A conformational mechanism for formation of a dead-end complex by the sarcoplasmic reticulum ATPase with thapsigargin.
Open Access
- 1 January 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (2), 1286-1292
- https://doi.org/10.1016/s0021-9258(18)48427-x
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Frequency-domain fluorescence spectroscopy resolves the location of maleimide-directed spectroscopic probes within the tertiary structure of the calcium ATPase of sarcoplasmic reticulumBiochemistry, 1991
- Role of Ca2+-ATPases in regulation of cellular Ca2+ signalling, as studied with the selective microsomal Ca2+-ATPase inhibitor, thapsigarginInflammation Research, 1990
- Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulumJournal of Molecular Biology, 1985
- The structure of the Ca2+ ATPase as revealed by electron microscopy and image processing of ordered arraysJournal of Ultrastructure Research, 1983
- Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+‐dependent adenosine triphosphatase of sarcoplasmic reticulumFEBS Letters, 1982
- Modulation of calcium binding in sarcoplasmic reticulum adenosinetriphosphataseBiochemistry, 1981
- Modification of the ATP binding site of the Ca2+‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanateFEBS Letters, 1981
- Two functional states of sarcoplasmic reticulum ATPaseBiochemistry, 1976
- Fluorescence studies of the sarcoplasmic reticulum calcium pumpBiochemical and Biophysical Research Communications, 1976
- Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ionsBiochemistry, 1973