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Both FMRP (show FMR1 Proteins) deficiency in Fmr1 (show FMR1 Proteins)(I304N) mice and Fmr1 (show FMR1 Proteins) knockdown impeded the axonal delivery of miR (show MLXIP Proteins)-181d, Map1b (show MAP1B Proteins), and Calm1 (show Calm2 Proteins) and reduced the protein levels of MAP1B (show MAP1B Proteins) and calmodulin (show Calm2 Proteins) in axons.
The association of calcium-bound calmodulin (CaM (show Calm2 Proteins)) with DREAM is mediated by a short amphipathic amino acid sequence located between residues 29 and 44 on DREAM.
Calcium plays a role in regulating the expression and function of beta-adducin to sustain normal organization of the spectrin-based cytoskeleton and the differentiation properties in keratinocytes through the calmodulin/EGFR/cadherin signaling pathway.
Data suggest that Cys3602 in RyR2 (ryanodine receptor 2) plays important role in activation/termination of Ca2+ release, but it is not essential for calmodulin regulation of RyR2.
CaM (show Calm2 Proteins) plays an active role in shaping both the spatial and temporal aspects of calcineurin (show PPP3CA Proteins)-mediated calcium signaling.
Calm1 (show Calm2 Proteins) signaling pathway is essential for the migration of mouse precerebellar neurons.
Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail.
Using mass spectrometry this study identified calmodulin (show Calm2 Proteins) as a calcium-dependent GluN2A (show GRIN2A Proteins) binding partner.
new insights into the role of BTK (show BTK Proteins), an important target for autoimmune diseases, in B cell activation (show BLNK Proteins)
The relationships between the interaction of alphaCaMKII with CaM (show Calm2 Proteins) and the conformational change of alphaCaMKII, were investigated.
Up-regulation of miR (show MLXIP Proteins)-335 suppressed CaM protein expression in patients with acute ischemic stroke, and CaM was confirmed as a direct target of miR (show MLXIP Proteins)-335.
The unique properties of the CaM-F142L mutation may provide novel clues on how to suppress excessive RyR2 Ca(2+) release by manipulating the CaM-RyR2 interaction.
CaM is required for the regulation of lysosome/vacuole size by TRPML1 (show MCOLN1 Proteins), suggesting that TRPML1 (show MCOLN1 Proteins) may promote lysosome fission by activating CaM.
Calmodulin-induced dimerization of ER-alpha (show ESR1 Proteins) is required for estrogen-stimulated transcriptional activation by the receptor.
Data indicate that the IQGAP1 N-terminal fragment spanning residues 1-191 (CHDF) binds to both F-actin and Ca(2 (show CA2 Proteins)+)/calmodulin.
This study reports how phosphorylation of a regulatory site (Ser-500) integrates with Ca(2+) and CaM to influence eEF-2K activity.
Findings show that calmodulin (CaM) stimulates phosphoinositide-3-kinase (PI3K (show PIK3CA Proteins)) lipid kinase activity by binding MARCKS (show MARCKS Proteins) and displacing it from phosphatidylinositol 4,5-bisphosphate (PIP2) headgroups, thereby releasing free PIP2 that recruits active PI3K (show PIK3CA Proteins) to the membrane and serves as the substrate for the generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3).
CaM D129G mutation led to bradycardia in zebrafish and an arrhythmic phenotype.
These findings suggest that ENT1 (show SLC29A1 Proteins) is regulated via receptor-dependent calcium-linked pathways resulting in an alteration of purine flux, which may modulate purinergic signaling and influence NA drug efficacy.
Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1 (show TRPV1 Proteins)-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions.
This gene encodes a member of the EF-hand calcium-binding protein family. It is one of three genes which encode an identical calcium binding protein which is one of the four subunits of phosphorylase kinase. Two pseudogenes have been identified on chromosome 7 and X. Multiple transcript variants encoding different isoforms have been found for this gene.
, Calmodulin 1 (phosphorylase kinase, delta)
, phosphorylase kinase, delta subunit
, prepro-calmodulin 1