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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
8 Escherichia coli encodes the metalloprotease oligopeptidase A (OpdA).
9                          We found that among oligopeptidases, a residue of the catalytic apparatus is
10 The group B streptococcal enzyme also showed oligopeptidase activity and degraded a variety of small
11 ial covalent reversible inhibitors of prolyl oligopeptidase activity.
12                    Additionally, with prolyl oligopeptidase and aminopeptidase B we identified two ne
13 opeptidase class of serine proteases, prolyl oligopeptidase and oligopeptidase B, showed that resonan
14 including DPP-4, DPP-7, DPP-8, DPP-9, prolyl oligopeptidase, and acylpeptide hydrolase.
15 e cytosol, endopeptidases, especially thimet oligopeptidase, and aminopeptidases degrade many proteas
16                                              Oligopeptidase B (OPB) is a serine peptidase with dibasi
17 the activity of a T. cruzi serine peptidase, oligopeptidase B (OPB).
18 ity followed by mass spectrometry identified oligopeptidase B (OPB; Clan SC, family S9A) as the respo
19                                              Oligopeptidase B (OpdB) is a serine peptidase broadly di
20 or OPB and provide the first structure of an oligopeptidase B at high resolution.
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
24           Our data suggest that the T. cruzi oligopeptidase B participates in processing events in th
25                        Exogenous recombinant oligopeptidase B reconstitutes the oligopeptidase B-depe
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
28                                 The T. cruzi oligopeptidase B was expressed as a fully active product
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
33 yl endopeptidase and the bacterial peptidase oligopeptidase B.
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
38                                       Thimet oligopeptidase (EC 3.4.24.15) and neurolysin (EC 3.4.24.
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
45   This mutant lacks the Dictyostelium prolyl oligopeptidase gene (dpoA).
46                                              Oligopeptidases impose a size limitation on their substr
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
50                                       Thimet oligopeptidase mutated so that neurolysin residues are a
51                                          The oligopeptidase neurolysin (EC 3.4.24.16; Nln) was first
52 tems in Arabidopsis thaliana, the organellar oligopeptidase, OOP (At5g65620).
53 P3 is induced in wild-type cells by a prolyl oligopeptidase (POase) inhibitor.
54                                       Prolyl oligopeptidase (POP) is a large 80 kDa protease, which c
55                                       Prolyl oligopeptidase (POP) is widely distributed in mammals, w
56  processing enzyme is a member of the prolyl oligopeptidase (POP) subfamily of proteases (EC 3.4.21.2
57 es, each containing a gene encoding a prolyl oligopeptidase (POP).
58 tides, similar to the closely related prolyl oligopeptidase (POP).
59                                       Prolyl oligopeptidase (PREP) accelerates the aggregation of alp
60                                       Prolyl oligopeptidase (PREP) can accelerate the aSyn aggregatio
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
63 idases (DPPs) DPPIV, DPP9, DPPII, and prolyl oligopeptidase (PREP).
64              The intracellular enzyme prolyl oligopeptidase probably degrades tasidotin to P5.
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
67                         Inhibitors of prolyl oligopeptidase reverse the effects of all three drugs on
68 n neurolysin switch hydrolysis to the thimet oligopeptidase site.
69                         Therefore, cytosolic oligopeptidases such as TPPII normalize rates of intrace
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
74                                       Thimet oligopeptidase (TOP) is a zinc metallopeptidase that met
75               One such endopeptidase, thimet oligopeptidase (TOP), which was recently shown to degrad
76 igest matched the protein sequence of thimet oligopeptidase (TOP).
77 degraded by the metalloendopeptidase, thimet oligopeptidase (TOP).
78                   We demonstrate that thimet oligopeptidases (TOPs) constitute a class of SA-binding
79                         We show that a large oligopeptidase, tripeptidylpeptidase II (TPPII), can com
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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