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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.
Competitive and non-competitive regulation of calcium-dependent inactivation in CaV1.2 (show CACNA1C Proteins) L-type Ca2 (show CA2 Proteins)+ channels by calmodulin and Ca2 (show CA2 Proteins)+-binding protein 1.
CaM binds two molecules of ER-alpha (show ESR1 Proteins) in a 1:2 complex and stabilizes ER-alpha (show ESR1 Proteins) 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 (show KRIT1 Proteins) phosphorylation at Tyr (show TYR Proteins)(99) by a Src (show SRC Proteins) family kinase and that phosphorylated CaM (show KRIT1 Proteins) activates PI3K to produce PIP3, which promotes TRPC6 (show TRPC6 Proteins) 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 (show KRIT1 Proteins) bound to eNOS (show NOS3 Proteins) reveal four distinct conformational states and single-molecule fluorescence trajectories show multiple fluorescence states with transitions between states
key regulatory role of CaM (show KRIT1 Proteins) involves the stabilization of structural intermediates and precise positioning of the pivot for the FMN (show FMN1 Proteins) domain tethered shuttling motion to accommodate efficient and rapid electron transfer in the homodimer of eNOS (show NOS3 Proteins).
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 (show KRIT1 Proteins) bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a (show MYO5A Proteins).
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 (show C9orf3 Proteins)-CaM (show KRIT1 Proteins) and the stepwise binding of the N lobe (show LTF Proteins) of CaM (show KRIT1 Proteins) to the suppressor domain are important elements of calcium/CaM (show KRIT1 Proteins) inhibition of IP(3)R (show ITPR1 Proteins)
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)