Comparison of H+-ATPase and Ca2+-ATPase suggests that a large conformational change initiates P-type ion pump reaction cycles
Open Access
- 1 July 1999
- journal article
- research article
- Published by Elsevier in Current Biology
- Vol. 9 (13) , 672-679
- https://doi.org/10.1016/s0960-9822(99)80307-8
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Structural Mechanism of Muscle ContractionAnnual Review of Biochemistry, 1999
- Structural organization, ion transport, and energy transduction of P-type ATPasesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1996
- Contributions of chemical derivatization and spectroscopic studies to the characterization of the Ca2+ transport ATPase of sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1992
- The plasma membrane H+ ‐ATPase from yeastEuropean Journal of Biochemistry, 1991
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Structural basis for E1–E2 conformational transitions in Na, K-pump and Ca-pump proteinsThe Journal of Membrane Biology, 1988
- Structure and function of proton translocating ATPase in plasma membranes of plants and fungiBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1988
- Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequencesCell, 1986
- Mechanism of the sarcoplasmic reticulum calcium pump. Fluorometric study of the phosphorylated intermediatesBiochemical and Biophysical Research Communications, 1978
- Possible functional states of the enzyme of the sarcoplasmic calcium pumpFEBS Letters, 1973