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  • Adenylate cyclase  (1)
  • Basal body connector  (1)
  • Bone resorption  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 630 (1980), S. 459-462 
    ISSN: 0304-4165
    Keywords: Bone resorption ; Ca^2^+ release ; Osteoclast ; Parathyroid hormone ; Platelet factor 4
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1615-6102
    Keywords: Basal body connector ; Centrin ; Flagellar roots ; Immunoblotting ; Immunolocalisation ; Phytophthora cinnamomi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Antibodies raised against the calcium-binding protein centrin, were used to identify and localise centrin containing structures in the flagellar apparatus of zoospores and cysts of the oomycetePhytophthora cinnamomi. Immunoblotting of extracts from zoospores indicates that theP. cinnamomi centrin homologue is a 20 kDa protein. Immunofluorescence microscopy with anti-centrin antibodies reveals labelling in the flagella, the basal body connector and co-localisation along the microtubular R1 root (formerly called AR3) that runs from the right side of the basal body of the anterior flagellum into the anterior of the zoospore close to the ventral surface. The centrin (R1cen) and tubulin components of the R1 root split into four loops on the right hand side of the ventral groove and rejoin along the left hand side of the groove. The R1 root continues down the left hand side of the zoospore past the basal bodies and parallel to the R4 root. We propose that at least inP. cinnamomi there is no R2 root. Immunogold labelling confirms that centrin is a component of the basal body connector complex. When the zoospores become spherical during encystment, the R1cen pivots by approximately 90 ° with respect to the nucleus.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1615-6102
    Keywords: Adenylate cyclase ; Cell cycle ; Chlamydomonas reinhardtii ; Cyclic AMP ; Cyclic nucleotide phosphodiesterase ; Mutant strains
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three independent isolates ofChlamydomonas, selected for caffeine resistance, were found to arrest in G1 phase, as determined by quantitative fluorescence measurements of DNA, when grown at a non-permissive temperature. This cell cycle arrest correlated with lowered levels of cAMP and of adenylate cyclase activity. The arrested cells could be rescued by added cAMP but not AMP, hence the defect was not one of general purine metabolism. Back-crosses to wild type revealed that the phenotypes observed result from a combination of three separable mutations. It is clear that the mutations define functions that are more stringently required for cell division than for growth since the mutant strains are able to grow up to fifteen times normal size while blocked at the non-permissive temperature. The possible interaction of cAMP dependent events with division is discussed.
    Type of Medium: Electronic Resource
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