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  • 1
    ISSN: 0248-4900
    Schlagwort(e): Paramecium ; anti-tubulin antibodies ; axoneme ; cilia ; isotype ; microtubules ; post-translational modification ; quall ; tubulin
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1434-601X
    Schlagwort(e): 21.10.Ft ; 25.70.Np ; 27.40.+Z
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract At the projectile-fragment separator FRS of GSI, relativistic secondary beams of about 520 MeV/nucleon were produced by fragmentation of a primary beam of58Ni at 650 MeV/nucleon in a beryllium target. By means of aΔE—Bρ—TOF measurement, the fragments have been identified and their charge-changing probabilities in targets of CH2, C, Al, and Pb have been determined. We describe the results for the total charge-changing cross sections in this first paper, whereas a second article deals with the partial charge-changing cross sections. At the drip line, the measured charge-changing cross sections exhaust close to 100% of the total interaction cross sections as calculated with semiempirical models. The measurements at the proton drip line with low-Z targets indicate that only a very small increase of the cross sections may be observed, whereas the measurements with a lead target show that no significant increase of the total charge-changing cross sections is present which would be a hint for low-lying dipole strength. Our experimental data are compared to Glauber-type calculations.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    ISSN: 1615-6102
    Schlagwort(e): Paramecium ; Microtubule diversity ; Cellular morphogenesis ; Immunofluorescence ; Tubulin post-translational modification
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Ciliates are highly differentiated cells which display extensive deployment of microtubular systems. Because genetic diversity of tubulin is extremely reduced in these cells, microtubule diversity is mostly generated at the post-translational level either through direct modification of tubulin or through the binding of associated proteins to microtubules. We have undertaken a systematic exploration of microtubule diversity in ciliates by way of production of monoclonal antibodies. Previously we reported the biochemical characterization of these antibodies. In addition to antibodies directed against primary sequences, we obtained antibodies directed against post-translational modifications. In this paper, we report a detailed analysis of the distribution of the various epitopes on the microtubular networks ofParamecium, both in interphase cells and during division morphogenesis. Each of these antibodies decorates a subset of microtubules. Acetylation, recognized by antibodies TEU 318 and TEU 348, is detected on stable microtubules early after microtubule assembly. Epitopes recognized by two other antibodies (TAP 952 and AXO 58) are found on a subset of stable microtubules; in addition, the TAP 952 antibody is also found on labile microtubules; both epitopes are detected as soon as microtubule assembly occurs. In contrast, the epitope of the antibody, AXO 49, is associated with only a restricted subset of stable microtubules in the interphase cell, and is detected a lag-time after microtubule assembly during division morphogenesis. These data show that microtubule diversity is generated through a time-dependent sequence and according to a definite spatial pattern.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    ISSN: 1434-601X
    Schlagwort(e): 21.10.Ft ; 25.70.Np ; 27.40.+z
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract At the projectile-fragment separator FRS of GSI, relativistic secondary beams of about 520 MeV/nucleon were produced by fragmentation of a primary beam of58Ni at 650 MeV/nucleon in a beryllium target. By means of aΔE—Bρ—TOF measurement, the fragments were identified and their charge-changing probabilities in targets of (CH2) n , C, Al, and Pb placed at the exit of the FRS were determined. Whereas a first article dealt with the total charge-changing cross sections, we describe in this second article the element distributions of these secondary fragments, which are found to depend strongly on the isospin of the secondary projectile as well as on the target material. In the case of the lead target, the influence of the electromagnetic dissociation is clearly visible in the one-proton and two-proton removal channels. The preference for the formation of even-Z fragments is much more pronounced for exotic secondary projectiles than for projectiles close to stability. Calculations with a geometrical abrasion-ablation model allow to understand the global features of the experimental data. However, far from stability, the discrepancies between calculations and experimental data increase.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 337-349 
    ISSN: 0886-1544
    Schlagwort(e): microtubules ; glutamylation ; Paramecium ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Microtubular networks are extensively developped in many ciliate species. In several of them, we investigate the occurrence of the post-translational glutamylation of tubulin [Eddé et al., 1990: Science 247:82-85; Eddé et al., 1991: J. Cell. Biochem. 46:134-142] using as a probe for such modified tubulin, the monoclonal antibody GT335 [Wolff et al., 1992: Eur. J. Cell Biol. 59:425-432]. Results obtained in Paramecium strongly suggest that both axonemal and cytoplasmic tubulin are glutamylated. As in the vertebrate brain tubulin so far tested, the GT335 epitope is located at the carboxy-terminal fragment of cytoplasmic tubulin removed by subtilisin treatment. Immunoblotting and immunofluorescence experiments reveal that, unlike tubulin acetylation, glutamylation is not restricted to cold-resistant microtubules. In addition, immunofluorescence studies performed on dividing cells show that glutamylation takes place soon after the polymerization of microtubules.Finally, glutamylated tubulin is also detected in the ciliate species Euplotes, Tetrahymena, and Paraurostyla. Together with results obtained on flagellate species, this suggests that tubulin glutamylation came out early in the course of eukaryotic evolution and has been widely exploited in various cellular strategies. © 1994 Wiley-Liss, Inc.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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