Papers on
calcineurin B
Hypercalcaemia in a Patient with 2p13.2-p16.1 Duplication.Ljunggren et al., Sweden. In Horm Res Paediatr, Jan 2016
CONCLUSION: We conclude that partial duplication of 2p can be associated with hypercalcaemia and hypercalciuria and hypothesise that the underlying mechanism is an increased extra-renal, parathyroid hormone-independent 25-hydroxyvitamin D 1α-hydroxylase activity, leading to raised amounts of 1,25-dihydroxyvitamin D. The increased enzymatic activity could possibly be caused by calcineurin B subunit-related macrophage stimulation.
Calcium signaling and biotic defense responses in plants.Poovaiah et al., Pullman, United States. In Plant Signal Behav, 2013
Alterations in the Ca(2+) concentration are sensed by Ca(2+)-binding proteins, including calmodulin, calcium-dependent protein kinases and calcineurin B-like proteins, which relay or decode the encoded Ca(2+) signals into specific cellular and physiological responses in order to survive challenges by pathogens.
The multiple faces of calcineurin signaling in Caenorhabditis elegans: development, behaviour and aging.Bandyopadhyay et al., Seattle, United States. In J Biosci, 2013
The C. elegans counterpart of the catalytic subunit, calcineurin A, cna-1/tax-6, and the regulatory subunit, calcineurin B, cnb-1, are known to express ubiquitously in multiple tissues including neurons.
CIB1 is a regulator of pathological cardiac hypertrophy.Molkentin et al., Cincinnati, United States. In Nat Med, 2010
Yeast two-hybrid screening for CIB1-interacting partners identified a related EF hand domain-containing protein, calcineurin B, the regulatory subunit of the prohypertrophic protein phosphatase calcineurin.
Calcineurin: form and function.Mertz et al., Rochester, United States. In Physiol Rev, 2000
It is a heterodimeric protein consisting of a catalytic subunit calcineurin A, which contains an active site dinuclear metal center, and a tightly associated, myristoylated, Ca(2+)-binding subunit, calcineurin B. The primary sequence of both subunits and heterodimeric quaternary structure is highly conserved from yeast to mammals.