The functional nature of calcium binding units in calmodulin, troponin C and parvalbumin
- 1 June 1985
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 114 (3) , 353-374
- https://doi.org/10.1016/s0022-5193(85)80171-5
Abstract
No abstract availableThis publication has 38 references indexed in Scilit:
- Drug interaction with calmodulin: The binding siteJournal of Theoretical Biology, 1983
- Pharmacological antagonism of calmodulinCanadian Journal of Biochemistry and Cell Biology, 1983
- High affinity binding of the mastoparans by calmodulinBiochemical and Biophysical Research Communications, 1983
- Phospholipid-sensitive calcium-dependent protein kinase: Inhibition by antipsychotic drugsBiochemical and Biophysical Research Communications, 1981
- Co-operativity and calcium/magnesium binding to troponin C and muscle calcium binding parvalbumin: An hypothesisJournal of Theoretical Biology, 1980
- Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteinsJournal of Molecular Evolution, 1979
- The amino acid sequence of bovine cardiac troponin-C. Comparison with rabbit skeletal troponin-CBiochemical and Biophysical Research Communications, 1975
- Structural homology of myosin alkali light chains, troponin C and carp calcium binding proteinNature, 1974
- Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequencesBiochemical and Biophysical Research Communications, 1974
- A molecular theory of lipid—protein interactions in the plasma lipoproteinsFEBS Letters, 1974