CALM cDNA ORF clone, Bos taurus(cattle)

Membrane translocation of TRPC6 channels and endothelial migration are regulated by calmodulin and PI3 kinase activation.
Chaudhuri P, Rosenbaum MA, Sinharoy P, Damron DS, Birnbaumer L, Graham LM
Proceedings of the National Academy of Sciences of the United States of America113(8)2110-5(2016 Feb)

Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.
He Y, Haque MM, Stuehr DJ, Lu HP
Proceedings of the National Academy of Sciences of the United States of America112(38)11835-40(2015 Sep)

CK2-regulated schwannomin-interacting protein IQCJ-SCHIP-1 association with AnkG contributes to the maintenance of the axon initial segment.
Papandr?ou MJ, Vacher H, Fache MP, Klingler E, Rueda-Boroni F, Ferracci G, Debarnot C, Pip?roglou C, Garcia Del Ca?o G, Goutebroze L, Dargent B
Journal of neurochemistry134(3)527-37(2015 Aug)

Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes.
Arnett DC, Persechini A, Tran QK, Black DJ, Johnson CK
FEBS letters589(11)1173-8(2015 May)

Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS).
Kaur P, Kiselar J, Yang S, Chance MR
Molecular & cellular proteomics : MCP14(4)1159-68(2015 Apr)

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.
Title: Membrane translocation of TRPC6 channels and endothelial migration are regulated by calmodulin and PI3 kinase activation.

calmodulin promotes catalysis by shaping the physical and temporal conformational behaviors of NOS.
Title: Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.

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
Title: Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes.

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.
Title: Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS).

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.
Title: Holoenzyme structures of endothelial nitric oxide synthase - an allosteric role for calmodulin in pivoting the FMN domain for electron transfer.