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CA2 — PVALB

Text-mined interactions from Literome

Lee et al., J Physiol 2000 : The effect of parvalbumin (PV) on [Ca2+ ] transients was investigated by perfusing adrenal chromaffin cells with fura-2 and fluorescein isothiocyanate ( FITC ) -labelled PV
Collin et al., J Neurosci 2005 (Calcium Signaling) : Developmental changes in parvalbumin regulate presynaptic Ca2+ signaling
Estrada et al., J Cell Sci 2006 (Calcium Signaling) : Cytoplasmic parvalbumin blocked Ca2+ signaling in both compartments ; nuclear parvalbumin blocked only nuclear signals
Pette et al., Med Sci Sports Exerc 1984 : Simultaneously, cytosolic Ca2+ binding and Ca2+-sequestration are reduced by a decrease in parvalbumin and a transformation of the sarcoplasmic reticulum membranes
Iio et al., J Biochem 1984 : The rate constant of the conformational change of parvalbumin induced by Ca2+ binding or removal decreases in the order of component 2 greater than component 1 greater than component 5 greater than or equal to component 3 ; that is, component 2 undergoes the fastest conformational change and component 3 the slowest in response to the rapid free Ca2+ concentration ([Ca2+]) change in the protein solution
Sudhakar et al., Biochemistry 1995 : For Ca ( 2+ ) -bound parvalbumin in the presence of excess Ca2+ , the decay of the triplet state tryptophan is approximately exponential, and the lifetime decreases from 6.5 to 3.8 ms as the temperature increases from 10 to 40 degrees C
Ushio et al., Biochem Biophys Res Commun 1994 : Immunoblotting using an anti-parvalbumin antibody revealed that parvalbumin bound to the light sarcoplasmic reticulum isolated from carp fast skeletal muscle in the presence of Ca2+