… expressed WT and mutant Kvβ subunits show that they confer … We find that the light-activated
redox reaction of the flavin … subunit Hk, which we show is a functional redox sensor in vivo. …

… β-synthase is shown with residues lining the active site being labeled and depicted in ball-and-stick
representation. Subunit … acids in both its α and β subunits to guide indole toward the …

… and elongation factors and several ribosomal subunits; cell stress proteins include several
… proteins include ATP synthase subunits and Complex I subunits; metabolic enzymes include …

… The redox-sensing cysteine residues and the disulfide bond formed between these cysteine
residues serve as redox-sensing … Cys 267 in α subunit and Cys 442 in β subunit activates …

… Furthermore, Dos is a tetramer in which each subunit has … β-α-β-α-β structural units, which
together form a parallel β-sheet flanked by α-helices 107 . In support of its role in redox sensing…

… We review the growing range of thiol redox sensor variants and their application in different
… in vivo sensing has been instrumental in changing our understanding of redox biology, …

… β-synthase is a heme-based redox sensor, which can modulate its activity under in vitro
conditions in response to changes in the ambient redox … β-synthase (63 kDa subunit MW) to a …

… Since the β 2 subunit modifies inactivation kinetics of the … the β 2 subunit binds to the alpha
subunit, redox modification of the Ca v 1.2 subunit could alter the behaviour of the β 2 subunit…

… between the dimeric subunits. Complementary site-… redox sensor in action establish a means
for slight differences in the nicotinamide charge, pucker, and orientation to signal the redox …

… , which has an open β-sheet A and can be stabilized by a disulfide bond between Cys-79
and Cys-161. Reduction of this disulfide bond results in closing of the β-sheet A and changing …