ライフサイエンスコーパス: tautomycin

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1 not inhibited by the PP1-selective inhibitor tautomycin.

2 by Chamberlin in a prior total synthesis of tautomycin.

3 orbol dibutyrate or a phosphatase inhibitor, tautomycin.

4 Pretreatment of cultures with tautomycin, a protein phosphatase type 1 inhibitor, bloc

5 The sensitivity of PP1 toward tautomycin and calyculin A was markedly decreased, by as

6 This hypophosphorylation was inhibited by tautomycin and not by okadaic acid, suggesting the invol

7 fic inhibitors of PP2A (fostriecin) and PP1 (tautomycin and siRNA against the PP1alpha catalytic subu

8 P2A, including microcystin-LR, okadaic acid, tautomycin, and calyculin A.

9 rophosphate, sodium vanadate, cyclosporin A, tautomycin, and okadaic acid had no effect on osmotic st

10 P1 in complex with nodularin-R at 1.63 A and tautomycin at 1.70 A resolution.

11 r of mutants of Tyr-272 toward okadaic acid, tautomycin, calyculin A, microcystin-LR, nodularin, inhi

12 th the protein phosphatase 1 (PP1) inhibitor tautomycin increased phosphorylation of YB-1(Ser(102)) i

13 in TC uptake and cytosolic [Ca2+], and only tautomycin inhibited basal TC uptake.

14 ive inhibition of protein phosphatase 1 with tautomycin inhibited pRB phosphatase activity and mainta

15 Okadaic acid and tautomycin, inhibitors of PP1/2A, inhibited cAMP-mediate

16 Furthermore, since tautomycin is a linear non-peptide-based toxin, our repo

17 The synthesis of a C1-C21 subunit of tautomycin is described.

18 Tautomycin is one of the few toxins that reportedly pref

19 , I-2, NIPP-1, and several toxins, including tautomycin, microcystin-LR, calyculin A, and okadaic aci

20 Calyculin A and tautomycin, on the other hand, blocked SAMe and MTA-medi

21 of U373 cells with the phosphatase inhibitor tautomycin resulted in the accumulation of gB at the PM.

22 Therefore, these results suggest that a tautomycin-sensitive phosphatase regulates cell-specific

23 Therefore, the PP1:tautomycin structure is the first complex structure with

24 osphatases like okadaic acid, calyculin, and tautomycin suggest that heparin inhibits CaM kinase II p

25 r was more sensitive to okadaic acid than to tautomycin, suggesting the involvement of a PP2A-type en

26 Tautomycin (TTM) is a highly potent and specific protein

27 Tautomycin (TTM), a potent protein phosphatase inhibitor

28 s converted to the core spiroketal moiety of tautomycin upon acid treatment.

29 Tautomycin was also able to block the hypophosphorylatio

30 ree toxins (okadaic acid, microcystin-LR and tautomycin), which block PP1- and PP2A-type phosphatases

31 A, which also potently inhibits PP2A, versus tautomycin, which does not, only the former increased Th

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