FK506 binding protein associated with the calcium release channel (ryanodine receptor).

TL;DR: The use of the calcineurin inhibitors—namely, FK506 and CsA, together with yeast genetics and the overexpression of calcineURin by transgenic mice, has established the critical roles of calcinesurin in the regulation of many cellular processes that are induced by changes in the concentration of intracellular Ca 2+ in response to external signals.

TL;DR: The hypothesis that chloroplast immunophilins have distinct and overlapping functions is supported as they serve as critical regulators in photosynthesis-related processes including the assembly of photosynthetic complexes and adaptation to various light intensities in the natural environment.

TL;DR: Results show that activated TRPC6 channels form the center of a dynamic multiprotein complex that includes PKC and calcineurin, which respectively phosphorylate and dephosphorylate the channels.

TL;DR: Findings indicate a new inhibitory function of FKBP12 as an adaptor molecule for the Smad7-Smurf1 complex to regulate the duration of the activin signal.

TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.

TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.

TL;DR: The results suggest that calcineurin is involved in a common step associated with T cell receptor and IgE receptor signaling pathways and that cyclophilin and FKBP mediate the actions of CsA and Fk506 by forming drug-dependent complexes with and altering the activity of calcineURin-calmodulin.