A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.
A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.
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来自质膜 Ca2 泵 ATP 酶的 C 末端钙调蛋白样调节域。
DOI：
10.1073/pnas.85.9.2914
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发表时间：
1988
影响因子：
11.1
通讯作者：
Vanaman,TC
中科院分区：
文献类型：
--
作者：
Brandt,P;Zurini,M;Neve,RL;Rhoads,RE;Vanaman,TC
A cDNA that encodes what appears to be the inhibitory domain of the plasma membrane calcium-pumping ATPase (Ca2+-ATPase) has been isolated by screening a lambda gt11 bovine brain cDNA library with antibodies prepared against the human erythrocyte membrane Ca2+-ATPase. This screening resulted in isolation of a bacteriophage containing a 1.5-kilobase cDNA insert encoding a 71-residue polypeptide, the remainder being a large 3' terminal noncoding region. A portion of this deduced peptide sequence was identical to that of a peptide isolated from a V8 protease digest of the human erythrocyte Ca2+-ATPase except for 1 residue. Antibodies purified by immunoabsorption to the fusion protein containing this cDNA-encoded polypeptide reacted only with those fragments of a limited trypsin digest of the human erythrocyte Ca2+-ATPase that contain the inhibitory domain. Moreover, these antibodies were able to partially stimulate basal enzyme activity and block further activation by calmodulin. The encoded polypeptide bears homology to the glutamic acid-rich regions N-terminal to the Ca2+-binding loops of calmodulin and to a lesser extent with the loops themselves. This encoded polypeptide also represents the C terminus of the Ca2+-ATPase. Portions of the isolated cDNA were homologous to the 3' noncoding region of the sarcoplasmic reticulum Ca2+-ATPase cDNA, indicating a possible mechanism for the evolution of these distinct membrane Ca2+ pumps.
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影响因子：
4.8
作者：
A. Edelman;Koji Takio;Donald K. Blumenthal;R. Hansen;Kenneth A. Walsh;K. Titani;E. Krebs
通讯作者：
E. Krebs
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DOI：
10.1016/s0021-9258(17)39754-5
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
G. Benaim;M. Zurini;E. Carafoli
通讯作者：
E. Carafoli
使用钙调蛋白亲和柱从人红细胞膜中纯化 (Ca2 -Mg2 )-ATP 酶。
影响因子：
4.8
作者：
V. Niggli;J. T. Penniston;E. Carafoli
通讯作者：
E. Carafoli
作为钙调蛋白功能探针的特定化学修饰。
影响因子：
--
作者：
D. Mann;T. Vanaman
通讯作者：
T. Vanaman
使用与琼脂糖偶联的钙调蛋白片段进行选择性亲和层析。
DOI：
10.1016/s0021-9258(18)88876-7
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
W. Ni;C. Klee
通讯作者：
C. Klee