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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
5 he most deadly species of malaria, using the photoprotein aequorin as a bioluminescent label has been
7 pecifically, we have prepared mutants of the photoprotein aequorin containing single cysteine residue
9 lecules or peptides to the N-terminus of the photoprotein aequorin such that the binding characterist
12 jellyfish Aequorea victoria consists of the photoprotein aequorin, which contains the molecule coele
17 the AEQ system for cells expressing both the photoprotein and the GPCR target of interest has necessi
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
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
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
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
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
39 e members of a subfamily of Ca(2+)-regulated photoproteins that is a part of the larger EF-hand calci
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