Homology of Calcium-Modulated Proteins: Their Evolutionary and Functional Relationships
- 1 January 1988
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Molecular cloning of cDNA for caltractin, a basal body-associated Ca2+-binding protein: homology in its protein sequence with calmodulin and the yeast CDC31 gene product.The Journal of cell biology, 1988
- Two calmodulin genes are expressed in Arbacia punctulata: An ancient gene duplication is indicatedJournal of Molecular Biology, 1988
- Crystal structure of calmodulinJournal of Inorganic Biochemistry, 1986
- A novel calmodulin-like gene from the nematode Caenorhabditis elegansJournal of Molecular Biology, 1986
- Structure of the Spec1 gene encoding a major calcium-binding protein in the embryonic ectoderm of the sea urchin, Strongylocentrotus purpuratusJournal of Molecular Biology, 1985
- Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteinsJournal of Molecular Evolution, 1979
- An iterative approach from the standpoint of the additive hypothesis to the dendrogram problem posed by molecular data setsJournal of Theoretical Biology, 1973
- A method for constructing maximum parsimony ancestral amino acid sequences on a given networkJournal of Theoretical Biology, 1973
- The amino acid sequence of the major parvalbumin from hake muscleBiochemical and Biophysical Research Communications, 1971
- A Crystalline Constituent from Myogen of Carp MusclesNature, 1952