1992
DOI: 10.1016/0022-2836(92)90324-d
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Calmodulin structure refined at 1.7 Å resolution

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Cited by 688 publications
(787 citation statements)
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“…This is important because the gCaM we cloned differs in amino acid composition from CaM purified from giardial extracts by Munoz et al (22). The amino acid composition determined by Munoz et al (22) for bovine CaM also differed from the published bovine CaM sequence (28). We cannot explain these differences, but we have confirmed our sequence, and gCaM expressed in Escherichia coli was active in stimulating cAMP phosphodiesterase activity (data not shown).…”
Section: Resultssupporting
confidence: 71%
“…This is important because the gCaM we cloned differs in amino acid composition from CaM purified from giardial extracts by Munoz et al (22). The amino acid composition determined by Munoz et al (22) for bovine CaM also differed from the published bovine CaM sequence (28). We cannot explain these differences, but we have confirmed our sequence, and gCaM expressed in Escherichia coli was active in stimulating cAMP phosphodiesterase activity (data not shown).…”
Section: Resultssupporting
confidence: 71%
“…Calmodulin is a ubiquitously expressed Ca 2þ -binding protein that can bind four Ca 2þ ions through its four EF-hand domains (Chattopadhyaya et al 1992). This protein has been highly conserved throughout evolution, is found in all eukaryotes, and is 100% identical across all vertebrates at the amino acid level.…”
Section: Neuronal Functions Of Calmodulinmentioning
confidence: 99%
“…23 In the "double native" Gō potential used, both the apo (Ca 2+ -free) 24 and holo (Ca 2+ -bound) 25 structures are stabilized, so that occasional spontaneous transitions are observed between the two states.…”
Section: Calmodulinmentioning
confidence: 99%