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1 rphin A was prevented by aminopeptidases and neutral endopeptidase.
2 he first evidence that keratinocytes produce neutral endopeptidase.
3 idase A and B, chymotrypsin, subtilisin, and neutral endopeptidase.
4 muscle is due to interaction with the enzyme neutral endopeptidase.
5 oup, comprise the M13 subfamily of mammalian neutral endopeptidases.
6  shares homology to members of the family of neutral endopeptidases.
7 e molecules that simultaneously inhibit both neutral endopeptidase 24.1 (NEP) and ACE.
8 The cell surface zinc metalloproteinase CD10/neutral endopeptidase 24.11 ([NEP] neprilysin) functions
9 eptidases, namely aminopeptidase N (APN) and neutral endopeptidase 24.11 (NEP 24.11).
10 s, angiotensin I-converting enzyme (ACE) and neutral endopeptidase 24.11 (NEP) are the major kininase
11 plays high amino acid sequence identity with neutral endopeptidase 24.11 (NEP) especially at the cata
12 ration of action in vivo, the dual ECE-1 and neutral endopeptidase 24.11 (NEP) inhibitor, CGS 26303,
13 zofused macrocyclic lactams were designed as neutral endopeptidase 24.11 (NEP) inhibitors.
14                                              Neutral endopeptidase 24.11 (NEP) is a cell surface pept
15                                              Neutral endopeptidase 24.11 (NEP) is a cell-surface enzy
16                                              Neutral endopeptidase 24.11 (NEP) is a cell-surface pept
17                                              Neutral endopeptidase 24.11 (NEP) is a metalloprotease t
18                                         CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemedia
19 n the crystal structure of the ectodomain of neutral endopeptidase 24.11 (NEP).
20                                              Neutral endopeptidase 24.11 (NEP, CD10) is a cell-surfac
21 ty and a small, but significant, increase in neutral endopeptidase 24.11 activity in the cheek pouch,
22                           Because the enzyme neutral endopeptidase 24.11 is an important kininase in
23               Kell has closest homology with neutral endopeptidase 24.11, endothelin converting enzym
24 thway is under the control of three enzymes: neutral endopeptidases 24.11 (neprilysin) and 24.15 and
25                   Adjacent skin had a median neutral endopeptidase activity 4.34 x higher (p<0.001) t
26                                This elevated neutral endopeptidase activity in the skin and chronic u
27                                   The median neutral endopeptidase activity of proximal skin was 2.90
28                                   The median neutral endopeptidase activity of the ulcer margin was 1
29                                          The neutral endopeptidase activity was approximately 7-fold
30                                              Neutral endopeptidase activity was measured using a fluo
31 scular drug that simultaneously inhibit both neutral endopeptidase and angiotensin-converting enzyme
32 ANP and fsANP are preferentially degraded by neutral endopeptidase and serine peptidases, respectivel
33                      We investigated whether neutral endopeptidase could inhibit angiogenesis in vivo
34                     The cell surface enzyme, neutral endopeptidase, degrades substance P, thereby reg
35 in metabolism is dependent on degradation by neutral endopeptidase, dipeptidyl peptidase IV, and amin
36 lts from this investigation demonstrate that neutral endopeptidase (EC 3.4.24.11) is one of the major
37 terized using a monoclonal antibody to human neutral endopeptidase, EC 3.4.24.11.
38  carotid body is structurally similar to the neutral endopeptidase, EC 3.4.24.11.
39                         We hypothesized that neutral endopeptidase enzymatic activity is increased in
40                                              Neutral endopeptidase enzymatic bioactivity was demonstr
41                        We compared cutaneous neutral endopeptidase expression and enzymatic activity
42 he objectives of this study were to evaluate neutral endopeptidase expression in wounded and unwounde
43 d on Xp22.1, is homologous to members of the neutral endopeptidase family.
44                          The distribution of neutral endopeptidase in normal skin and wounded human s
45 vascular endothelial cells demonstrated that neutral endopeptidase inhibition significantly enhanced
46  Three strategies were tested: inhibition of neutral endopeptidase, inhibition of aldose reductase pl
47 se severity when given in combination with a neutral endopeptidase inhibitor (enhances endogenous nat
48 -135 and Gly-136, which was inhibited by the neutral endopeptidase inhibitor CGS24592 and heparin.
49            Through single coinjection of the neutral endopeptidase inhibitor phosphoramidon (PA), we
50 ibitor captopril, to -6.33 +/- 0.19 with the neutral endopeptidase inhibitor phosphoramidon and to -7
51 eletal muscle, we examined the effect of the neutral endopeptidase inhibitor phosphoramidon on the bi
52 ramiprilat (10(-4) mol/L, -21+/-2%), and the neutral endopeptidase inhibitor thiorphan (10(-4) mol/L,
53 (n = 10), phosphoramidon (a combined ECE and neutral endopeptidase inhibitor) and BQ-123 (an ETA rece
54 2), respectively, and thiorphan (a selective neutral endopeptidase inhibitor) reduced FBF by 15 +/- 5
55 n=87) versus the vasopeptidase (dual ACE and neutral endopeptidase) inhibitor omapatrilat 80 mg daily
56                          Clinical studies of neutral endopeptidase inhibitors and angiotensin II rece
57                                              Neutral endopeptidase is a cell surface enzyme that degr
58 the matrix metalloproteinase (MMP) family of neutral endopeptidases, is expressed in the skeleton dur
59                                              Neutral endopeptidase may terminate the proinflammatory
60                                              Neutral endopeptidase mRNA was detected in normal skin a
61 es like dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase (NEP) 24.11 severely compromises i
62 y was to establish the effect of oleacein on neutral endopeptidase (NEP) activity and other functions
63 both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) activity in vitro were obser
64 fections and HOXC6 overexpression identified neutral endopeptidase (NEP) and insulin-like growth fact
65 gest that insulin-degrading enzyme (IDE) and neutral endopeptidase (NEP) are involved in the extracel
66 s of angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) both in vitro and in vivo.
67                                              Neutral endopeptidase (NEP) degrades vasoactive peptides
68 f the natriuretic peptide (NP) receptors and neutral endopeptidase (NEP) in mediating and modulating
69                      The cell-surface enzyme neutral endopeptidase (NEP) inactivates both peptides.
70 e herein our efforts to identify a selective neutral endopeptidase (NEP) inhibitor as a potential tre
71                                              Neutral endopeptidase (NEP) is a cell surface enzyme fou
72                                              Neutral endopeptidase (NEP) is a cell-surface enzyme tha
73                                              Neutral endopeptidase (NEP) is a genetically distinct me
74                                              Neutral endopeptidase (NEP) is expressed on normal prost
75 as the expression of the SP-degrading enzyme neutral endopeptidase (NEP) is increased, compared to co
76  the angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) may produce greater benefits
77                                              Neutral endopeptidase (NEP) uses SP as a substrate to pr
78 ndrogen-sensitive LNCaP cells, which express neutral endopeptidase (NEP), but not in androgen-indepen
79 nt vasoconstrictor into its active form, and neutral endopeptidase (NEP), which is involved in termin
80 ors indicated that the previously identified neutral endopeptidase (NEP)-like activity is the major p
81 nstrated substrate preference for Ang I, was neutral endopeptidase (NEP)-like.
82  and absence of long-term oral inhibition of neutral endopeptidase (NEP).
83 kephalin, the natural substrate of the human neutral endopeptidase (NEP).
84 both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP).
85 nhibitors of the two zinc metallopeptidases, neutral endopeptidase (NEP, EC 3.4.24.11) and angiotensi
86                                              Neutral endopeptidase (NEP; CALLA, CD10, EC 3.4.24.11) i
87 ed plasma half-life due to its resistance to neutral-endopeptidase (NEP) digestion.
88 ich blocks angiotensin converting enzyme and neutral endopeptidase, on these endpoints.
89 common acute lymphoblastic leukemia antigen, neutral endopeptidase, or enkephalinase, can be used as
90 dipeptidyl carboxypeptidase (captopril), and neutral endopeptidase (phosphoramidon) dramatically incr
91                        By 28 d post wounding neutral endopeptidase staining again was detected only i
92 me required for kidney membranes or purified neutral endopeptidase to abolish ANP-dependent activatio
93                                              Neutral endopeptidase was localized by immunohistochemis
94                                 Staining for neutral endopeptidase was noted in the wound bed 6 h aft
95                                              Neutral endopeptidase was strikingly localized in normal
96 otein levels of the enzyme that degrades SP, neutral endopeptidase, were increased.
97                              Incubation with neutral endopeptidase, which degrades bombesin, or bombe
98 eptidase inhibitors inhibit ACE activity and neutral endopeptidase, which degrades natriuretic peptid
99 bits angiotensin-converting enzyme (ACE) and neutral endopeptidase, which degrades vasodilatory facto
100 at released opioids are primarily cleaved by neutral endopeptidase, with a lesser involvement of amin

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