aus dem eigenen Krankheitsgut vorgestellt und entsprechende Schlußfolgerungen gezogen.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The location of the 3′ end of 16S rRNA in E. coli 30S ribosomal subunits has been determined by immuno electron microscopy. The 3′ terminal adenosine of isolated 16S rRNA was oxidized with sodium periodate and reacted with N-γ-(2,4-dinitrophenyl) aminobutyric acid hydrazide. Functionally active 30S subunits were reconstituted from DNP-16S rRNA and total 30S ribosomal proteins. DNP-30S subunits were complexed with DNP-specific IgG-antibody and examined in the electron microscope. The 3′ end of the 16S rRNA was mapped at a single region located at the inner side of the large lobe of the 30S subunit. The location of the 3′ end also provides information as to the topography of the binding domain of natural mRNA on 30S subunits, since a pyrimidine-rich sequence at the 3′ terminal region of 16S rRNA participates in the correct alignment of natural mRNAs during initiation complex formation.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In spite of considerable effort there is still serious disagreement in the literature about the question of whether epitopes of ribosomal protein S4 are accessible for antibody binding on the intact small ribosomal subunit. We have attempted to resolve this issue using three independent approaches: (i) a re-investigation of the exposure and the location of epitopes of ribosomal protein S4 on the surface of the 30S subunit and 30S core particles of the E. coli ribosome, including rigorous controls of antibody specificity, (ii) a similar investigation of protein S4 from Bacillus stearothermophilus and (iii) the labelling of residue Cys-31 of E. coli S4 with a fluorescein derivative the accessibility of which towards a fluorescein-specific antibody was demonstrated directly by fluorimetry. In each of the three cases the antigen (E. coli S4, B. stearothermophilus S4 or fluorescein) was found to reside on the small lobe.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1617-4623
    Keywords: Ribosomal topography ; Ribosomal protein L27 ; Immuno-electron microscopy ; Peptidyl transferase centre
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Protein L27 has been localized on the ribosomal surface by immuno-electron microscopy by using antibodies specific for Escherichia coli L27, and by reconstituting 50 S subunits from an E. coli mutant, which lacks protein L27, with the homologous protein from Bacillus subtilis and using antibodies specific for the B. subtilis protein. With both approaches, protein L27 has been located at the base of the central protuberance at the interface side of the 50 S particle and thus in proximity to the peptidyl transferase centre. The immuno-electron microscopic data also suggest that the interface region of the 50 S particle is not as flat as most of the proposed three-dimensional models suggest, but instead there is a significant depression.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two mutants lacking protein L15 from the ribosome as determined by two dimensional gels were investigated using a number of different immunological methods. One strain was found to possess several protein L15 moieties which differed in net charge and in size. The other showed no evidence of L15 cross-reacting material (CRM) on the ribosome or in the supernatant. Ribosomes of this strain were used as a control in the process of the localisation of protein L15 on the surface of the large subunit of Escherichia coli ribosomes. Antigenic determinants mapped in the angle between the central protuberance and the L1 protuberance. Protein L15 has been assigned a central role in the large subunit in vitro assembly map, in peptidyltransferase activity and in the binding of erythromycin, so the significance of a mutant lacking this protein is discussed.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mice were immunised with 30S subunits from E. coli and their spleen cells were fused with myeloma cells. From this fusion two monoclonal antibodies were obtained, one of which was shown to be specific for ribosomal protein S3, the other for ribosomal protein S7. The two monoclonal antibodies formed stable complexes with intact 30S subunits and were therefore used for the three-dimensional localisation of ribosomal proteins S3 and S7 on the surface of the E. coli small subunit by immuno electron microscopy. The antibody binding sites determined with the two monoclonal antibodies were found to lie in the same area as those obtained with conventional antibodies. Both proteins S3 and S7 are located on the head of the 30S subunit, close to the one-third/two-thirds partition. Protein S3 is located just above the small lobe, whereas protein S7 is located on the side of the large lobe.
    Type of Medium: Electronic Resource
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