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1 o acids with the corresponding residues from fibroblast collagenase.
2 zymes containing domains of gelatinase B and fibroblast collagenase.
3 ilarity to the metal-binding domain of human fibroblast collagenase.
5 y migrate in a dose-dependent manner to both fibroblast collagenase and to type I collagen degradatio
9 o understand the role of the hinge region of fibroblast collagenase in its collagenolytic activity, w
10 icating that the presence of this residue in fibroblast collagenase is particularly important for the
11 e fibronectin-like domain of gelatinase B to fibroblast collagenase is sufficient to endow the enzyme
13 r 16 with IC50 = 20.5 nM and 24.4 nM against fibroblast collagenase (MMP-1) and stromelysin (MMP-3),
14 h the use of the catalytic fragment of human fibroblast collagenase (MMP-1) as a target protein and t
15 structure of the catalytic fragment of human fibroblast collagenase (MMP-1) complexed with a sulfonam
16 an example, the catalytic fragment of human fibroblast collagenase (MMP-1) was used to follow the ef
17 ture of a complex of the catalytic domain of fibroblast collagenase (MMP-1) with the N-terminal inhib
18 e inhibitor-free catalytic fragment of human fibroblast collagenase (MMP-1), a protein of 18.7 kDa, w
19 stitial collagenases (MMP-13), but not human fibroblast collagenase (MMP-1), cleave type I collagen a
21 the effects of type I collagen fragments and fibroblast collagenase on PDL cell migration, since PDL
22 ubated with the N-terminal fragment of human fibroblast collagenase prior to the addition of ANS, the
24 ed variable expression of 72 kDa gelatinase, fibroblast collagenase, stromelysin, tissue inhibitor of
25 arbon-carbon double bond) complexes of human fibroblast collagenase to obtain insights into the struc
26 catalytic zinc-binding active site region of fibroblast collagenase with that of gelatinase B increas
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