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1 muscle is due to interaction with the enzyme neutral endopeptidase.
2 rphin A was prevented by aminopeptidases and neutral endopeptidase.
3 he first evidence that keratinocytes produce neutral endopeptidase.
4 idase A and B, chymotrypsin, subtilisin, and 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 c injury that treatment with GLP-1(28-36), a neutral endopeptidase-generated (NEP-generated) metaboli
45                          The distribution of neutral endopeptidase in normal skin and wounded human s
46 vascular endothelial cells demonstrated that neutral endopeptidase inhibition significantly enhanced
47  Three strategies were tested: inhibition of neutral endopeptidase, inhibition of aldose reductase pl
48 se severity when given in combination with a neutral endopeptidase inhibitor (enhances endogenous nat
49 -135 and Gly-136, which was inhibited by the neutral endopeptidase inhibitor CGS24592 and heparin.
50            Through single coinjection of the neutral endopeptidase inhibitor phosphoramidon (PA), we
51 ibitor captopril, to -6.33 +/- 0.19 with the neutral endopeptidase inhibitor phosphoramidon and to -7
52 eletal muscle, we examined the effect of the neutral endopeptidase inhibitor phosphoramidon on the bi
53 ramiprilat (10(-4) mol/L, -21+/-2%), and the neutral endopeptidase inhibitor thiorphan (10(-4) mol/L,
54 (n = 10), phosphoramidon (a combined ECE and neutral endopeptidase inhibitor) and BQ-123 (an ETA rece
55 2), respectively, and thiorphan (a selective neutral endopeptidase inhibitor) reduced FBF by 15 +/- 5
56 he transcriptome, and identified thiorphan-a neutral endopeptidase inhibitor-as a lead candidate.
57 n=87) versus the vasopeptidase (dual ACE and neutral endopeptidase) inhibitor omapatrilat 80 mg daily
58                          Clinical studies of neutral endopeptidase inhibitors and angiotensin II rece
59                                              Neutral endopeptidase is a cell surface enzyme that degr
60 the matrix metalloproteinase (MMP) family of neutral endopeptidases, is expressed in the skeleton dur
61                                              Neutral endopeptidase may terminate the proinflammatory
62                                              Neutral endopeptidase mRNA was detected in normal skin a
63 es like dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase (NEP) 24.11 severely compromises i
64 y was to establish the effect of oleacein on neutral endopeptidase (NEP) activity and other functions
65 both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) activity in vitro were obser
66 fections and HOXC6 overexpression identified neutral endopeptidase (NEP) and insulin-like growth fact
67 gest that insulin-degrading enzyme (IDE) and neutral endopeptidase (NEP) are involved in the extracel
68 s of angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) both in vitro and in vivo.
69                                              Neutral endopeptidase (NEP) degrades vasoactive peptides
70 f the natriuretic peptide (NP) receptors and neutral endopeptidase (NEP) in mediating and modulating
71                      The cell-surface enzyme neutral endopeptidase (NEP) inactivates both peptides.
72 e herein our efforts to identify a selective neutral endopeptidase (NEP) inhibitor as a potential tre
73                                              Neutral endopeptidase (NEP) is a cell surface enzyme fou
74                                              Neutral endopeptidase (NEP) is a cell-surface enzyme tha
75                                              Neutral endopeptidase (NEP) is a genetically distinct me
76                                              Neutral endopeptidase (NEP) is expressed on normal prost
77 as the expression of the SP-degrading enzyme neutral endopeptidase (NEP) is increased, compared to co
78  the angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP) may produce greater benefits
79 ical, and modeling approaches, we identified neutral endopeptidase (NEP) that is up-regulated in huma
80                                              Neutral endopeptidase (NEP) uses SP as a substrate to pr
81 ndrogen-sensitive LNCaP cells, which express neutral endopeptidase (NEP), but not in androgen-indepen
82 nt vasoconstrictor into its active form, and neutral endopeptidase (NEP), which is involved in termin
83 ors indicated that the previously identified neutral endopeptidase (NEP)-like activity is the major p
84 nstrated substrate preference for Ang I, was neutral endopeptidase (NEP)-like.
85  and absence of long-term oral inhibition of neutral endopeptidase (NEP).
86 kephalin, the natural substrate of the human neutral endopeptidase (NEP).
87 both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP).
88 nhibitors of the two zinc metallopeptidases, neutral endopeptidase (NEP, EC 3.4.24.11) and angiotensi
89                                              Neutral endopeptidase (NEP; CALLA, CD10, EC 3.4.24.11) i
90 ed plasma half-life due to its resistance to neutral-endopeptidase (NEP) digestion.
91 ich blocks angiotensin converting enzyme and neutral endopeptidase, on these endpoints.
92 common acute lymphoblastic leukemia antigen, neutral endopeptidase, or enkephalinase, can be used as
93 dipeptidyl carboxypeptidase (captopril), and neutral endopeptidase (phosphoramidon) dramatically incr
94                        By 28 d post wounding neutral endopeptidase staining again was detected only i
95 me required for kidney membranes or purified neutral endopeptidase to abolish ANP-dependent activatio
96                                              Neutral endopeptidase was localized by immunohistochemis
97                                 Staining for neutral endopeptidase was noted in the wound bed 6 h aft
98                                              Neutral endopeptidase was strikingly localized in normal
99 otein levels of the enzyme that degrades SP, neutral endopeptidase, were increased.
100                              Incubation with neutral endopeptidase, which degrades bombesin, or bombe
101 eptidase inhibitors inhibit ACE activity and neutral endopeptidase, which degrades natriuretic peptid
102 bits angiotensin-converting enzyme (ACE) and neutral endopeptidase, which degrades vasodilatory facto
103 at released opioids are primarily cleaved by neutral endopeptidase, with a lesser involvement of amin

 
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