ライフサイエンスコーパス: carboxypeptidase E

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1 nally processed to remove Arg31 and Arg32 by carboxypeptidase E.

2 and a C-terminal domain with 39% identity to carboxypeptidase E.

3 ignificant suppression of mRNA abundance for carboxypeptidase E, 14-3-3 protein and phosphoprotein en

4 ntified in the brains of mice lacking active carboxypeptidase E, a neuropeptide-processing enzyme.

5 s due to the absence of enzymatically active carboxypeptidase E, a peptide-processing exopeptidase.

6 processing intermediates from mice that lack carboxypeptidase E activity (Cpe fat/fat mice) due to a

7 from Cpe(fat)/Cpe(fat) mice; these mice lack carboxypeptidase E activity and this defect causes an ac

8 idase domain with 49% amino acid identity to carboxypeptidases E and N.

9 ation enzymes, prohormone convertases (PCs), carboxypeptidase E, and peptidyl alpha-amidating enzyme,

10 Because studies have identified membrane carboxypeptidase E as a sorting receptor for targeting p

11 jacent to the trans-Golgi network, contained carboxypeptidase E, chromogranin C, and IL-2, and had an

12 nied by downregulation of genes encoding for carboxypeptidase E (CPE) and Interleukin 1B (IL1B) in th

13 ne encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the

14 ferent peptide precursor processing enzymes: carboxypeptidase E (CPE) and the prohormone convertases

15 med a yeast two-hybrid screen and identified carboxypeptidase E (CPE) as a binding partner for the mi

16 t on the expression of the convertase enzyme carboxypeptidase E (CPE) by inhibition of the eukaryotic

17 (here called Pomc-Foxo1(-/-) mice) increases Carboxypeptidase E (Cpe) expression, resulting in select

18 Several recently discovered members of the carboxypeptidase E (CPE) gene family lack critical activ

19 The carboxypeptidase E (CPE) gene is expressed in human lens

20 s point mutation in the coding region of the carboxypeptidase E (CPE) gene results in a loss of CPE a

21 ch a sorting receptor as membrane-associated carboxypeptidase E (CPE) in pituitary Golgi-enriched and

22 Inclusion of carboxypeptidase E (CPE) in the reaction greatly diminis

23 We have previously shown that carboxypeptidase E (CPE) is a novel regulator of the can

24 Carboxypeptidase E (CPE) is a prohormone-processing enzy

25 Membrane carboxypeptidase E (CPE) is a sorting receptor for targe

26 Carboxypeptidase E (CPE) is a sorting receptor that dire

27 Carboxypeptidase E (CPE) is involved in peptide processi

28 Carboxypeptidase E (CPE) is involved in the biosynthesis

29 Carboxypeptidase E (CPE) is involved in the biosynthesis

30 A mutation of carboxypeptidase E (CPE), an enzyme active in the proces

31 They have a mutation in carboxypeptidase E (CPE), an enzyme that converts prohor

32 two basic residues in the sorting receptor, carboxypeptidase E (CPE).

33 d intracellular prohormone sorting receptor, carboxypeptidase E (CPE).

34 Carboxypeptidase E (CPE, EC 3.4.17.10) is an essential e

35 phic factor-alpha1 (NF-alpha1; also known as carboxypeptidase E, CPE), concomitant with enhanced fibr

36 y structure of BDNF and the sorting receptor carboxypeptidase E directs this neurotrophin to the regu

37 aturally occurring point mutation within the carboxypeptidase E gene that inactivates this enzyme, le

38 Cpefat mice carry a mutation in the carboxypeptidase E/H gene which encodes an exopeptidase

39 g enzymes, prohormone convertase 1 (PC1) and carboxypeptidase E, have been implicated in enhancing th

40 g by regulating cap-dependent translation of carboxypeptidase E in a 4EBP2/eIF4E-dependent manner.

41 Carboxypeptidase E is a major enzyme in the biosynthesis

42 a recently discovered 180-kDa membrane-bound carboxypeptidase E-like enzyme.

43 was approximately 10-fold lower than either carboxypeptidase E or D expressed using the same viral s

44 t the activity of enzymes other than PC1 and carboxypeptidase E, such as the enzyme SKI-1.

45 These data provide evidence that the lack of carboxypeptidase E, the sorting receptor, results in the

46 ing, we transfected a chimera of CPEDelta15 (carboxypeptidase E without the last 15 residues) and the

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