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1 nular pH and thereby inhibiting pH-sensitive prohormone convertases.
2 e mechanisms of proprotein processing by the prohormone convertases.
3 th the cleavage specificities of PC1 and PC2 prohormone convertases.
4 es, particularly fungal kexins and mammalian prohormone convertases.
5 okaryotic and eukaryotic proteins, including prohormone-convertases.
6                  A candidate endoprotease is prohormone convertase 1 (PC1) also known as PC3, a Ca2+-
7 two different prohormone-processing enzymes, prohormone convertase 1 (PC1) and carboxypeptidase E, ha
8 al inhibitory peptides for recombinant mouse prohormone convertase 1 (PC1) and PC2 and to provide inf
9 ion for the neuropeptide processing enzymes, prohormone convertase 1 (PC1) and PC2, were determined.
10 ro-TRH by the actions of the endopeptidases, prohormone convertase 1 (PC1) and PC2.
11 a product of proopiomelanocortin (POMC), and prohormone convertase 1 (PC1) in granules at the tips of
12                                              Prohormone convertase 1 (PC1) mutations lead to obesity
13                   We have purified the mouse prohormone convertase 1 (PC1) pro-domain expressed in Es
14 ne distribution generally similar to that of prohormone convertase 1 (PC1), a peptide-processing endo
15  prohormone processing by the endopeptidase, prohormone convertase 1 (PC1).
16 types may be linked to reduced expression of prohormone convertase 1 (PC1).
17 duction of glucagon, alpha cells up-regulate prohormone convertase 1 (PC1/3) to generate GLP-1 and en
18                                              Prohormone convertase 1 (PC1; also known as PC3) is beli
19 pressed in p-FLCs were neuroendocrine genes: prohormone convertase 1 (PCSK1); neurotensin; delta/notc
20                    Purified proSAAS inhibits prohormone convertase 1 activity with an IC(50) of 590 n
21       They revealed that cholecystokinin and prohormone convertase 1 mRNA levels in cerebral cortex a
22 lve increased expression of cholecystokinin, prohormone convertase 1 or 5 mRNA.
23 had higher expression of cholecystokinin and prohormone convertase 1, 2, and 5 mRNA than male mice.
24 e ghrelin was produced by human furin, mouse prohormone convertase 1, and human prohormone convertase
25 rocesses PEN-LEN, an endogenous inhibitor of prohormone convertase 1, into products that do not inhib
26 AAS may represent an endogenous inhibitor of prohormone convertase 1.
27                                              Prohormone convertase 1/3 (also known as PCSK1/3) repres
28 at mouse beta-cells process proinsulin using prohormone convertase 1/3 (PC1/3) and then prohormone co
29 have demonstrated that (a) in mouse stomach, prohormone convertase 1/3 (PC1/3) is the endoprotease re
30  growth factor 15, and unexpectedly Tgr5 and prohormone convertase 1/3 gene expression in the ileum.
31 been identified, thus far, no small-molecule prohormone convertase 1/3 or prohormone convertase 2 (PC
32                                    Increased prohormone convertase 1/3 was detected in glucagon-posit
33 ption factor that controls the expression of prohormone convertase 1/3, therefore having an impact on
34                                              Prohormone convertases 1 (PC1) and 2 (PC2) are members o
35 te stimulating hormone, adrenocorticotropin, prohormone convertases 1 and 2 (PC1 and PC2) and the PC2
36 oproteolytically cleaved by enzymes known as prohormone convertases 1 and 2 (PC1 and PC2) to generate
37  maturation requires proteolytic cleavage by prohormone convertases 1 and 2 (PC1 and PC2).
38 y the action of two members of the family of prohormone convertases 1 and 2 (PC1 and PC2).
39 lisin-like serine endoproteases PC1 and PC2 (prohormone convertases 1 and 2), and furin.
40 evertheless, the POMC processing components, prohormone convertases 1, 2 and regulatory protein 7B2,
41 values for the related convertases PACE4 and prohormone convertase-1 (PC1) were 110 nm and 2.5 microm
42 ormone (pro-TRH) is initially cleaved by the prohormone convertase-1/3 (PC1/3) in the trans-Golgi net
43 mozygous for a deletion in the gene encoding prohormone convertase 2 (PC2) are generally healthy but
44 hermore, VHS-GAT-GFP-overexpression disrupts prohormone convertase 2 (PC2) autocatalytic cleavage, pr
45 og of the vertebrate neuroendocrine-specific Prohormone Convertase 2 (PC2) gene, and showed that amon
46  small-molecule prohormone convertase 1/3 or prohormone convertase 2 (PC2) inhibitors have been descr
47                                              Prohormone convertase 2 (PC2) is a member of the subtili
48                                              Prohormone convertase 2 (PC2) is a subtilisin-like prote
49 s two domains, a 21-kDa protein required for prohormone convertase 2 (PC2) maturation and a carboxyl-
50                                              Prohormone convertase 2 (PC2) plays an essential role in
51 ese enzymes are evolutionarily related, only prohormone convertase 2 (PC2) requires 7B2 for activatio
52 Here, gene-targeted mice producing defective prohormone convertase 2 (PC2) were used to examine the p
53 7B2 is required for the production of active prohormone convertase 2 (PC2), an enzyme involved in the
54 ein 7B2 has been implicated in activation of prohormone convertase 2 (PC2), an important neuroendocri
55                          The serine protease prohormone convertase 2 (PC2), principally involved in t
56 g prohormone convertase 1/3 (PC1/3) and then prohormone convertase 2 (PC2), this finding has not been
57 involved in the biosynthesis and activity of prohormone convertase 2 (PC2).
58 educes secretogranin II (SgII) processing by prohormone convertase 2 (PC2).
59                                  The loss of prohormone convertase 2 alters CCK processing in specifi
60 nin levels in these brain regions shows that prohormone convertase 2 is important for cholecystokinin
61                                              Prohormone convertase 2 is widely co-localized with chol
62 ere measured in dissected brain regions from prohormone convertase 2 knock-out mice.
63 emale mice were more affected by the loss of prohormone convertase 2 than male mice.
64   In Drosophila melanogaster, the homolog of prohormone convertase 2, dPC2 (amontillado), is required
65 man prohormone convertase 7 but not by mouse prohormone convertase 2.
66 ith an IC(50) of 590 nM but does not inhibit prohormone convertase 2.
67 he cDNA revealed that it corresponded to the prohormone convertase-2 (PC2) gene, which is involved in
68                                              Prohormone convertase-2 (PC2) is the only convertase tha
69 rd CPA substrates, but after incubation with prohormone convertase 4 the resulting protein was able t
70 , whereas the latter also expresses mRNA for prohormone convertase 5, an enzyme that cleaves pro-NT i
71 in, mouse prohormone convertase 1, and human prohormone convertase 7 but not by mouse prohormone conv
72 due to an alteration in carboxypeptidase and prohormone convertase activities and that this may lead
73 t of a decrease in both carboxypeptidase and prohormone convertase activities.
74 uding propeptide precursors, subtilisin-like prohormone convertases, amidated products, and receptors
75   Mass spectrometric analysis of a potential prohormone convertase and the amidated proGATI-derived p
76 tin, by sequential proteolytic processing by prohormone convertases and carboxypeptidase E.
77  sites cleaved by subtilisin-like proprotein/prohormone convertases and is shown to be specifically c
78 ly five contain consensus cleavage sites for prohormone convertases at both the C and N termini.
79                                              Prohormone convertases belonging to the subtilisin famil
80   Proinsulin loci included genes that affect prohormone convertases, beta-cell dysfunction, vesicle t
81 elix or reorganize as recently proposed in a prohormone-convertase complex?
82 man proteolytic peptide fragments cleaved by prohormone convertases, enabling the identification of n
83  inducible deletion of the genes for the two prohormone convertase enzymes that process proglucagon .
84 ulin, presence of glucose-sensing machinery, prohormone convertase expression, and a regulated secret
85 icity of proSAAS toward other members of the prohormone convertase family was determined.
86 y the recombinant subtilisin-like proprotein/prohormone convertase furin.
87               There is also the 5' exon of a prohormone convertase gene, possibly PACE4.
88 trate for PC5, thereby supporting a role for prohormone convertases in the activation of transforming
89 es are recognized and cleaved by one or more prohormone convertases in the first processing step to y
90  (proghrelin) into mature ghrelin in various prohormone convertase null mouse strains generated in ou
91 inal domains of PAM must undergo a series of prohormone convertase or alpha-secretase-mediated cleava
92 terized family of processing enzymes are the prohormone convertases or kexins, and these are responsi
93 protein that was previously found to inhibit prohormone convertase (PC) 1 and not PC2.
94 pointed to the subtilisin/kexin-like enzymes prohormone convertase (PC) 1, PC2, and PC5 as potential
95 icted alpha-helical loops and four potential prohormone convertase (PC) cleavage sites, was necessary
96                     Among the members of the prohormone convertase (PC) family, PC2 has a unique matu
97 s complex, requiring sequential actions of a prohormone convertase (PC), carboxypeptidase H, and pept
98                                              Prohormone convertases (PC) 1 and 2, enzymes found prima
99  that require proteolytic processing by the "prohormone convertase" (PC) family of endoproteases.
100  nescient helix loop helix 2 (NHLH2) and the prohormone convertase PC1 (encoded by PCSK1) were reduce
101 ced by proinsulin accumulation and decreased prohormone convertase PC1/3.
102 he major precursor processing endoproteases, prohormone convertases PC1 and PC2 in Cpe(fat) mice.
103  vaccinia viruses were used to coexpress the prohormone convertases PC1, PC2, PACE4, PC5-B, furin, or
104                                          The prohormone convertases PC1/3 and PC2 are eukaryotic seri
105 ne alpha-amidating mono-oxygenase (PAM), the prohormone convertases PC1/3, PC2, PC5 and the PC2 chape
106          Endoproteolysis is performed by two prohormone convertases, PC1 and PC2.
107                                          The prohormone convertases PC2 (SPC2) and PC3/PC1 (SPC3) are
108  effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cul
109 for the neuroendocrine subtilisin/kexin-like prohormone convertases, PC2 (SPC2) and PC1/3 (SPC3).
110 PP was incubated (0.5-16 h) with recombinant prohormone convertases, PC2 or PC3 at appropriate condit
111                                          The prohormone convertases (PCs) are an evolutionarily ancie
112                                              Prohormone convertases (PCs) are endoproteases that proc
113                                          The prohormone convertases (PCs) are serine proteinases resp
114                                          The prohormone convertases (PCs) are synthesized as zymogens
115                          The subtilisin-like prohormone convertases (PCs) contain an essential downst
116 ng enzymes: carboxypeptidase E (CPE) and the prohormone convertases (PCs) PC1/3 and PC2.
117 rent posttranslational modification enzymes, prohormone convertases (PCs), carboxypeptidase E, and pe
118  by members of the subtilisin-like family of prohormone convertases (PCs), which are either soluble o
119 f subtilisin-like endoproteases known as the prohormone convertases (PCs).
120                                          The prohormone convertases play important roles in the matur
121  is processed in parallel by subtilisin-like prohormone convertases prior to secretion.
122                                          The prohormone convertase SPC2 (PC2) participates in the pro
123 ) junction, catalyzed by the subtilisin-like prohormone convertases SPC3 (PC1/PC3) and SPC2 (PC2), re
124 lated secretory cells containing appropriate prohormone convertases, the hProCpepGFP construct underg
125 ity of S1P(983)-C differs from that of furin/prohormone convertases, two related proteases, in its mo
126 le catecholamines, and an optimal pH for the prohormone convertases which cleave hormone precursors.
127 e same cells express phc2, a neural specific prohormone convertase, which suggests that they form an
128 ibasic amino acid residues whose cleavage by prohormone convertases would give rise to additional pep

 
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