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

TL;DR: The role of ryanodine receptors (RyRs) and their role in human diseases of heart, muscle, and brain was discussed in this article. But, their role was not discussed in this paper.

TL;DR: The RyR2-G230C mutant exhibits similar biophysical defects compared with previously characterized CPVT mutations: decreased binding of the stabilizing subunit calstabin2 and a leftward shift in the Ca2+ dependence for activation under conditions that simulate exercise, consistent with a “leaky” channel.

TL;DR: Each CPVT subtype and how CPVT mutations alter protein function, RyR2 calcium release channel regulation, and cellular calcium handling are reviewed and how therapy could be improved in the future is reviewed.

TL;DR: It is conceivable that calcium homeostasis and signaling are attractive targets for future insecticide discovery and the first examples proving the validity of this concept are specific peptide toxins blocking insect voltage-gated calcium channels and the new diamide insecticides targeting ryanodine-sensitive release channels.

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.