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Human Calmodulin 2 Protein expressed in Wheat germ - ABIN1347887
Lin, Hsieh, Lin, Fang, Yang, Tsai, Chiang, Pan, Chen: Label-free detection of protein-protein interactions using a calmodulin-modified nanowire transistor. in Proceedings of the National Academy of Sciences of the United States of America 2010
Impaired Ca(2+)-dependent inactivation in human cardiomyocytes as the plausible mechanism for Long QT Syndrome associated with 2 novel CaM mutations.
Authors successfully recapitulated the disease phenotypes of LQT15 and revealed that inactivation of LTCC currents was impaired in CALM2-N98S hiPSC model.
the spectrum and prevalence of pathogenic CaM variants in a cohort of genetically elusive long QT syndrome, were determined.
Calmodulin 2 Mutation N98S Is Associated with Unexplained Cardiac Arrest in Infants Due to Low Clinical Penetrance Electrical Disorders.
5 novel de novo CALM2 mutations in association with long-QT syndrome and exertioninduced arrhythmias.(p.N98S, p.N98I, p.D134H, p.D132E, p.Q136P)
CaM-2-ext interacts biochemically with the C-terminus of Ca(v)2.3 similar to the classical CaM-2 as shown by co-immunoprecipitation
Human calmodulin mutations disrupt calcium binding to the protein and are associated with cardiac arrest in early infancy.
The 1.35 A structure of Ca(2+)-bound calmodulin in complex with the DIII-IV linker of Na(V)1.5 suggests that Ca(2+)/CaM destabilizes binding of the inactivation gate to its receptor, biasing inactivation toward more depolarized potentials.
These findings suggest that the CALM2 gene may be a genetic determinant of hip Osteoarthritis.
P53 protein stimulates CAMII gene expression in 041 cells.
These results suggest that calmodulin plays a crucial role in the processes of Ca(2+)-induced neuronal cell death and the possibility that the blockage of calmodulin attenuates brain injury after cerebral ischemia.
Competitive and non-competitive regulation of calcium-dependent inactivation in CaV1.2 L-type Ca2+ channels by calmodulin and Ca2+-binding protein 1.
CaM binds two molecules of ER-alpha in a 1:2 complex and stabilizes ER-alpha dimerization.
Calmodulin is well known to modulate many cytoplasmic reactions; thus, its passage through gap junctions opens possibilities of additional means by which cells may be supplied with this signaling molecule, and by which their supply may be regulated.
These results provide genetic evidence of the involvement of a CAM gene in pollen germination and support the theory of functional diversification of the CAM gene family.
These findings suggest that lysoPC induces CaM phosphorylation at Tyr(99) by a Src family kinase and that phosphorylated CaM activates PI3K to produce PIP3, which promotes TRPC6 translocation to the cell membrane.
calmodulin promotes catalysis by shaping the physical and temporal conformational behaviors of NOS.
examination of Ca(+2)-calmodulin showing highly significant correlations between surface area and side-chain contact predictions for individual side chains and the crystal structure, is reported.
Fluorescence decays of fluorescently labeled CaM bound to eNOS reveal four distinct conformational states and single-molecule fluorescence trajectories show multiple fluorescence states with transitions between states
key regulatory role of CaM involves the stabilization of structural intermediates and precise positioning of the pivot for the FMN domain tethered shuttling motion to accommodate efficient and rapid electron transfer in the homodimer of eNOS.
The results provide a basic idea that could lead to the development of small peptides binding with high affinity to CaM and inhibiting Ca(2)-CaM complex formation in the future.
CaM is collapsed around the adenylyl cyclase 8 peptides that binds to CaM in an antiparallel orientation.
Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a.
Data indicate that the information obtained can enhance understanding of how CaM interacts with K-RasB in physiological environments.
we propose a model in which the partial unfolding of the suppressor domain by apo-CaM and the stepwise binding of the N lobe of CaM to the suppressor domain are important elements of calcium/CaM inhibition of IP(3)R
the rates of oxidation for both apo- and holo-CaM are essentially identical, suggesting the two assume similar structures.
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.
, phosphorylase kinase delta
, prepro-calmodulin 2
, calmodulin 2 (phosphorylase kinase, delta)