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1 ge disk on which it is hydrolyzed by a yeast exopolyphosphatase.
2 the polyP-binding domain of Escherichia coli exopolyphosphatase.
3 ood fold similarity between NTPDase3 and the exopolyphosphatase.
7 t, in contrast to the yeast enzyme and other exopolyphosphatases investigated before, acts on polyP o
8 ion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of
10 of PPN1 and PPX1 (the gene encoding a potent exopolyphosphatase) loses viability rapidly in stationar
14 were reversed concomitantly when expressing exopolyphosphatase PPX from a recombinant plasmid, or by
16 synthesizes poly-P reversibly from ATP, (ii) exopolyphosphatase (PPX), which hydrolyzes poly-P to P(i
18 tis and Aquifex, PRUNE of Drosophila, and an exopolyphosphatase (PPX1) of Saccharomyces cereviseae.
21 convert poly P and ADP to ATP and of a yeast exopolyphosphatase that can hydrolyze poly P to Pi, prov
22 des for a 45 kDa, metal-dependent, cytosolic exopolyphosphatase that processively cleaves the termina
23 pGpp of the hydrolytic breakdown of polyP by exopolyphosphatase, thereby blocking the dynamic turnove
24 J motifs are shared between exonucleases and exopolyphosphatases, they may constitute an ancient phos
26 ctional enzyme that was similar to the yeast exopolyphosphatase with respect to its Mg(2+) requiremen
27 d after addition of Saccharomyces cerevisiae exopolyphosphatase X to the bilayer, providing functiona
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