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Effects of perchlorate on depolarization-induced conformational changes in the junctional foot protein and Ca2+ release from sarcoplasmic reticulum.
Yano M, el-Hayek R, Ikemoto N. Yano M, et al. Among authors: ikemoto n. Biochemistry. 1995 Oct 3;34(39):12584-9. doi: 10.1021/bi00039a013. Biochemistry. 1995. PMID: 7548007
In order to gain further insights, we monitored the conformational change in the junctional foot protein (JFP), which presumably is an important intermediate step in E-C coupling [Yano, M., El-Hayek, R., & Ikemoto, N. (1995) J. Biol. Chem. 270, 3017-3021], using …
In order to gain further insights, we monitored the conformational change in the junctional foot protein (JFP), which presumably is an impor …
Rapid flow chemical quench studies of calcium release from isolated sarcoplasmic reticulum.
Ikemoto N, Antoniu B, Mészáros LG. Ikemoto N, et al. J Biol Chem. 1985 Nov 15;260(26):14096-100. J Biol Chem. 1985. PMID: 2414290
At low ATP (e.g. 0.2 mM) and low extravesicular [Ca2+] (e.g. 0.1 microM), the time course of depolarization-induced Ca2+ release was similar to that determined by a spectrophotometric method (Ikemoto, N., Antoniu, B., and Kim, D.H. (1984) J. Biol. Chem. 259, 13151-1 …
At low ATP (e.g. 0.2 mM) and low extravesicular [Ca2+] (e.g. 0.1 microM), the time course of depolarization-induced Ca2+ release was similar …
Transport and inhibitory Ca2+ binding sites on the ATPase enzyme isolated from the sarcoplasmic reticulum.
Ikemoto N. Ikemoto N. J Biol Chem. 1975 Sep 25;250(18):7219-24. J Biol Chem. 1975. PMID: 126233
Ca2+ binding sites located on the Ca2+-dependent ATPase purified from the fragmented sarcoplasmic reticulum (Ikemoto, N (1974) J. Biol. Chem. 249, 649) have been further studied. ...
Ca2+ binding sites located on the Ca2+-dependent ATPase purified from the fragmented sarcoplasmic reticulum (Ikemoto, N (1974) …
Behavior of the Ca2+ transport sites linked with the phosphorylation reaction of ATPase purified from the sarcoplasmic reticulum.
Ikemoto N. Ikemoto N. J Biol Chem. 1976 Nov 25;251(22):7275-7. J Biol Chem. 1976. PMID: 136449
Assuming that phosphorylation of the enzyme releases both Ca2+ bound to it (Ikemoto, N. (1975) J. Biol. Chem. 250, 7219), these data are consistent with the sequential formation of two acid-stable intermediates differing in Ca2+ affinity and a third acid-labile phos …
Assuming that phosphorylation of the enzyme releases both Ca2+ bound to it (Ikemoto, N. (1975) J. Biol. Chem. 250, 7219), thes …
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