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1 tic processing by prohormone convertases and carboxypeptidase E.
2 nally processed to remove Arg31 and Arg32 by carboxypeptidase E.
3 and a C-terminal domain with 39% identity to carboxypeptidase E.
4 ignificant suppression of mRNA abundance for carboxypeptidase E, 14-3-3 protein and phosphoprotein en
5 ntified in the brains of mice lacking active carboxypeptidase E, a neuropeptide-processing enzyme.
6 s due to the absence of enzymatically active carboxypeptidase E, a peptide-processing exopeptidase.
7 processing intermediates from mice that lack carboxypeptidase E activity (Cpe fat/fat mice) due to a
8 from Cpe(fat)/Cpe(fat) mice; these mice lack carboxypeptidase E activity and this defect causes an ac
9 idase domain with 49% amino acid identity to carboxypeptidases E and N.
10 ation enzymes, prohormone convertases (PCs), carboxypeptidase E, and peptidyl alpha-amidating enzyme,
11     Because studies have identified membrane carboxypeptidase E as a sorting receptor for targeting p
12 jacent to the trans-Golgi network, contained carboxypeptidase E, chromogranin C, and IL-2, and had an
13 , and mature DCV cargoes such as insulin and carboxypeptidase E (CPE) accumulate near the trans-Golgi
14 nied by downregulation of genes encoding for carboxypeptidase E (CPE) and Interleukin 1B (IL1B) in th
15 ne encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the
16 es, including dipeptidyl peptidase 4 (DPP4), carboxypeptidase E (CPE) and prostate specific antigen (
17 ferent peptide precursor processing enzymes: carboxypeptidase E (CPE) and the prohormone convertases
18 med a yeast two-hybrid screen and identified carboxypeptidase E (CPE) as a binding partner for the mi
19 t on the expression of the convertase enzyme carboxypeptidase E (CPE) by inhibition of the eukaryotic
20 (here called Pomc-Foxo1(-/-) mice) increases Carboxypeptidase E (Cpe) expression, resulting in select
21                                              Carboxypeptidase E (CPE) facilitates the conversion of p
22   Several recently discovered members of the carboxypeptidase E (CPE) gene family lack critical activ
23                                          The carboxypeptidase E (CPE) gene is expressed in human lens
24 s point mutation in the coding region of the carboxypeptidase E (CPE) gene results in a loss of CPE a
25 ch a sorting receptor as membrane-associated carboxypeptidase E (CPE) in pituitary Golgi-enriched and
26                                 Inclusion of carboxypeptidase E (CPE) in the reaction greatly diminis
27                We have previously shown that carboxypeptidase E (CPE) is a novel regulator of the can
28                                              Carboxypeptidase E (CPE) is a prohormone-processing enzy
29                                     Membrane carboxypeptidase E (CPE) is a sorting receptor for targe
30                                              Carboxypeptidase E (CPE) is a sorting receptor that dire
31                                              Carboxypeptidase E (Cpe) is an enzyme that removes the c
32                                              Carboxypeptidase E (CPE) is involved in peptide processi
33                                              Carboxypeptidase E (CPE) is involved in the biosynthesis
34                                              Carboxypeptidase E (CPE) is involved in the biosynthesis
35                                A mutation of carboxypeptidase E (CPE), an enzyme active in the proces
36                      They have a mutation in carboxypeptidase E (CPE), an enzyme that converts prohor
37                                              Carboxypeptidase E (CPE), an exopeptidase involved in pr
38 ation initiation factor 4gamma1 (eIF4G1) and carboxypeptidase E (CPE)-dependent proinsulin processing
39  two basic residues in the sorting receptor, carboxypeptidase E (CPE).
40 d intracellular prohormone sorting receptor, carboxypeptidase E (CPE).
41                                              Carboxypeptidase E (CPE, EC 3.4.17.10) is an essential e
42 phic factor-alpha1 (NF-alpha1; also known as carboxypeptidase E, CPE), concomitant with enhanced fibr
43 y structure of BDNF and the sorting receptor carboxypeptidase E directs this neurotrophin to the regu
44 aturally occurring point mutation within the carboxypeptidase E gene that inactivates this enzyme, le
45          Cpefat mice carry a mutation in the carboxypeptidase E/H gene which encodes an exopeptidase
46 g enzymes, prohormone convertase 1 (PC1) and carboxypeptidase E, have been implicated in enhancing th
47 g by regulating cap-dependent translation of carboxypeptidase E in a 4EBP2/eIF4E-dependent manner.
48                                              Carboxypeptidase E is a major enzyme in the biosynthesis
49 a recently discovered 180-kDa membrane-bound carboxypeptidase E-like enzyme.
50 tion functions of novel N-terminal-truncated carboxypeptidase E/neurotrophic factor-alphal variants i
51 (AAV) delivery of Neurotrophic Factor-alpha1/Carboxypeptidase E (NF-alpha1/CPE) gene in hippocampus a
52  was approximately 10-fold lower than either carboxypeptidase E or D expressed using the same viral s
53 t the activity of enzymes other than PC1 and carboxypeptidase E, such as the enzyme SKI-1.
54 These data provide evidence that the lack of carboxypeptidase E, the sorting receptor, results in the
55 ing, we transfected a chimera of CPEDelta15 (carboxypeptidase E without the last 15 residues) and the