ライフサイエンスコーパス: IMPase

1 low sequence homology, they seem to activate IMPase-1 in a similar mode.

2 troduced extragenically despite being active IMPases.

3 e important to ascorbate synthesis, or as an IMPase important to Ins(1,4,5)P3 signal recycling.

4 A structural comparison of the two archaeal IMPases identified a hydrogen bonding network present in

5 lated regions (5'- and 3'-UTRs) of rat brain IMPase.

6 In summary, this lithium-sensitive brain IMPase mRNA has the following characteristics: a 5'-CpG-

7 Calbindin D28k (calbindin) and S100B enhance IMPase-1 activity.

8 rted Km (Ins P1) values for other eukaryotic IMPases (43-330 microM) or with a reported Km (L-Gal-1P)

9 the second member of this family, an FBPase/IMPase from Archaeoglobus fulgidus (AF2372), has been so

10 n ethyl nitrosourea mutant mouse library for IMPase gene (Impa) mutations and identified an Impa1 T95

11 ii IMPase, the disruption (e.g., A. fulgidus IMPase S171A or T174L) of which prevented the drop in K(

12 are strikingly similar to human hippocampal IMPase.

13 Electrophoretically homogeneous IMPase was prepared from three different sources: (i) bo

14 has significant sequence similarity to human IMPase and has most of its key active-site residues.

15 ording to the inositol depletion hypothesis, IMPase activity is assumed to be higher than normal in p

16 enhances macroautophagy by mTOR-independent (IMPase inhibition by lithium) and mTOR-dependent (mTOR i

17 fulgidus enzyme and not in the M. jannaschii IMPase, the disruption (e.g., A. fulgidus IMPase S171A o

18 utative carbohydrate response element) links IMPase mRNA to brain carbohydrate metabolic pathways.

19 t ebselen inhibits inositol monophosphatase (IMPase) and exhibits lithium-like effects in animal mode

20 hagy by inhibiting inositol monophosphatase (IMPase) and reducing inositol and IP3 levels.

21 Inositol monophosphatase (IMPase) catalyzes the hydrolysis of inositol monophospha

22 synthesized by myo-inositol monophosphatase (IMPase) from inositol monophosphate species.

23 hium sensitive myo-inositol monophosphatase (IMPase) is a pivotal enzyme which controls the levels of

24 gene, SuhB, is an inositol monophosphatase (IMPase) that is best known as a suppressor of temperatur

25 ur analysis of myo-inositol monophosphatase (IMPase), a key enzyme of brain inositol signaling, we fo

26 , we examined host inositol monophosphatase (IMPase), reduced levels of which have been implicated in

27 synthesis, nor the inositol monophosphatase (IMPase), which generates myo-inositol, are significantly

28 ough inhibition of inositol monophosphatase (IMPase).

29 Li inhibits inositol-monophosphatase (IMPase)-1.

30 Ins monophosphatase (IMPase; EC 3.1.3.25) activity is essential for the de no

31 and resembles myo-inositol monophosphatases (IMPases).

32 The ability of IMPase to use both inositol 1-phosphates and galactose 1

33 The enzymatic activity of IMPase is inhibited by lithium, a drug used for the trea

34 We show here that complete inhibition of IMPase has no effect on the morphogenesis of Xenopus emb

35 usly modulated through lithium inhibition of IMPase.

36 Treatment with Li(+), an inhibitor of IMPase, reduces its activity, but the mechanism by which

37 olecules interfering with the interaction of IMPase-1 with either of its activators will have Li-like

38 results indicate that lithium inhibition of IMPases at clinically relevant concentrations, may modul

39 uctures, the enzymatic reaction mechanism of IMPases is accustomed to fit the data for MtHPP.

40 -inositol-1-phosphate, the main substrate of IMPases.

41 showed a dimer organization similar to other IMPases, but with an altered interface suggesting that t

42 he effect of a blood-brain barrier-penetrant IMPase inhibitor on human central nervous system (CNS) f

43 Escherichia coli SuhB gene product possesses IMPase activity, which is also strongly inhibited by Li(

44 2+, Ba2+ ions as inhibitors demonstrate that IMPase is a single enzyme possessing the ability to hydr

45 n chromatographic analysis demonstrated that IMPase and galactose 1-phosphatase activities co-purify

46 TOR-independent autophagy, and we found that IMPase activity is significantly decreased in infected c

47 In contrast, the IMPase from Methanococcus jannaschii, an organism in whi

48 h RNA polymerase (RNA pol) that inhibits the IMPase catalytic activity of SuhB.

49 he temperature dependence of the K(m) of the IMPase activity in the cells.

50 is an 8-10-fold decrease in the K(m) of the IMPase for inositol phosphates between 75 and 85 degrees

51 We compared our in silico model of the IMPase-1/calbindin complex with the crystal structure of

52 In contrast to IMPase inhibition that enhances autophagy, GSK3beta inhi

53 s yet another carbohydrate pathway utilizing IMPase.

54 erminal domain, sharing little identity with IMPases, is responsible for the substrate specificity (i