999 resultados para Napoleón III, Emperador de Francia, 1808-1873
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Mode of access: Internet.
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This is a continuation of Jean Baptiste Fellen's work, by an unknown author.
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Original compiled by Albert Fermé.
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Mode of access: Internet.
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Mode of access: Internet.
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Robert Wilhelm Ekman (1808-1873) oli Tukholmassa ja Pariisissakin opiskellut taidemaalari, joka kehitti Suomen taide-elämää ja erityisesti taidekoulutusta. Hänen monipuoliseen tuotantoonsa kuului kirkkotaidetta, kansankuvausta ja muinaissuomalaisia aiheita, joista tunnetuin on Ylioppilastaloon sijoitettu Väinämöisen soitto. Ekman tutustui myös Runebergiin ja kuvitti hänen aiheitaan, tässä pienessä kuvateoksessa Vänrikki Stålin tarinoita.
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UANL
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To investigate the molecular basis of the voltage sensor that triggers excitation–contraction (EC) coupling, the four-domain pore subunit of the dihydropyridine receptor (DHPR) was cut in the cytoplasmic linker between domains II and III. cDNAs for the I-II domain (α1S 1–670) and the III-IV domain (α1S 701-1873) were expressed in dysgenic α1S-null myotubes. Coexpression of the two fragments resulted in complete recovery of DHPR intramembrane charge movement and voltage-evoked Ca2+ transients. When fragments were expressed separately, EC coupling was not recovered. However, charge movement was detected in the I-II domain expressed alone. Compared with I-II and III-IV together, the charge movement in the I-II domain accounted for about half of the total charge (Qmax = 3 ± 0.23 vs. 5.4 ± 0.76 fC/pF, respectively), and the half-activation potential for charge movement was significantly more negative (V1/2 = 0.2 ± 3.5 vs. 22 ± 3.4 mV, respectively). Thus, interactions between the four internal domains of the pore subunit in the assembled DHPR profoundly affect the voltage dependence of intramembrane charge movement. We also tested a two-domain I-II construct of the neuronal α1A Ca2+ channel. The neuronal I-II domain recovered charge movements like those of the skeletal I-II domain but could not assist the skeletal III-IV domain in the recovery of EC coupling. The results demonstrate that a functional voltage sensor capable of triggering EC coupling in skeletal myotubes can be recovered by the expression of complementary fragments of the DHPR pore subunit. Furthermore, the intrinsic voltage-sensing properties of the α1A I-II domain suggest that this hemi-Ca2+ channel could be relevant to neuronal function.
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Mode of access: Internet.
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ICCU,
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Mode of access: Internet.
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Mode of access: Internet.
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With memoir.