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1 equence homology to genes encoding mammalian metalloendopeptidases.
2 s (ADAM-TS) describes a novel family of zinc metalloendopeptidases.
3 hat shows sequence homology with a family of metalloendopeptidases.
4 and beta subunits of meprins, mammalian zinc metalloendopeptidases, are extensively glycosylated; app
5 IQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for
7 HRH1-5-like peptide and its cleavage enzyme, metalloendopeptidase E.C.3.4.24.15 (EP24.15), which clea
9 stigated the functional relationship between metalloendopeptidase EC 3.4.24.15 (MP24.15) and the amyl
11 Insulin-degrading enzyme (IDE), a 110-kDa metalloendopeptidase, hydrolyzes several physiologically
12 transcribed pepO gene, which encodes a zinc metalloendopeptidase, indicated that their promoter and
13 tallography and used as models for mammalian metalloendopeptidases, indicates conserved residues.
14 stead, it had a large domain homologous to a metalloendopeptidase isolated from crayfish, an epiderma
21 proteinase (APR), a member of the metzincin metalloendopeptidase superfamily, and an 11.4-kDa alkali
22 cessing peptidase (SPP) of chloroplasts is a metalloendopeptidase that cleaves in vitro a broad range
24 from insulin-degrading enzyme (IDE), a thiol metalloendopeptidase that degrades small peptides such a
25 dopeptidase EC 3.4.24.15 (EP24.15) is a zinc metalloendopeptidase that is broadly distributed within
27 highly regulated, secreted, and cell-surface metalloendopeptidases that are abundantly expressed in t
28 meric, glycosylated cell surface or secreted metalloendopeptidases that are composed of multidomain d
29 ecreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue
31 einase inhibitor, but not with inhibitors of metalloendopeptidases (thiorphan and phosphoramidon), se
32 antibodies raised to the 70 kDa human matrix metalloendopeptidase, type III procollagen N-proteinase.
34 related proteins, we show that for metzincin metalloendopeptidase, which has a broad spectrum of subs
35 ignaling at the cell surface is regulated by metalloendopeptidases, which degrade peptides in the ext
36 guis PepO is a member of the M13 category of metalloendopeptidases, which includes NEP and endothelin
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