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anti-Human Calmodulin 3 Anticorps:
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Study identified the structure and function of Ca2+-dependent interaction of CaM with the inactivation gate (IG) of NaV1.5 channels. Models of full-length NaV1.5 suggest that CaM binding to the IG directly modulates its function by destabilizing the inactivated state, which would promote resetting of the IG after channels close.
results suggest that ACE2, TNNI3K and CALM3 polymorphisms are associated with increased risk of hypertrophic cardiomyopathies and dilated cardiomyopathies and may act as disease modifiers of these diseases.
We discovered a novel CPVT mutation in the CALM3 gene that shares functional characteristics with established CPVT-associated mutations in CALM1. A small proportion of A103V-CaM is sufficient to evoke arrhythmogenic Ca disturbances via ryanodine receptor 2 dysregulation, which explains the autosomal dominant inheritance.
the spectrum and prevalence of pathogenic CaM variants in a cohort of genetically elusive long QT syndrome, were determined.
CALM3 had the highest ranking in the 1629-gene LQTS nodal network of the 7 genes identified through our filtering process.
the association of EGFR, CALM3 and SMARCD1 gene polymorphisms with bone mineral density in white women, as conducted.
Differentiation paralleled the activation of Wnt5/Calmodulin signalling by autocrine/paracrine intense secretion of Wnt5a and Wnt5b
The rat and mouse 3'-UTR region had an identity of approximately 80% with the human. Three common polyadenylation signals in the 3'-UTR may account for the multiple CaM III transcripts.
These findings demonstrate that physical interaction of CaM with recombinant and native 5-HT(2C) receptors is critical for G protein-independent, arrestin-dependent receptor signaling.
data suggest that the -34T>A CALM3 polymorphism is a modifier gene for Familial Hypertrophy Cardiomyopathy, potentially by affecting expression level of CALM3 and therefore Ca(2+)-handling and development of hypertrophy.
Calmodulin (CaM) has three separate nonallelic genes that encode for three identical proteins.
Results indicate that myosin V motility is regulated by Ca(2+) through a reduction in actin-binding affinity resulting from the dissociation of single calmodulin molecules.
Data show that a recombinant troponin C/calmodulin chimera, in which the carboxyl-terminal domain of TnC is replaced by that of CaM, has the same ability as CaM to bind and transmit the signal to calcium sites on the enzyme.
Results support the hypothesis that Ca(2)(+) binding to CaM's C-terminal acts as the switch converting CaM from a RyR1 activator into a channel inhibitor.
Results describe the mechanism of switching of alpha-calcium-calmodulin-dependent protein kinase II between two types of activity: Ca(2+)-independent partial activity and Ca(2+)/calmodulin-activated full activity.
Met124 was required for both high-affinity CaM binding to RyR2 and for maximal CaM inhibition. These results thus identify a Met residue critical for the productive association of CaM with RyR2 channels.
calmodulin behaves as an activator of ammodytoxin under both nonreducing and reducing (cytosol-like) conditions by stimulating its enzymatic activity up to 21-fold
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
, prepro-calmodulin 3
, Calmodulin III