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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.
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
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,
16 t Phe(3) is a key residue for neprilysin and aminopeptidase N (AP-N) ectoenkephalinase inhibition.
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
25 It has been known that CCoV-HuPn-2018 uses aminopeptidase N (APN) from canines, felines, and porcin
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
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
33 ctase-phlorizin hydrolase (LPH), and neutral Aminopeptidase N (ApN) were analyzed in duodenal and col
35 of this family that has been well studied is aminopeptidase N (APN), a multifunctional protease known
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
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
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
61 t viral entry factors ACE2 (for SARS-CoV-2), aminopeptidase N (for 229E), and glycosaminoglycans (for
65 es of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomic
69 EMV binds to a heavily glycosylated receptor aminopeptidase N in the pea aphid gut and is transcytose
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
76 r with the lack of receptor functionality of aminopeptidase N proteins might account for some of the
79 against partially purified mouse intestinal aminopeptidase N specifically blocked the binding of K-1
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
84 f a receptor protein in the aphid gut called aminopeptidase N, which is responsible for entry of the