Transmembrane segment M3 is essential to thapsigargin sensitivity of the sarcoplasmic reticulum Ca(2+)-ATPase.
Open Access
- 1 October 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (43) , 26598-26601
- https://doi.org/10.1016/s0021-9258(18)47057-3
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Chimeric Ca2+‐ATPase/Na+,K+‐ATPase moleculesFEBS Letters, 1993
- Characterisation of ATP binding inhibition to the sarcoplasmic reticulum Ca2+‐ATPase by thapsigarginFEBS Letters, 1993
- The amino-terminal 200 amino acids of the plasma membrane Na+,K+-ATPase alpha subunit confer ouabain sensitivity on the sarcoplasmic reticulum Ca(2+)-ATPase.Proceedings of the National Academy of Sciences, 1993
- Functional consequences of alterations to Pro328 and Leu332 located in the 4th transmembrane segment of the α‐subunit of the rat kidney Na+,K+‐ATPaseFEBS Letters, 1992
- Mechanism of inhibition of the calcium pump of sarcoplasmic reticulum by thapsigarginBiochemical Journal, 1992
- Functional evidence of a transmembrane channel within the Ca2+ transport ATPase of sarcoplasmic reticulumFEBS Letters, 1992
- Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase.Proceedings of the National Academy of Sciences, 1990
- Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequenceNature, 1985
- Rapid and efficient site-specific mutagenesis without phenotypic selection.Proceedings of the National Academy of Sciences, 1985
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977