Zobrazeno 1 - 10
of 254
pro vyhledávání: '"L. Beaugé"'
Publikováno v:
Proceedings of SPIE; 5/13/2019, Vol. 11070, p1107012-1-1107012-8, 8p
Akademický článek
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Autor:
L. Beaugé, R. Gathmann
Publikováno v:
Simulateurs et réacteurs.
Publikováno v:
Journal of Biological Chemistry. 269:18028-18036
Based on work of Post et al. (Post, R. L. Toda, G., and Rogers, F.N. (1975) J. Biol, Chem. 250, 691-701), we studied the E2 form reactivity of Na(+),K(+)-ATPase (EC 3.6.1.37) during Na(+)-ATPase turnover by following ATP hydrolysis with and without P
Publikováno v:
Journal of Neuroscience Research. 27:47-54
To gain insight into the mechanisms responsible for differentiation of hippocampal neurons growing in vitro, the effects of estrogen on neuritic development and on activity and distribution of isoforms of the Na,K-ATPase, were evaluated. Dissociated
Autor:
L, Beaugé
Publikováno v:
European journal of biochemistry. 268(21)
The reactivity towards Na+ and K+ of Na+/K+-ATPase phosphoenzymes formed from ATP and Pi during Na+-ATPase turnover and that obtained from Pi in the absence of ATP, Na+ and K+ was studied. The phosphoenzyme formed from Pi in the absence of cycling an
Publikováno v:
European journal of biochemistry. 268(2)
This work shows the existence of a phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) bound form of the cardiac sarcolemmal Na+/Ca2+ exchanger. That was demonstrated in Western blots and cross-immunoprecipitation by using specific antibodies again
Autor:
Reinaldo DiPolo, L Beaugé
Publikováno v:
The Journal of physiology. 487(1)
1. [Na+]o-dependent Ca2+ efflux (forward Na(+)-Ca2+ exchange), [32P]ATP wash-out curves and [ATP] were measured in internally dialysed squid giant axons at 17-18 degrees C. 2. We found that dialysing squid axons without ATP and with [Ca2+]i around 1
Autor:
A, Holgado, L, Beaugé
Publikováno v:
Glia. 14(2)
Cultured rat glial cells display a Na(+)-Ca2+ exchange system located at the plasma membrane levels. This was evidenced by the Na+ (i)-dependency of a Na+ (o)-inhibitable influx of Ca2+, or reversal exchange mode. This antiporter has an external site
Publikováno v:
The Journal of biological chemistry. 269(27)
Based on work of Post et al. (Post, R. L. Toda, G., and Rogers, F.N. (1975) J. Biol, Chem. 250, 691-701), we studied the E2 form reactivity of Na(+),K(+)-ATPase (EC 3.6.1.37) during Na(+)-ATPase turnover by following ATP hydrolysis with and without P