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1 imited to the enamel organ, we have named it enamelysin.
2 rts current ideas concerning the function of enamelysin.
4 re the appearances of mRNA of the proteases, enamelysin and kallikrein-4) on days 0 and 1, persisted
5 fied the catalytic domain of recombinant pig enamelysin, and expressed a recombinant form of the majo
10 characterize the in vivo biological role of enamelysin during tooth development, we generated an ena
14 oping enamel matrix, and the precise role of enamelysin in the processing of enamel proteins is unkno
19 opment, matrix metalloproteinase-20 (MMP-20, enamelysin) is expressed early during the secretory stag
21 the potential role of the metalloproteinase enamelysin (MMP-20) in controlling some of the most crit
23 BN), amelotin (AMTN), tumor-related proteins enamelysin (MMP-20), kallikrein-4 (KLK-4), and odontogen
24 and mutations in the kallikrein 4 (KLK4) and enamelysin (MMP20) genes cause autosomal-recessive amelo
26 view we suggest that the tooth-specific MMP, enamelysin (MMP20), facilitates ameloblast movements dur
28 the mutation have no apparent phenotype, the enamelysin null mouse has a severe and profound tooth ph
29 secreted proteins amelogenin, enamelin, and enamelysin result in visibly, structurally, or mechanica
31 lysis by matrix metalloproteinase 20 (MMP20, enamelysin) soon after secretion, the present study was
32 study was aimed to assess the selectivity of enamelysin to the three most abundant cleavage sites on
34 support of this interpretation, recombinant enamelysin was previously demonstrated to cleave recombi
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