戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 (endothelin-converting enzyme) 1, and ANPEP (aminopeptidase N).
2 ding to the 120 kDa Cry1Ac putative receptor aminopeptidase N.
3 ts strongly indicate that mouse p161 is CD13/aminopeptidase N.
4 t p161 is homologous with rat and human CD13/aminopeptidase N.
5  transmigration via induction of endothelial aminopeptidase N.
6 t of aminopeptidase N that is conserved with aminopeptidase Ns.
7                       The apical PM proteins aminopeptidase N, 5'nucleotidase, and the polymeric IgA
8 NMR molecular probe for in vivo detection of aminopeptidase N activity.
9 lar characterization of an Anopheles gambiae aminopeptidase N (AgAPN1) as the predominant jacalin tar
10  activity (64.5 +/- 3.5% of control) but not aminopeptidase N, aminopeptidase P, and 5'-nucleotidase
11        The midgut-specific anopheline alanyl aminopeptidase N (AnAPN1) is highly conserved across Ano
12 ide GNGRAHA, a ligand of the surface protein aminopeptidase N and of integrin alphavbeta3.
13 to trans-regulate differential expression of aminopeptidase N and other midgut genes in an insect hos
14    The viruses used the human entry receptor aminopeptidase N and replicated in human hepatoma cells,
15 ch as alpha(v)beta3/alpha(v)beta5 integrins, aminopeptidase N, and aminopeptidase A.
16 t Phe(3) is a key residue for neprilysin and aminopeptidase N (AP-N) ectoenkephalinase inhibition.
17  angiotensin-I-converting enzyme (ACE I) and aminopeptidase N (AP-N).
18 ced the levels of the AngIV-degrading enzyme aminopeptidase N (AP-N).
19                           Tumor cell surface aminopeptidase N (APN or CD13) has two puzzling function
20 activity of specific neuropeptidases, namely aminopeptidase N (APN) and neutral endopeptidase 24.11 (
21   Mouse Dmp1 has been shown to activate CD13/aminopeptidase N (APN) and p19ARF gene expression via bi
22             Here we identify membrane alanyl aminopeptidase N (APN) as a receptor for pea enation mos
23 nsmissible gastroenteritis virus (TGEV), use aminopeptidase N (APN) as their cellular receptors.
24 bound purified gypsy moth (Lymantria dispar) aminopeptidase N (APN) biphasically.
25   It has been known that CCoV-HuPn-2018 uses aminopeptidase N (APN) from canines, felines, and porcin
26 ation in the Drosophila homolog of the human aminopeptidase N (APN) gene.
27 which belong to the group 1 coronavirus, use aminopeptidase N (APN) of their natural host and feline
28 2018 spike binds canine, feline, and porcine aminopeptidase N (APN) orthologs, which serve as entry r
29                                    Mammalian aminopeptidase N (APN) plays multifunctional roles in ma
30   Further binding assays were performed with aminopeptidase N (APN) purified from L. dispar and M. se
31  and we show that inhibition of cell surface aminopeptidase N (APN) using actinonin, bestatin, or inh
32                          Recently, a 100-kDa aminopeptidase N (APN) was isolated from brush border me
33 ctase-phlorizin hydrolase (LPH), and neutral Aminopeptidase N (ApN) were analyzed in duodenal and col
34                                              Aminopeptidase N (APN), a 150-kDa metalloprotease also c
35 of this family that has been well studied is aminopeptidase N (APN), a multifunctional protease known
36                                    A 106-kDa aminopeptidase N (APN), called AgAPN2, was previously id
37                  A nonspecific exopeptidase, aminopeptidase N (APN), is inhibited sequence-specifical
38                              We also analyze aminopeptidase N (APN), the receptor for the human coron
39 tosis of the single-spanning apical resident aminopeptidase N (APN).
40                                              Aminopeptidase N (APN, CD13) is a transmembrane ectopept
41                                              Aminopeptidase N (APN, CD13; EC 3.4.11.2) is a transmemb
42 ptidases, neprilysin (NEP, EC 3.4.24.11) and aminopeptidase N (APN, EC 3.4.11.2).
43                                              Aminopeptidase N (APN/CD13) is a zinc-dependent M1 amino
44                                              Aminopeptidase N (APN; also called CD13) is a cellular r
45 for the NGR peptides in tumor vasculature is aminopeptidase N (APN; also called CD13).
46                          The metalloprotease aminopeptidase N (APN; CD13) is often overexpressed in t
47  of natural promoters revealed that the CD13/aminopeptidase N (APN; EC 3.4.11.2) promoter could bind
48 d with differential alteration of two midgut aminopeptidases N, APN1 and APN6, conferred by a trans-r
49                          Lepidopteran midgut aminopeptidases N (APNs) are phylogenetically divided in
50 nsin-converting enzyme; aminopeptidase A and aminopeptidase n; at(1); and at(2) receptors were shown
51  both mAbs competitively interfere with host aminopeptidase N binding to neutralize PDCoV and used de
52    ATP-binding cassette transporter (ABCC4), aminopeptidase-N, cadherin, and cathepsin-B were previou
53 cificity of human, pig, and rat orthologs of aminopeptidase N (CD13), a highly conserved cell surface
54 ibitors tested, or by a mAb directed against aminopeptidase N (CD13).
55                                         CD13/aminopeptidase N (CD13/APN) is a potent regulator of ang
56                                     The CD13/aminopeptidase N (CD13/APN) metalloprotease is an import
57               The Ets-1- and c-Myb-dependent aminopeptidase N (CD13/APN) promoter and an Ets-1-depend
58 ular adhesion molecule 1 (ICAM-1), anti-LG3, aminopeptidase N, CXCL9, endothelin-1, and gelsolin.
59     We have recently demonstrated that CD13 (aminopeptidase N) expressed by nonmalignant host cells o
60                                        CD13 (aminopeptidase N) expression in pericytes was determined
61 t viral entry factors ACE2 (for SARS-CoV-2), aminopeptidase N (for 229E), and glycosaminoglycans (for
62                                              Aminopeptidase N from Escherichia coli is a M1 class ami
63             PEDV recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor
64       Human coronavirus HCoV-229E uses human aminopeptidase N (hAPN) as its receptor.
65 es of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomic
66 d to purified, soluble virus receptor, human aminopeptidase N (hAPN).
67                                        Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane prot
68 lasma membrane proteins, 5'-nucleotidase and aminopeptidase N in lysosomal vacuoles.
69 EMV binds to a heavily glycosylated receptor aminopeptidase N in the pea aphid gut and is transcytose
70 the aminopeptidase A inhibitor, EC33, or the aminopeptidase N inhibitor, PC18.
71                                         CD13/aminopeptidase N is a negative regulator of mast cell ac
72                                         CD13/aminopeptidase N is a transmembrane peptidase that is in
73 iensis Cry1Ac toxin to the putative receptor aminopeptidase N is specifically inhibited by N-acetylga
74 we found the receptor for HCoV-229E (CD13 or aminopeptidase N) localized mainly to the apical surface
75         We show that FCoV-23 can use several aminopeptidase N orthologues as receptors and reveal the
76 r with the lack of receptor functionality of aminopeptidase N proteins might account for some of the
77 eprilysin, angiotensin-converting enzyme, or aminopeptidase N, respectively.
78 tomegalovirus (CMV) infection by human CD13 (aminopeptidase N)-specific antibodies were studied.
79  against partially purified mouse intestinal aminopeptidase N specifically blocked the binding of K-1
80                                In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sod
81 d hydrophobic character for the S1 pocket of aminopeptidase N that is conserved with aminopeptidase N
82 nding to the endothelial cell surface enzyme aminopeptidase N, the inert matrix transformed into an a
83 s residue methionine 260 in Escherichia coli aminopeptidase N were characterized.
84 f a receptor protein in the aphid gut called aminopeptidase N, which is responsible for entry of the