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1 nin precursor 1, and down-regulated membrane metalloendopeptidase.
2 equence homology to genes encoding mammalian metalloendopeptidases.
3 s (ADAM-TS) describes a novel family of zinc metalloendopeptidases.
4 hat shows sequence homology with a family of metalloendopeptidases.
5 and beta subunits of meprins, mammalian zinc metalloendopeptidases, are extensively glycosylated; app
6 IQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for
7                           The zinc-dependent metalloendopeptidase CpaA is a predominant substrate of
8                        Although cell surface metalloendopeptidases degrade neuropeptides in the extra
9 HRH1-5-like peptide and its cleavage enzyme, metalloendopeptidase E.C.3.4.24.15 (EP24.15), which clea
10                                          The metalloendopeptidase EC (EP24.15) is a neuropeptide-meta
11 stigated the functional relationship between metalloendopeptidase EC 3.4.24.15 (MP24.15) and the amyl
12                                  Meprins are metalloendopeptidases expressed by leukocytes in the lam
13    Insulin-degrading enzyme (IDE), a 110-kDa metalloendopeptidase, hydrolyzes several physiologically
14  transcribed pepO gene, which encodes a zinc metalloendopeptidase, indicated that their promoter and
15 tallography and used as models for mammalian metalloendopeptidases, indicates conserved residues.
16 stead, it had a large domain homologous to a metalloendopeptidase isolated from crayfish, an epiderma
17 ission of the precursor p72Plk3 at Arg354 by metalloendopeptidase nardilysin (NRDC), and the resultin
18  site might be the membrane-bound variant of metalloendopeptidase neurolysin (EC 3.4.24.16).
19 l to N-arginine dibasic convertase (NRDc), a metalloendopeptidase of the M16 family.
20 opeptidase (EC 3.4.24.15), a closely related metalloendopeptidase of the same family.
21                                              Metalloendopeptidases of the astacin family contain a ho
22                                     Meprins, metalloendopeptidases of the astacin family, are compose
23 tress response mediated by the mitochondrial metalloendopeptidase OMA1.
24                              ECE-1 is a zinc metalloendopeptidase related in amino acid sequence to n
25  proteinase (APR), a member of the metzincin metalloendopeptidase superfamily, and an 11.4-kDa alkali
26 cessing peptidase (SPP) of chloroplasts is a metalloendopeptidase that cleaves in vitro a broad range
27 on, cortical granules exocytose ovastacin, a metalloendopeptidase that cleaves ZP2 in the zona pelluc
28                Neprilysin is a transmembrane metalloendopeptidase that degrades neuropeptides that ar
29 from insulin-degrading enzyme (IDE), a thiol metalloendopeptidase that degrades small peptides such a
30 dopeptidase EC 3.4.24.15 (EP24.15) is a zinc metalloendopeptidase that is broadly distributed within
31            The Kell blood group protein is a metalloendopeptidase that preferentially cleaves a Trp(2
32 highly regulated, secreted, and cell-surface metalloendopeptidases that are abundantly expressed in t
33 meric, glycosylated cell surface or secreted metalloendopeptidases that are composed of multidomain d
34 ecreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue
35  most antigenic peptides are degraded by the metalloendopeptidase, thimet oligopeptidase (TOP).
36 einase inhibitor, but not with inhibitors of metalloendopeptidases (thiorphan and phosphoramidon), se
37 antibodies raised to the 70 kDa human matrix metalloendopeptidase, type III procollagen N-proteinase.
38 e belongs to the M4 family of bacterial zinc metalloendopeptidases, typified by thermolysin.
39 related proteins, we show that for metzincin metalloendopeptidase, which has a broad spectrum of subs
40 ignaling at the cell surface is regulated by metalloendopeptidases, which degrade peptides in the ext
41 guis PepO is a member of the M13 category of metalloendopeptidases, which includes NEP and endothelin
42                   Meprins are mammalian zinc metalloendopeptidases with protease domains structurally