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1 y effect on the luminescence activity of the photoprotein.
2 luminescence ordinarily observed from native photoproteins.
3 nt dyes, although the use of the recombinant photoprotein aequorin (AEQ) as a Ca(2+) sensor has gaine
4 ding protein (SBP) into the structure of the photoprotein aequorin (AEQ).
5 he most deadly species of malaria, using the photoprotein aequorin as a bioluminescent label has been
6 n in picoliter vials was developed using the photoprotein aequorin as the label.
7 pecifically, we have prepared mutants of the photoprotein aequorin containing single cysteine residue
8 cortisol in saliva, in which a mutant of the photoprotein aequorin has been used as a label.
9 lecules or peptides to the N-terminus of the photoprotein aequorin such that the binding characterist
10                            Specifically, the photoprotein aequorin was utilized for the detection of
11                     In the calcium-activated photoprotein aequorin, light is produced by the oxidatio
12  jellyfish Aequorea victoria consists of the photoprotein aequorin, which contains the molecule coele
13  calcium-dependent oxidation mediated by the photoprotein aequorin.
14 he bioluminescence emission generated by the photoprotein aequorin.
15 r carboxyl terminus to the calcium-sensitive photoprotein aequorin.
16                                         This photoprotein allows for the study of kinetic properties
17 the AEQ system for cells expressing both the photoprotein and the GPCR target of interest has necessi
18 s was tested with hydrogen peroxide to track photoprotein and/or protein-bound chromophore.
19                                              Photoproteins are attractive as labels in analytical app
20                                        These photoproteins are known to be globally distributed in th
21                               Ca2+-regulated photoproteins are members of the EF-hand calcium-binding
22 mide as the primary excited state product in photoprotein bioluminescence.
23 ntitative measurements of a Ca(2+)-activated photoprotein biosensor of recombinant OR function in an
24 s environment were recently shown to contain photoproteins called proteorhodopsins, thought to contri
25                                         This photoprotein consists of a stable complex of its apoprot
26    Transgenic fish with the Ca(2+)-sensitive photoprotein green fluorescent protein (GFP)-Aequorin in
27 nt molecules to fluorescent biomolecules and photoproteins ingeniously engineered to follow signaling
28 ow of the mucus from Chaetopterus involves a photoprotein, iron and flavins.
29 2 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of
30 inescence reaction in these Ca(2+)-regulated photoproteins may be a shift of the hydrogen bond donor-
31 h bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy sta
32 the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-A resolution.
33 as developed on the base of Ca(2+)-regulated photoprotein obelin mutants with altered color and kinet
34 njugate of this aptamer and Ca(2+)-regulated photoprotein obelin was obtained for the first time and
35              Aequorin is a calcium-sensitive photoprotein originally obtained from the jellyfish Aequ
36 ndent fitness contributions, which drive the photoprotein's lateral acquisition and retention, but co
37 rom re-binding of fresh chromophore to spent photoprotein, suggesting that a minority fraction of the
38                                Aequorin is a photoprotein that emits light at 469 nm and has been emp
39 e members of a subfamily of Ca(2+)-regulated photoproteins that is a part of the larger EF-hand calci
40 ased almost exclusively on a single class of photoproteins, the opsins.
41       However, despite extensive research on photoproteins, there has been no evidence to indicate th
42                       The gene encoding this photoprotein was originally discovered on a large genome
43                        Aequorin, a jellyfish photoprotein with Ca(2+)-dependent luminescence, measure

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