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1 idase IV, dipeptidyl peptidase 9, and prolyl oligopeptidase.
2 they are predicted to be cleaved by a prolyl oligopeptidase.
3 than the analogous Y473F mutation of prolyl oligopeptidase.
4 , act separately from SPP as a novel stromal oligopeptidase.
5 ability of peptidase IImes to act also as an oligopeptidase.
6 acts and synthetic peptides, an enzyme named oligopeptidase 1 (OLP1) was found that catalyzes the cle
7 es dipeptidyl peptidase 3 (DPP-3) and thimet oligopeptidase 1 (TOP-1), both of which are present in n
10 The group B streptococcal enzyme also showed oligopeptidase activity and degraded a variety of small
13 opeptidase class of serine proteases, prolyl oligopeptidase and oligopeptidase B, showed that resonan
15 e cytosol, endopeptidases, especially thimet oligopeptidase, and aminopeptidases degrade many proteas
18 ity followed by mass spectrometry identified oligopeptidase B (OPB; Clan SC, family S9A) as the respo
21 85-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes.
22 work implicated the T.cruzi serine hydrolase oligopeptidase B in the generation of Ca2+-signaling act
23 n defect is associated with the inability of oligopeptidase B null mutant trypomastigotes to mobilize
26 id t-butoxycarbonyl-(D)Val-Leu-(L)boroArg to oligopeptidase B resulted in potent, slow binding inhibi
27 e we show that deletion of the gene encoding oligopeptidase B results in a marked defect in host cell
29 serine proteases, prolyl oligopeptidase and oligopeptidase B, showed that resonances corresponding t
30 he H652A and H652Q active center variants of oligopeptidase B, there are two resonances observed in t
31 evealed a novel enzyme, denominated T. cruzi oligopeptidase B, which is homologous to members of the
32 combinant oligopeptidase B reconstitutes the oligopeptidase B-dependent Ca2+ signaling activity in nu
34 de chain to form the oxyanion hole is prolyl oligopeptidase, but the Y44F mutation of cocE has a more
35 ies between the active centers of the prolyl oligopeptidase class of serine proteases and the pancrea
36 on NMR spectra for two members of the prolyl oligopeptidase class of serine proteases, prolyl oligope
37 e-substituted dirhodium catalyst to a prolyl oligopeptidase containing a genetically encoded L-4-azid
39 ls overexpressing mouse neurolysin or thimet oligopeptidase (EC 3.4.24.15), a closely related metallo
40 peptidase IV (DP-IV), a member of the prolyl oligopeptidase family of peptidases, is involved in the
41 which is homologous to members of the prolyl oligopeptidase family of serine hydrolases, known to par
42 triad residues characteristic of the prolyl oligopeptidase family of serine proteinases (Ser-Asp-His
43 d sequence showed 66.4% identity to the PepF oligopeptidase from Lactococcus lactis, a member of the
44 structure of a hexameric serine protease, an oligopeptidase from Pyrococcus horikoshii (PhAAP), revea
47 II-(1-7) or bradykinin(1-5), and the prolyl oligopeptidase inhibitor Fmoc-Ala-Pyr-CN (IC(50) = 50 nm
48 -KO mice were treated with S-17092, a prolyl-oligopeptidase inhibitor that inhibits the formation of
49 s, we have reported covalent bicyclic prolyl oligopeptidase inhibitors that were highly selective for
56 processing enzyme is a member of the prolyl oligopeptidase (POP) subfamily of proteases (EC 3.4.21.2
61 exert toxic effects on neurons, while prolyl oligopeptidase (PREP) has been shown to interact with aS
62 shares exopeptidase specificity, and prolyl oligopeptidase (PREP), with which it shares endopeptidas
65 expression of leucine aminopeptidase, thymet oligopeptidase, puromycin-sensitive aminopeptidase, and
66 His-495/Asn-496, and Arg-498/Thr-499; thimet oligopeptidase residues listed first) in their substrate
70 that proteases, such as the trypanopains and oligopeptidases that are released by trypanosomes, could
71 er one of the two sites is mutated in thimet oligopeptidase, then the enzyme cleaves almost equally a
72 rolylprolinal (BCPP), an inhibitor of prolyl oligopeptidase, there was a 30-fold increase in the IC(5
73 bitor of the cytosolic endopeptidase, thimet oligopeptidase (TOP) (EC ), whose physiological function
80 ent aggregation, and we found that different oligopeptidases use different strategies to achieve such
81 e ITC-ERM approach to another enzyme (prolyl oligopeptidase), we unexpectedly discovered non-Michaeli
82 y deletion of the gene that codes for prolyl oligopeptidase, which also regulates inositol metabolism
83 quences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identi
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