ライフサイエンスコーパス: insulin receptor tyrosine kinase

1 IRS1 and IRS2 are key substrates of the insulin receptor tyrosine kinase.

2 ys a positive role in phosphorylation by the insulin receptor tyrosine kinase.

3 a potent counterregulatory inhibitor of the insulin receptor tyrosine kinase.

4 n on Tyr(488) in its cytoplasmic tail by the insulin receptor tyrosine kinase.

5 dependent protein kinase rather than that of insulin receptor tyrosine kinase.

6 onalized from a known x-ray structure of the insulin receptor tyrosine kinase.

7 pus oocytes and then activated the intrinsic insulin receptor tyrosine kinase.

8 f insulin are initiated by activation of the insulin receptor tyrosine kinase.

9 of Abl based on the crystal structure of the insulin receptor tyrosine kinase.

10 ressed by hepatocytes, is a substrate of the insulin receptor tyrosine kinase.

11 RS-1 and -2) are important substrates of the insulin receptor tyrosine kinase.

12 protein (IRS-1) is a specific substrate for insulin receptor tyrosine kinase.

13 for small molecules that activate the human insulin receptor tyrosine kinase, a nonpeptidyl fungal m

14 Here, insulin-dependent insulin receptor tyrosine kinase activation was examined

15 Muscle insulin receptor tyrosine kinase activity (IR-TKA) incre

16 sible new mechanism for the amplification of insulin receptor tyrosine kinase activity in response to

17 The ability of LMWCr to stimulate insulin receptor tyrosine kinase activity is dependent o

18 Insulin receptor tyrosine kinase activity was depressed

19 uscle from insulin-resistant obese patients, insulin receptor tyrosine kinase activity was reduced be

20 cromol x kg[-1] x min[-1], P < 0.01), and in insulin receptor-tyrosine kinase activity (IR-TKA) (248

21 ntial downstream signaling components of the insulin receptor tyrosine kinase and that the PH domain

22 wn inhibitors of insulin-like growth factors/insulin receptor tyrosine kinases, do not modulate the e

23 pp120, a substrate of the insulin receptor tyrosine kinase, does not undergo ligan

24 that two naturally occurring mutants of the insulin receptor tyrosine kinase domain, Arg-1174 --> Gl

25 Here we show that the insulin receptor tyrosine kinase family, comprising Ir,

26 HIV Tar RNA, thymidylate synthase, kinesin, insulin receptor, tyrosine kinases, farnesyltransferase,

27 he cSrc-family tyrosine kinase (PP1), or the insulin receptor tyrosine kinase (genistein) markedly di

28 of the phosphorylated, activated form of the insulin receptor tyrosine kinase in complex with a pepti

29 horylation of the enzyme were blocked by the insulin receptor tyrosine kinase inhibitor AG1024.

30 Iinsulin was largely blocked by the insulin receptor tyrosine kinase inhibitor HNMPA-(AM)3 a

31 Signaling through the insulin receptor tyrosine kinase involves its autophosph

32 aling proteins, including substrates for the insulin receptor tyrosine kinase (IRS proteins).

33 U), hepatic glucose output (HGO), and muscle insulin receptor tyrosine kinase (IRTK) activation were

34 PC-1) has been identified as an inhibitor of insulin receptor tyrosine kinase (IRTK) activity.

35 Tub is a substrate of insulin receptor tyrosine kinase (IRTK) and leptin recep

36 heir abilities to selectively activate human insulin receptor tyrosine kinase (IRTK).

37 es, tyrosine phosphorylation of IRS-2 by the insulin receptor tyrosine kinase is not sufficient for m

38 pp120, a substrate of the insulin receptor tyrosine kinase, is a plasma membrane g

39 notion that the dominant-negative effect of insulin receptor tyrosine kinase mutations involves the

40 nd rapamycin, consistent with a role for the insulin receptor tyrosine kinase, phosphoinositide 3 (PI

41 Epidermal growth factor (EGF) and insulin receptor tyrosine kinases (RTKs) exemplify how r

42 portant intracellular molecules that mediate insulin receptor tyrosine kinase signaling.

43 to bind EspF(U) identified the SH3 domain of insulin receptor tyrosine kinase substrate (IRTKS), a fa

44 which is recruited to Tir via IRSp53 and/or insulin receptor tyrosine kinase substrate (IRTKS).

45 The scaffolding protein insulin receptor tyrosine kinase substrate p53 (IRSp53),

46 d, revealing that p58/53 is identical to the insulin receptor tyrosine kinase substrate p58/53 (IRSp5

47 These and previous studies with the insulin receptor tyrosine kinase suggest that receptor-t

48 eptor fused to the cytoplasmic domain of the insulin receptor tyrosine kinase to produce the chimeric

49 ut it is not essential to the ability of the insulin receptor tyrosine kinase to use IRS-2 as a subst