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1 imited to the enamel organ, we have named it enamelysin.
2 rts current ideas concerning the function of enamelysin.
3                Our findings demonstrate that enamelysin activity is essential for proper enamel devel
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
6        We tested the hypothesis that MMP-20 (enamelysin) catalyzes the cleavages that generate secret
7  isolation and characterization of the mouse enamelysin cDNA.
8 in during tooth development, we generated an enamelysin-deficient mouse by gene targeting.
9                    Characterization of mouse enamelysin demonstrated that it is highly conserved in b
10  characterize the in vivo biological role of enamelysin during tooth development, we generated an ena
11 ptides, indicating comparable selectivity of enamelysin for these peptide bonds.
12                                    The mouse enamelysin gene (Mmp20) is made up of 10 exons spanning
13         Matrix metalloproteinase-20 (MMP-20, enamelysin) has a highly restricted pattern of expressio
14 oping enamel matrix, and the precise role of enamelysin in the processing of enamel proteins is unkno
15                                              Enamelysin is a recently isolated member of the matrix m
16                                              Enamelysin is a tooth-specific matrix metalloproteinase
17                                        Thus, enamelysin is likely an important amelogenin-processing
18                              We propose that enamelysin is the predominant proteinase that processes
19 opment, matrix metalloproteinase-20 (MMP-20, enamelysin) is expressed early during the secretory stag
20 e developmental time period, suggesting that enamelysin may play a role in their hydrolysis.
21  the potential role of the metalloproteinase enamelysin (MMP-20) in controlling some of the most crit
22                                              Enamelysin (MMP-20) is a tooth-specific matrix metallopr
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
25                                        Mouse enamelysin (Mmp20), a member of the matrix metalloprotei
26 view we suggest that the tooth-specific MMP, enamelysin (MMP20), facilitates ameloblast movements dur
27                 Matrix metalloproteinase-20 (enamelysin, MMP20) is essential for dental enamel develo
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
30 n kidney 293F cells, and recombinant porcine enamelysin (rpMMP-20) was expressed in bacteria.
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
33                          Expression of mouse enamelysin was detectable only in ameloblasts and odonto
34  support of this interpretation, recombinant enamelysin was previously demonstrated to cleave recombi

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