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Asp (show ASIP Proteins)-CaM complex has a critical role in centrosome-pole cohesion and centrosome inheritance in neural stem cells
Basal body formation in the male testes and the production of functional sperm does not rely on the PLP-CaM interaction, whereas production of functional mechanosensory neurons does.
characterized the interdomain motions in the calcium-bound state of calmodulin (Ca(2 (show CA2 Proteins)+)-CaM) using NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations
Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V (show MYO5A Proteins).
null behavioral phenotype originates in the nervous system and involves a calmodulin function that requires calcium binding to all four sites of the protein
the direct interaction of melatonin with intact calcium-saturated CaM is calcium-dependent; Molecular dynamics simulations follow the dynamics of melatonin in the binding pocket of CaM
potential functional role for calmodulin in regulation of the glycolytic pathway
A mutation to the gene encoding calmodulin deregulates muscle contraction.
Drosophila CaM is able to fully activate inducible nitric oxide synthase (iNOS (show NOS2 Proteins)); moreover, iNOS (show NOS2 Proteins) activation by CaM, like neuronal NOS (show NOS1 Proteins), is not dependent on Ca2 (show CA2 Proteins)+ being bound to all four Ca2 (show CA2 Proteins)+-binding sites, but has specific and distinct requirements.
Calmodulin/CAMTA/Fbxl4 may mediate a long-term feedback regulation of the activity of Ca(2 (show CA2 Proteins)+)-stimulating G protein-coupled receptor (show GPBAR1 Proteins), which could prevent cell damage due to extra Ca(2 (show CA2 Proteins)+) influx.
These results rule out the calmodulin/MLCK (show MYLK Proteins) pathway as the missing regulator of cytokinesis in the C. elegans early embryo.
the conformational changes of calmodulin (show KRIT1 Proteins) upon Ca(2 (show CA2 Proteins)+) and mastoparan binding
MLCK (show MYLK Proteins) and calmodulin (CaM (show KRIT1 Proteins)) co-purify with unphosphorylated SMM from chicken gizzard, suggesting that they are tightly bound.
Calmodulin (CaM) has three separate nonallelic genes that encode for three identical proteins.
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 (show CALM1 Proteins) variants in a cohort of genetically elusive long QT syndrome, were determined.
CALM3 (show CALM1 Proteins) had the highest ranking in the 1629-gene LQTS nodal network of the 7 genes identified through our filtering process.
the association of EGFR (show EGFR Proteins), CALM3 (show CALM1 Proteins) and SMARCD1 (show SMARCD1 Proteins) gene polymorphisms with bone mineral density in white women, as conducted.
Differentiation paralleled the activation of Wnt5 (show WNT5A Proteins)/Calmodulin (show CALM1 Proteins) signalling by autocrine/paracrine intense secretion of Wnt5a (show WNT5A Proteins) and Wnt5b (show WNT5B Proteins)
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 (show CALM1 Proteins) III transcripts.
These findings demonstrate that physical interaction of CaM (show CALM1 Proteins) with recombinant and native 5-HT(2C) receptors is critical for G protein-independent, arrestin (show SAG Proteins)-dependent receptor signaling.
data suggest that the -34T>A CALM3 (show CALM1 Proteins) polymorphism is a modifier gene for Familial Hypertrophy Cardiomyopathy, potentially by affecting expression level of CALM3 (show CALM1 Proteins) and therefore Ca(2 (show CA2 Proteins)+)-handling and development of hypertrophy.
Molecular dynamics simulations of conformational transitions in calmodulin are presented.
The NMR data indicate that calcium-sensing calmodulin CaM binds HIV-1 MA via its N- and C-terminal lobes and induces a dramatic conformational change involving a significant loss of secondary and tertiary structure within MA.
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.
, hypothetical protein
, calmodulin protein
, calmodulin 2 (phosphorylase kinase, delta)-1
, calmodulin 2 (phosphorylase kinase, delta)-2
, calmodulin 2 (phosphorylase kinase, delta)
, calmodulin 2
, calmodulin 3
, prepro-calmodulin 3
, CaM Gamma 2
, cam mRNA