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  • 1
    Electronic Resource
    Electronic Resource
    X-ray titration of binding of β, γ-imido-ATP to myosin in insect flight muscle (1976)
    [s.l.] : Nature Publishing Group
    Nature 262 (1976), S. 613-615 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Unfortunately both structural signs can be faulted, the electron microscopy because of the possibility of fixation or postfixation changes6, and the X-ray diffraction because of the long time which was used to obtain the required exposures2,4. We have tried to overcome these objections by observing ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/262613a0
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence concerning Crossbridge Attachment during Muscle Contraction (1970)
    [s.l.] : Nature Publishing Group
    Nature 226 (1970), S. 1060-1061 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Insect flight muscle was used in these experiments. The myofilaments in this muscle are very well ordered4 so that reproducible intensity measurements are possible. When extracted with glycerol the muscle can be either relaxed, Ca2+ activated or placed into rigor at will, by changing the bathing ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2261060a0
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  • 3
    Electronic Resource
    Electronic Resource
    Induced Changes in Orientation of the Cross-Bridges of Glycerinated Insect Flight Muscle (1965)
    [s.l.] : Nature Publishing Group
    Nature 207 (1965), S. 1276-1280 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] MYOGENIC fibrillar insect flight muscle is known to perform considerable work by means of small-amplitude oscillations both in life1 and when glycerinated2. The structure of the muscle is exceptionally well ordered3"4. Electron microscope studies indicate that the ends of the myosin filaments are ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2071276a0
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  • 4
    Electronic Resource
    Electronic Resource
    The Crossbridge Theory (1979)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 41 (1979), S. 723-736 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.41.030179.003451
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  • 5
    Electronic Resource
    Electronic Resource
    Evidence of Crossbridge Movement during Contraction of Insect Flight Muscle (1969)
    [s.l.] : Nature Publishing Group
    Nature 222 (1969), S. 1184-1185 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fibres of glycerol-extracted flight muscle from the water-bug Lethocerus cordofanus, provided with MgATP and Ca2+ and subjected to a forced longitudinal oscillation, will work in a way analogous to their performance during flight; in optimal conditions a large part of the myosin is activated in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2221184a0
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  • 6
    Electronic Resource
    Electronic Resource
    Movement and force produced by a single myosin head (1995)
    [s.l.] : Nature Publishing Group
    Nature 378 (1995), S. 209-212 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Previous studies7 9, under conditions in which several molecules are interacting with the actin filament, indicated that both SI and single-headed myosin are capable of generating movement and force. To demonstrate that such events occur between a single myosin head and an actin monomer, we have ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/378209a0
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  • 7
    Electronic Resource
    Electronic Resource
    Interpretation of Skin Impedance Measurements (1965)
    [s.l.] : Nature Publishing Group
    Nature 205 (1965), S. 600-601 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig, 1. Impedance of akin in contact with 0.9 per cent sodium chloride as a function of frequency of applied alternating current I have investigated how the impedance to low-frequency a.c. recorded from skin is influenced by the way in which contact is made with the skin surface. A circular metal ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/205600a0
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  • 8
    Electronic Resource
    Electronic Resource
    GTP γ causes contraction of skinned frog skeletal muscle via the DHP-sensitive Ca2+ channels of sealed T-tubules (1991)
    Springer
    Pflügers Archiv 418 (1991), S. 137-143 
    Details
    ISSN: 1432-2013
    Keywords: Skeletal muscle ; Skinned fibres ; Tension activation ; Excitation-contraction coupling ; GTP γ S ; G-Proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have investigated the involvement of G-proteins in excitation-contraction coupling of fast-twitch skeletal muscle, using a fibre preparation designed to retain intact T-tubules and sarcoplasmic reticulum. The nonhydrolysable analogue of guanosine triphosphate, GTP γ S (50–500 μM) caused a strong, transient isometric contraction in this preparation. Reduction of ethylene-bis(oxonitrilo) tetraacetete (EGTA) in the sealed T-tubules from 5 mM to 0.1 mM lowered the threshold to GTP γ S and removal of sodium reversibly raised it. The dihydropyridine (DHP) calcium channel antagonists nicardipine and nifedipine allowed a first contraction and then blocked subsequent GTP γ S action. The phenylalkylamine methoxyverapamil (D-600) did likewise, reversibly, at 10° C. The guanosine diphosphate analogue, GDP β S, and procaine reversibly blocked the action of GTP γ S pertussis toxin also blocked it. Photolytic release of 40–100 μM GTP γ S within 0.1 s from S-caged GTP γ S caused contraction after a latent period of 0.3–20 s. We conclude that GTP γ S can activate contraction in frog skeletal muscle via a route requiring both the integrity of the T-tubular DHP-sensitive calcium channel (DHPr) and the presence of sodium in the sealed T-tubules. We propose that in this preparation GTP γ S activates a G-protein, which in turn activates the DHPr as a calcium channel and releases stored calcium from within the sealed T-tubule. Implications of these results for the excitation-contraction coupling mechanism in skeletal muscle are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00370462
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  • 9
    Electronic Resource
    Electronic Resource
    Isoproterenol and GTPγS inhibit L-type calcium channels of differentiating rat skeletal muscle cells (1993)
    Springer
    Journal of muscle research and cell motility 14 (1993), S. 341-346 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In adult skeletal muscle, G-proteins have been shown to modulate the calcium channels both directly and through a cAMP-dependent phosphorylating mechanism. We have investigated the action of G-proteins on the L-type calcium current in cultured rat muscle cells (myoballs) under voltage clamp in whole cell or perforated patch modes. Intracellular photolytic release of 200 μM GTPγS inhibited the L-type calcium current. Inclusion of 500 μM uncaged GTPγS in the patch pipette in the whole cell configuration reduced the calcium current by a similar amount. Under perforated patch conditions external application of 10 μM of the β-adrenergic agonist isoproterenol also reduced the calcium current. Pretreatment of the cells with pertussis toxin reversed the effect of GTPγS and removed that of isoproterenol. We conclude that rat myoballs contain β-adrenergic receptors that inhibit the L-type calcium current, and that this inhibition is mediated by a pertussis toxinsensitive G-protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00123099
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  • 10
    Electronic Resource
    Electronic Resource
    Thirty-fifth Annual Meeting of the Society of General Physiologists, Woods Hole, Massachusetts, September 1981 (1981)
    Springer
    Journal of muscle research and cell motility 2 (1981), S. 345-345 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00711964
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