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  • 1
    Online Resource
    Online Resource
    Identifizierung von Apoptose-modifizierten Proteinen : Abschlußbericht zum Projekt (2002)
    [Berlin]
    Details Availability
    Keywords: Forschungsbericht
    Description / Table of Contents: Proteome analysis, apoptosis, caspase, 2-DE electrophoresis, mass spectrometry, target
    Type of Medium: Online Resource
    Pages: Online-Ressource (10 p. = 131 KB)
    Edition: [Elektronische Ressource]
    URL: https://edocs.tib.eu/files/e01fb02/357621247.pdf
    URL: https://edocs.tib.eu/files/e01fb02/357621247l.pdf
    Language: German
    Note: Contract BMBF 0312260. - Differences between the printed and electronic version of the document are possible. - nIndex p. 6 - 7. - nBibliography p. 7. - Engl. title: Identification and characterisation of apoptosis-modified proteins , Also available as printed version , Systemvoraussetzungen: Acrobat Reader.
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  • 2
    Electronic Resource
    Electronic Resource
    Interaction of two variable proteins (PilE and PilC) required for pilus-mediated adherence of Neisseria gonorrhoeae to human epithelial cells (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Pili confer the initial ability of Neisseria gonorrhoeae to bind to epithelial cells. Pilin (PilE), the major pilus subunit, and a minor protein termed PilC, reportedly essential for pilus biogenesis, undergo intra-strain phase and structural variation. We demonstrate here that at least two different adherence properties are associated with the gonococcal pili: one is specific for erythrocytes, which is virtually unaffected by PilE variation, and another is specific for epithelial cells, and is modulated in response to the variation of PilE. Based on this finding, mutants of a recA - strain were selected that had lost the ability to bind to human cornea epithelial cells (A-) but retained the ability to form pili (P+) and to agglutinate human erythrocytes (H+). The adherence-negative mutants failed to produce detectable levels of PMC1 or PilC2 proteins, representing pilC phase variants generated in the absence of RecA. The A-pilC phase variants were indistinguishable from their A+parents and spontaneous A+ revertants with regard to the amount of PilE produced and its electrophoretic mobility, the degrees of piliation and haemagglutination, and the pilE nucleotide sequence. These data demonstrate a central role for PilC in pilus-mediated adherence of N. gonorrhoeae to human epithelial cells and further indicate that neither PNC1 nor PilC2 is obligatory for the assembly of gonococcal pili.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb02211.x
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