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1 on trypsinogen activation catalyzed by human enteropeptidase.
2 fic substrate for human, but not for bovine, enteropeptidase.
3                                              Enteropeptidase, a type II transmembrane protein of the
4 ther, metformin-treated mice exhibit reduced enteropeptidase activity, reduced trypsin activity, and
5 strointestinal tissue with metformin reduces enteropeptidase activity; further, metformin-treated mic
6                                              Enteropeptidase, also known as enterokinase, initiates t
7 port that metformin inhibits the activity of enteropeptidase and other digestive enzymes at drug conc
8                                         Thus enteropeptidase appears to have at least three distinct
9 e solved the crystal structure of the bovine enteropeptidase catalytic domain to 2.3 A resolution in
10                            In this location, enteropeptidase cleaves and activates trypsinogen, there
11  as a single-chain protein, whereas purified enteropeptidase contains a approximately 47-kDa serine p
12      These results suggest apical sorting of enteropeptidase depends on N-linked glycosylation of the
13 contrast to many apically targeted proteins, enteropeptidase does not form detergent-resistant associ
14 inogen was activated efficiently by purified enteropeptidase from bovine intestine (Km = 5.6 microM a
15         These kinetic data indicate that the enteropeptidase heavy chain has little influence on the
16          Despite this, it remains unclear if enteropeptidase inhibition affects EECs function.
17 estern style diet (WSD) supplemented with an enteropeptidase inhibitor (WSD-ETPi), analyzed the expre
18                                              Enteropeptidase inhibitors block host protein digestion
19                                              Enteropeptidase is a heterodimeric type II membrane prot
20                                              Enteropeptidase is a membrane-bound serine protease that
21                                              Enteropeptidase is synthesized as a single-chain protein
22 ty of two unrelated proteases, caspase-3 and enteropeptidase (or enterokinase).
23 light chain (pro-HL-BEK (where BEK is bovine enteropeptidase)) or only the catalytic domain (pro-L-BE
24  Asp(19-22) motif per se is not required for enteropeptidase recognition, whereas it is essential for
25         Treatment of conditioned medium with enteropeptidase reduced the apparent molecular mass of t
26          Thus, a unique basic exosite on the enteropeptidase surface has evolved to facilitate the cl
27 dic motif as a specific recognition site for enteropeptidase, the physiological activator of trypsino
28                           Recombinant bovine enteropeptidase was sorted directly to the apical surfac
29                                              Enteropeptidase was unexpectedly promiscuous, but exhibi
30 ed mRNA encoding PAR(2), trypsinogen IV, and enteropeptidase, which activates the zymogen.