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  • 1
    Electronic Resource
    Electronic Resource
    Molecular diversity of cyclic nucleotide-gated cation channels (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 353 (1995), S. 1-10 
    Details
    ISSN: 1432-1912
    Keywords: Key words Cyclic nucleotide-gated channels ; Second messenger ; Cyclic GMP ; Calcium ; Nitric oxide ; Molecular cloning ; Gene family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cyclic nucleotide-gated cation channels (CNG channels) form a multi-gene family consisting of at least five distinct members (CNG1–5). Expression studies have indicated that only CNG1–3 are able to form functional homooligomeric channels. Although structurally related, the cDNAs of CNG4–5 fail to induce cyclic nucleotide-dependent currents when expressed alone. However, when co-expressed with CNG1–3 they confer some of the physiologically observed properties of native CNG channels which are absent from the homooligomeric CNG1–3 channels. CNG channels are expressed in several tissues and cell types pointing to a general function of these channels in a wide variety of cellular systems. There is now increasing evidence that a major function of CNG channels may consist in providing a second messenger-regulated pathway for Ca2+ influx.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168909
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The low-energy thermal excitation spectrum of nitrogen molecules adsorbed on Ni(110): Implications for molecular adsorption sites (1996)
    Springer
    Applied physics 62 (1996), S. 95-101 
    Details
    ISSN: 1432-0630
    Keywords: 34.50 ; 79.60
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The adsorption of N2 molecules on Ni(110) has been investigated by high-resolution He-atom energy-loss spectroscopy. Two external vibrations in the subthermal (〈 30 meV) energy regime at 5.75 and 4.5 meV have been observed and are shown to imply the existence of two different adsorption sites, which are assigned to an on-top and a bridge-site. This finding is at variance with the interpretation of data from electron energy loss spectroscopy and InfraRed (IR) spectroscopy, where only one mode of the internal stretch vibration v1 at frequencies is observed for the chemisorbed nitrogen molecules. A reanalysis of previously published high-resolution IR data reveals that the presence of the second unexpected adsorbate species correlates with a feature in the IR spectra, which previously has been assigned to N2 molecules adsorbed at defect sites. These findings reveal that in this case the external vibrations are significantly more sensitive to different adsorption sites than the internal vibration, the latter exhibiting a difference between on-top and bridge sites of less than 6 cm−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575707
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Expression and functional characterization of the cardiac L-type calcium channel carrying a skeletal muscle DHP-receptor mutation causing hypokalaemic periodic paralysis (1996)
    Springer
    Pflügers Archiv 431 (1996), S. 461-463 
    Details
    ISSN: 1432-2013
    Keywords: dihydropyridine receptor ; L-type calcium channel ; voltage sensor ; subunits ; patch clamp ; site-directed mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A histidine substitution for the outermost arginine in II/S4 of the α1 subunit of the human skeletal muscle dihydropyridine (DHP) receptor has been reported to cause hypokalaemic periodic paralysis (HypoPP). This mutation shifts the voltage dependence of L-type Ca current inactivation in myotubes from HypoPP patients by −40 mV without affecting activation. Based on the strong homology of II/S4 in cardiac and skeletal muscle α1, we introduced the corresponding mutation into the rabbit cardiac α1 subunit (R650H). Wild type (WT) and mutant constructs were transiently transfected in HEK cells together with β and α2δ subunits and Ca and Ba currents were studied using the whole-cell patch-clamp technique. In contrast to the results obtained from human myotubes, R650H produced a small (−5 mV) but significant shift of both the steady-state activation and inactivation curves. When external pH was increased from 7.4 to 8.4 in order to favour deprotonization of H650, the only difference between WT and mutant channels was a slightly reduced steepness of the inactivation curve. Additional cotransfection of the γ subunit which is only found in skeletal but not in heart muscle, shifted the inactivation curves of both WT and R650H by −20 mV. We conclude that R650 plays a different role in voltage-dependent gating of the cardiac L-type Ca channel than the corresponding residue in the human skeletal muscle L-type channel, since a distinct and selective effect on the midpoint voltage of steady-state inactivation could not be found for R650H.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02207287
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    Paper (German National Licenses)
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