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1 ycogen synthase, glycogen phosphorylase, and phosphorylase kinase.
2 eas of contact between the alpha subunits of phosphorylase kinase.
3 olamban, troponin I, C protein, and glycogen phosphorylase kinase.
4 led to each other and with the activation of phosphorylase kinase.
10 s [cyclin-dependent protein kinase 2 (CDK2), phosphorylase kinase and glycogen synthase kinase 3beta]
11 has dual opposing enzymatic activities; OmpR-phosphorylase (kinase) and phospho-OmpR-dephosphorylase
13 ed by resorcinol (25 pmol/l), which inhibits phosphorylase kinase by a mechanism analogous to the ant
15 organization of the (alphabetagammadelta)(4) phosphorylase kinase complex has been studied using the
16 C terminus of the catalytic gamma-subunit of phosphorylase kinase comprises a regulatory domain that
17 C terminus of the catalytic gamma subunit of phosphorylase kinase contains two autoinhibitory calmodu
19 minant manner to completely inhibit glycogen phosphorylase kinase enzyme activity and that this inter
21 oxidation during ferroptosis, which involves phosphorylase kinase G2 (PHKG2) regulation of iron avail
25 Ca(2+) ions, of the (alphabetagammadelta)(4) phosphorylase kinase holoenzyme (PhK) alter the interact
26 icant effects on the catalytic activities of phosphorylase kinase holoenzyme and the gamma delta comp
27 These results suggest that activators of the phosphorylase kinase holoenzyme perturb interactions bet
28 n in the catalytic subunit of liver glycogen phosphorylase kinase in a patient with Mauriac syndrome
29 ause PTG also binds to glycogen synthase and phosphorylase kinase, it has been suggested that it serv
30 IMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the po
32 phorylase-b (P-b) and its only known kinase, phosphorylase kinase (PbK) and the relationship of this
33 ruses were created and used to coexpress rat phosphorylase kinase (Phk) alpha, gamma, and delta subun
41 es indicated that only the testis isoform of phosphorylase kinase (PhK-gammaT) was detectable in feta
42 PP1C to glycogen, PTG formed complexes with phosphorylase kinase, phosphorylase a, and glycogen synt
44 's mother possessed the same mutant glycogen phosphorylase kinase subunit, but did not have diabetes
45 in mRNAs for several glycolytic enzymes and phosphorylase kinase subunits, and dramatic increases in
46 ycogen synthase, glycogen phosphorylase, and phosphorylase kinase, thereby serving as molecular scaff
47 with residues 1-1059 of the alpha subunit of phosphorylase kinase, we have isolated 16 interacting, i
48 ne Ca-ATPase, a MARCKS homolog, and glycogen phosphorylase kinase were assessed using frequency-domai
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