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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
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 290 (1981), S. 708-710 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Our observations on the ultrastructure of the flagellum of M. pusilla (previously named Chromulina pusilla 9) agree well with those of Manton8. The flagellum is ∼5 µm long and has the appearance of a short thick stub terminated by a long thin fibre (Fig. la). The thicker proximal portion ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 279 (1979), S. 532-534 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The force required for motion of cilia, eukaryotic flagella and sperm tails is generated by the dynein arms, which cause sliding of adjacent peripheral microtubule doublets2"4. The dynein arms have been shown to contain Mg2+-ATPases5. The force generated by the arms can only cause the adjacent ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 13 (1992), S. 635-639 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The axonemal motion supported by fluorescent ribose-modified analogues, anthraniloyl ATP (Ant-ATP) and methylanthraniloyl ATP (Mant-ATP), was investigated. Ant-ATP and Mant-ATP supported good vigorous motion. A detailed study of the movement shows that the maximum beat frequencies (Vmax) were significantly lower with the analogues. However, Michaelis constants (Km) for beat frequency were also significantly lower than with ATP. Thus the net effect of changes in these two parameters, Vmax/Km, was similar for ATP and Ant-ATP and higher with Mant-ATP. Thus these fluorescent analogues are good substrates for axonemal movement. The consistently higher value of Vmax/Km, a measure of substrate selectivity, with Mant-ATP over Ant-ATP suggests a feature of the ribose binding site. Other significant differences in the movement with the fluorescent analogues are quantified in terms of kinetic measures of sliding velocity and bend propagation velocity.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 13 (1989), S. 239-244 
    ISSN: 0886-1544
    Keywords: sperm ; nucleotide analog ; kinetics ; Stronglyocentrotus purpuratus ; reactivation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The 2-substituted ATP analog 2-Chloro ATP was tested for its capacity to support axonemal movement. The movement of sea urchin axonemes reactivated with 2-CI ATP appeared very similar to that with ATP. Detailed waveform analysis indicated that bend angle and shear amplitude were not significantly different for ATP and 2-CI ATP. Although wavelength differs at particular nucleotide concentrations, if normalized to the beat frequency, it is similar for ATP and 2-CI ATP. The main difference in the movement with the two analogs was seen in beat frequency and sliding velocity. The Vmax for beat frequency and mean sliding velocity was lower for 2-CI ATP. The apparent Km for beat frequency and sliding velocity was much lower for 2-CI ATP. The ratio of these two effects, that is, (Vmax/Km) is higher for 2-CI ATP. Thus 2-CI ATP is a good substrate for axonemal movement. The significantly lower Km of 2-CI ATP was also demonstrated by its ability to support oscillatory motion at concentrations below that for ATP. The observations identify the structures and conformation of substrate necessary to support axonemal movement.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 21 (1992), S. 74-82 
    ISSN: 0886-1544
    Keywords: motion analysis ; sperm activation ; K+inhibition ; Fluo-3 ; eukaryotic flagella ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We investigated the swimming patterns of trout sperm using computer-assisted analyses of video microscopy. Under full activation conditions, in which 80-100% of sperm activate their motility, sperm swim in circular paths for 2-5 sec, followed by 30-60 sec of a more linear swimming, and, finally, cessation of movement, with a straightening of the flagella. Threshold activation, in which 50% of the sperm activate, is characterized by circular patterns of swimming for less than 20 sec, with straightened flagella upon cessation. Full activation and threshold activation are observed in low-K+ solution or in an Mg++ -supplemented K+ solution. Similarities in swimming patterns in low-K+ solution and in a Mg++ -supplemented K+ solution suggest a common underlying mechanism of activation. Initiation of movement in solutions with high Ca++ to K+ ratio is similar to activation in K+ -free solution. However, sperm in Ca++ -supplemented media resume circular swimming within 20-25 sec after activation, and, upon cessation of movement, the flagella are frequently cane shaped or bent. Differences in swimming patterns upon activation by high Ca++ concentration suggest additional effects of Ca++ on regulating swimming patterns. We used the fluorescent Ca++ indicator Fluo-3 to measure changes in intracellular Ca++ concentration upon activation. Intracellular Ca++ concentration transiently increases upon activation, with peak Ca++ concentration coinciding with the period of circular swimming. This transient increase in Ca++ concentration is seen in the absence of external Ca++, providing strong evidence for the released of Ca++ from intracellular stores upon activation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 46-54 
    ISSN: 0886-1544
    Keywords: sliding disintegration ; Tetrahymena ; active site ; ribose-modified ATP ; dynein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Axonemal sliding involves both sliding velocity and the extent of sliding, that is how many doublets slide. It is clear that axonemes cannot beat if all doublets were to slide simultaneously, thus sliding extent is important. Using the turbidimetric assay of sliding disintegration of Tetrahymena axonemes, we examined the sliding extent and the effect of ADP, ATP, and ATP analogs on the sliding extent. Of course, ATP is necessary to produce sliding disintegration, but ATP alone did not produce extensive sliding disintegration. The addition of ADP allowed greater extent of sliding disintegration. The additions of higher ATP concentration even in the presence of ADP inhibited sliding disintegration. We also observed sliding disintegration using ribose-modified ATP analogs, anthraniloylATP, and methylanthraniloylATP. The extent of sliding disintegration was proportional to the analog concentration. Thus in contrast to ATP, higher analog concentration was not inhibitory. These results indicate that high ATP concentration acts to inhibit the extent of sliding disintegration and that ADP relieves this inhibition. We propose a model in which the affinity of multiple cooperative active sites are regulated by binding of ATP or ADP to a regulatory site. This model provides a mechanism by which nucleotides regulate the extent of sliding necessary for effective axonemal bending. © 1995 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 161-168 
    ISSN: 0886-1544
    Keywords: fluorescent nucleotide analogs ; methylanthraniloyl ATP ; anthraniloyl ATP ; Chlamydomonas ; axonemal mutants ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Substrate analogs are useful for studying the structures of active sites and for distinguishing between similar enzyme activities. Fluorescent ribose-modified ATP analogs were used to investigate the functional differences between dynein ATPases. These analogs reactivate (support the movement of) sea urchin sperm axonemes, yet they do not reactivate wild-type Chalmydomonas axonemes. Surprisingly, the analogs reactivate the axonemes of mutants completely missing the outer arm dyneins. Competition experiments using ATP and these analogs provide strong evidence that the analogs bind to all dynein active sites but fail to release a subset of dyneins from rigor. We suggest that this subset of Chlamydomonas outer arm dyneins unable to use the analogs remains in rigor in the presence of the analogs and paralyzes the axoneme. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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